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  • 301.
    Pettersson, Jean
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University.
    Procedure for the determination of n-octanol/water partition of boron-organic compounds1999In: ICP Information Newsletter, Vol. 25, p. 183-186Article in journal (Refereed)
  • 302.
    Pettersson, Mattias
    et al.
    Umea Univ, Dept Odontol, Prosthet Dent, Fac Med, Umea, Sweden.
    Pettersson, Jean
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Johansson, Anders
    Umea Univ, Dept Odontol, Mol Periodontol, Fac Med, Umea, Sweden.
    Molin Thorén, Margareta
    Umea Univ, Dept Odontol, Prosthet Dent, Fac Med, Umea, Sweden.
    Titanium release in peri-implantitis2019In: Journal of Oral Rehabilitation, ISSN 0305-182X, E-ISSN 1365-2842, Vol. 46, no 2, p. 179-188Article in journal (Refereed)
    Abstract [en]

    Objectives: The aim of this study was to investigate the titanium (Ti) content of biopsies from patients with severe peri-implantitis or controls without Ti exposure.

    Background: Peri-implantitis is considered to be an infectious disease, but recent studies have shown that Ti can aggravate inflammation in combination with bacterial products. The Ti content of peri-implantitis and periodontitis (controls) tissue is unknown.

    Methods: Thirteen patients referred for peri-implantitis and eleven for periodontitis treatment were included in the study. Disease severity was obtained from dental records. Biopsies were taken from both groups and chemically analysed with inductively coupled plasma mass spectrometry for Ti content. Additionally, two patients with peri-implantitis and two with periodontitis were recruited and their biopsies were analysed microscopically with light microscopy, transmission electron microscopy and scanning electron microscopy with element analysis to investigate the presence of particulate Ti.

    Results: All patients lost one or more implants despite undergoing peri-implant or treatment. Peri-implantitis tissue contained significantly higher concentrations of Ti than control samples with a mean +/- SD of 98.7 +/- 85.6 and 1.2 +/- 0.9 mu g/g, respectively. Particulate metal was identified in peri-implantitis and control biopsies, but element analyses could confirm only the presence of Ti in peri-implantitis tissue.

    Conclusion: We showed that high contents of particulate and submicron Ti were present in peri-implantitis tissue. These high Ti contents in peri-implant mucosa can potentially aggravate inflammation, which might reduce the prognosis of treatment interventions.

  • 303.
    Pettersson, Mattias
    et al.
    Umea Univ, Prosthet Dent, Umea, Sweden.
    Pettersson, Jean
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Thoren, Margareta Molin
    Umea Univ, Prosthet Dent, Umea, Sweden.
    Johansson, Anders
    Umea Univ, Fac Med, Dept Odontol, Mol Periodontol, Umea, Sweden.
    Effect of cobalt ions on the interaction between macrophages and titanium2018In: Journal of Biomedical Materials Research. Part A, ISSN 1549-3296, E-ISSN 1552-4965, Vol. 106, no 9, p. 2518-2530Article in journal (Refereed)
    Abstract [en]

    Inflammation and bone reduction around dental implants are described as peri-implantitis and can be caused by an inflammatory response against bacterial products and toxins. Titanium (Ti) forms aggregates with serum proteins, which activate and cause release of the cytokine interleukin (IL-1) from human macrophages. It was hypothesized that cobalt (Co) ions can interact in the formation of pro-inflammatory aggregates, formed by titanium. To test this hypothesis, we differentiated THP-1 cells into macrophages and exposed them to Ti ions alone or in combination with Co ions to investigate if IL-1 release and cytotoxicity were affected. We also investigated aggregate formation, cell uptake and human biopsies with inductively coupled plasma atomic emission spectroscopy and electron microscopy. Co at a concentration of 100 mu M neutralized the IL-1 release from human macrophages and affected the aggregate formation. The aggregates formed by Ti could be detected in the cytosol of macrophages. In the presence of Co, the Ti-induced aggregates were located in the cytosol of the cultured macrophages, but outside the lysosomal structures. It is concluded that Co can neutralize the Ti-induced activation and release of active IL-1 from human macrophages in vitro. Also, serum proteins are needed for the formation of metal-protein aggregates in cell medium. Furthermore, the structures of the aggregates as well as the localisation after cellular uptake differ if Co is present in a Ti solution. Phagocytized aggregates with a similar appearance seen in vitro with Ti present, were also visible in a sample from human peri-implant tissue.

  • 304.
    Qaisar, Rizwan
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Clinical Neurophysiology.
    Renaud, Guillaume
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Clinical Neurophysiology.
    Hedström, Yvette
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Clinical Neurophysiology.
    Pollanen, Eija
    Ronkainen, Paula
    Kaprio, Jaakko
    Alen, Markku
    Sipila, Sarianna
    Artemenko, Konstantin
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Kovanen, Vuokko
    Larsson, Lars
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Clinical Neurophysiology.
    Hormone replacement therapy improves contractile function and myonuclear organization of single muscle fibres from postmenopausal monozygotic female twin pairs2013In: Journal of Physiology, ISSN 0022-3751, E-ISSN 1469-7793, Vol. 591, no 9, p. 2333-2344Article in journal (Refereed)
    Abstract [en]

    Ageing is associated with a decline in muscle mass and strength leading to increased physical dependency in old age. Postmenopausal women experience a greater decline than men of similar age in parallel with the decrease in female sex steroid hormone production. We recruited six monozygous female twin pairs (5559 years old) where only one twin pair was on hormone replacement therapy (HRT use = 7.8 +/- 4.3 years) to investigate the association of HRT with the cytoplasmic volume supported by individual myonuclei (myonuclear domain (MND) size,) together with specific force at the single fibre level. HRT use was associated with a significantly smaller (approximate to 27%; P < 0.05) mean MND size in muscle fibres expressing the type I but not the IIa myosin heavy chain (MyHC) isoform. In comparison to non-users, higher specific force was recorded in HRT users both in muscle fibres expressing type I (approximate to 27%; P < 0.05) and type IIa (approximate to 23%; P < 0.05) MyHC isoforms. These differences were fibre-type dependent, i.e. the higher specific force in fast-twitch muscle fibres was primarily caused by higher force per cross-bridge while slow-twitch fibres relied on both a higher number and force per cross-bridge. HRT use had no effect on fibre cross-sectional area (CSA), velocity of unloaded shortening (V0) and relative proportion of MyHC isoforms. In conclusion, HRT appears to have significant positive effects on both regulation of muscle contraction and myonuclei organization in postmenopausal women.

  • 305.
    Qi, Xiaoying
    et al.
    Binzhou Med Univ, Med & Pharm Res Ctr, Yantai, Peoples R China.
    Zhang, Yunyun
    Yantai Zestern Biotech Co LTD, Yantai, Peoples R China.
    Zhang, Yuan
    Binzhou Med Univ, Med & Pharm Res Ctr, Yantai, Peoples R China.
    Ni, Tianhui
    Binzhou Med Univ, Precis Med Res Ctr, Yantai, Shandong, Peoples R China.
    Zhang, Wenfeng
    Yantai Zestern Biotech Co LTD, Yantai, Peoples R China.
    Yang, Chunhua
    Binzhou Med Univ, Med & Pharm Res Ctr, Yantai, Peoples R China.
    Mi, Jia
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Binzhou Med Univ, Med & Pharm Res Ctr, Yantai, Peoples R China.
    Zhang, Jiandi
    Yantai Zestern Biotech Co LTD, Yantai, Peoples R China;Binzhou Med Univ, Precis Med Res Ctr, Yantai, Shandong, Peoples R China.
    Tian, Geng
    Binzhou Med Univ, Med & Pharm Res Ctr, Yantai, Peoples R China.
    High Throughput, Absolute Determination of the Content of a Selected Protein at Tissue Levels Using Quantitative Dot Blot Analysis (QDB)2018In: Journal of Visualized Experiments, ISSN 1940-087X, E-ISSN 1940-087X, no 138, article id e56885Article in journal (Refereed)
    Abstract [en]

    Lacking a convenient, quantitative, high throughput immunoblot method for absolute determination of the content of a specific protein at cellular and tissue level significantly hampers the progress in proteomic research. Results derived from currently available immunoblot techniques are also relative, preventing any efforts to combine independent studies with a large-scale analysis of protein samples. In this study, we demonstrate the process of quantitative dot blot analysis (QDB) to achieve absolute quantification in a high throughput format. Using a commercially available protein standard, we are able to determine the absolute content of capping actin protein, gelsolin-like (CAPG) in protein samples prepared from three different mouse tissues (kidney, spleen, and prostate) together with a detailed explanation of the experimental details. We propose the QDB analysis as a convenient, quantitative, high throughput immunoblot method of absolute quantification of individual proteins at the cellular and tissue level. This method will substantially aid biomarker validation and pathway verification in various areas of biological and biomedical research.

  • 306.
    Ramström, Margareta
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Palmblad, Magnus
    Jonfysik. Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Ion Physics. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Analytical Chemistry.
    Markides, Karin E
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Håkansson, Per
    Jonfysik. Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Ion Physics. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Analytical Chemistry.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Protein identification in cerebrospinal fluid using packed capillary liquid chromatography Fourier transform ion cyclotron resonance mass spectrometry2003In: Proteomics, Vol. 3, no 2, p. 184-190Article in journal (Refereed)
    Abstract [en]

    The identification and characterization of proteins in complex biological samples such as body fluids, require powerful and reliable tools. Mass spectrometry is today one of the most important methods in such research. This paper reports on the results from the first experiment where a tryptic digest of cerebrospinal fluid was analyzed applying reversed phase liquid chromatography coupled on-line to a 9.4 T Fourier transform ion cyclotron resonance mass spectrometer. In total, 70 204 peaks were detected, which originated from 16 296 isotopic clusters corresponding to 6551 unique peptide masses. From these masses, 39 proteins were identified in the sample. The amount of sample required for one experiment corresponds to 32 μL of cerebrospinal fluid.

  • 307.
    Recknagel, Constantin
    et al.
    Leibniz Inst Balt Sea Res Warnemuende, Dept Marine Chem, Seestr 15, D-18119 Rostock, Germany.
    Thelin, Pernilla
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Abraham, Marion
    Leibniz Inst Balt Sea Res Warnemuende, Dept Marine Chem, Seestr 15, D-18119 Rostock, Germany.
    Schulz-Bull, Detlef
    Leibniz Inst Balt Sea Res Warnemuende, Dept Marine Chem, Seestr 15, D-18119 Rostock, Germany.
    Sjöberg, Per J. R.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Using standard additions to improve extraction and quantification of inositol hexakisphosphate in sediment samples by ion chromatography electrospray ionization mass spectrometry2018In: Talanta: The International Journal of Pure and Applied Analytical Chemistry, ISSN 0039-9140, E-ISSN 1873-3573, Vol. 188, p. 192-198Article in journal (Refereed)
    Abstract [en]

    Several key aspects for the analysis of inositol hexakisphosphate (InsP(6)) have been investigated in order to establish a suitable method for the study of sediment samples from different aquatic systems. Apparent matrix effects for the ion chromatography electrospray ionization tandem mass spectrometric detection (IC-ESI-MS/MS) method were accounted for with a standard addition approach, which also compensated for variation in extraction efficiency. Several parameters of the extraction method were optimized to improve the extraction efficiency for different sediment types. We observed an improvement in the extraction efficiency between 18% and 720%. Finally, the method was used to gain first insights into the relevance of InsP(6) in two aquatic systems located at the German Baltic coastal area. InsP(6) was detected in several sediment samples with concentrations between 2.3 and 15.2 mu g InsP(6)-P/g dry weight (DW).

  • 308.
    Recknagel, Sebastian
    et al.
    BAM Bundesanstalt für Materialforschung und -prüfung, Berlin, Germany.
    Richter, Silke
    BAM Bundesanstalt für Materialforschung und -prüfung, Berlin, Germany.
    Reinholdsson, Fredrik
    Ovako Hofors AB, Hofors, Sweden.
    Pettersson, Jean
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Gustavsson, Ingemar
    Gustavsson Consulting, Stockholm, Sweden.
    An Intercomparison Study of Analytical Methods for the Determination of Magnesium in Low Alloy Steel2012In: Steel Research International, ISSN 1611-3683, E-ISSN 1869-344X, Vol. 83, no 2, p. 146-149Article in journal (Refereed)
    Abstract [en]

    In an intercomparison study three low alloy steel materials were analyzed on their content of the trace element Mg, and five different analytical techniques were used, namely spark-OES, inductively coupled plasma optical emission spectrometry (ICP-OES), inductively coupled plasma time of flight mass spectrometry (ICP-TOFMS), inductively coupled plasma quadrupole mass spectrometry (ICP-QMS), and glow discharge mass spectrometry (GD-MS). Solid steel discs were used for analysis with spark-OES and GD-MS. For the analyses with ICP-OES, ICP-TOFMS, and ICP-QMS steel chips were wet-digested in aqua regia, and the wet-digestion was performed either in polypropylene tubes placed in a heating block or in Teflon pressure vessels using a microwave assisted system. The Mg concentrations obtained for the three steel materials were: 2.0, 2.8, and 10.3 mu gg-1, respectively, and the spread in results was acceptable, giving RSD values in the range of 20-30%.

  • 309.
    Rehnlund, David
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Böhme, Solveig
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Nordh, Tim
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Zou, Yiming
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Lindgren, Fredrik
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Pettersson, Jean
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bexell, Ulf
    Boman, Mats
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Edström, Kristina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Nyholm, Leif
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Diffusion Controlled Trapping of Elemental Lithium in Alloy forming Materials and Current Collectors for Lithium based BatteriesManuscript (preprint) (Other academic)
  • 310.
    Rehnlund, David
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Lindgren, Fredrik
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Böhme, Solveig
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Nordh, Tim
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Zou, Yiming
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Pettersson, Jean
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bexell, Ulf
    Dalarna University.
    Boman, Mats
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Edström, Kristina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Nyholm, Leif
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Improved cycling stability of conversion and alloying anodes through the use of nanomaterials2016Conference paper (Other academic)
    Abstract [en]

    In order to meet the growing need for portable energy storage future batteries need to provide improved energydensities. One major problem lies in the current use of intercalation based electrode materials which are typicallylimited to storing one lithium ion per formula unit. Improved energy storage can be achieved through the use ofconversion and alloying reactions where it is possible to store multiple lithium ions per formula unit. Eventhough impressive energy densities can be obtained through the use of conversion and alloying anode materials,only surpassed by the use of lithium metal itself, these systems are typically plagued by capacity fading duringcycling. The origin is generally ascribed to irreversible reactions with the electrolyte amplified by major volumeexpansion, causing the growth of a solid electrolyte interphase (i.e. SEI). One promising strategy to address thisissue is through the use of nanosized electrode materials (e.g. Si nanoparticles), as it has been shown thatnanoparticles and nanowires show better cycling stability than their bulk counterparts [1, 2]. Large particles (i.emicrometer sized) form cracks during cycling as opposed to smaller particles (i.e. < 150 nm) [3]. Even thoughthe use of nanoparticles can reduce crack formation and the accompanied SEI growth, capacity fading is stillobserved for these systems. Our work has focused on studying freestanding nanostructured conversion materials(e.g. Cu2O nanowires), which offer in depth analyses of the conversion reactions without disturbance frombinders or conducting additives. Contrary to previous understanding nanosized Cu2O thin films and multilayerednanostructures show an increase in capacity during cycling [4, 5]. This behaviour is caused by improvedaccess to the entire material when using the nanomaterials. The system has also shown improved performanceduring cycling likely caused by electrochemical milling of the particles thereby consistently reducing the particlesize and thus allowing more of the material to be accessible. With the successful use of nanosized conversionmaterials our research is now focused on addressing the stability problems of alloying materials by studying theeffect of nanomaterials.

    References

    1. A. Magasinski, et al.. Nat. Mater., 2010. 22: p. 353-3582.

    2 C.K. Chan, et al.. Nat. Nanotechnol., 2008. 3: p. 31-353.

    3 X. H. Liu, et al.. Adv. En. Mater., 2012. 2: p. 722-7414.

    4 D. Rehnlund, et al.. J. Mat. Chem. A., 2014. 2: p. 9574-95865.

    5 D. Rehnlund, et al.. Nanoscale, 2015. 7: p. 13591-13604

  • 311.
    Rehnlund, David
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Lindgren, Fredrik
    Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics and Astronomy, Molecular and Condensed Matter Physics.
    Böhme, Solveig
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Nordh, Tim
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Zou, Yiming
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Pettersson, Jean
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bexell, Ulf
    Dalarna University.
    Boman, Mats
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Edström, Kristina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Nyholm, Leif
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Lithium trapping in alloy forming electrodes and current collectors for lithium based batteries2017Conference paper (Other academic)
  • 312.
    Rehnlund, David
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Lindgren, Fredrik
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Böhme, Solveig
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Nordh, Tim
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Zou, Yiming
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Pettersson, Jean
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bexell, Ulf
    Dalarna Univ, Sch Technol & Business Studies Mat Technol, Falun, Sweden..
    Boman, Mats
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Edström, Kristina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Nyholm, Leif
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Lithium trapping in alloy forming electrodes and current collectors for lithium based batteries2017In: Energy & Environmental Science, ISSN 1754-5692, E-ISSN 1754-5706, Vol. 10, no 6, p. 1350-1357Article in journal (Refereed)
    Abstract [en]

    Significant capacity losses are generally seen for batteries containing high-capacity lithium alloy forming anode materials such as silicon, tin and aluminium. These losses are generally ascribed to a combination of volume expansion effects and irreversible electrolyte reduction reactions. Here, it is shown, based on e.g. elemental analyses of cycled electrodes, that the capacity losses for tin nanorod and silicon composite electrodes in fact involve diffusion controlled trapping of lithium in the electrodes. While an analogous effect is also demonstrated for copper, nickel and titanium current collectors, boron-doped diamond is shown to function as an effective lithium diffusion barrier. The present findings indicate that the durability of lithium based batteries can be improved significantly via proper electrode design or regeneration of the used electrodes.

  • 313.
    Rehnlund, David
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Lindgren, Fredrik
    Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics and Astronomy, Molecular and Condensed Matter Physics.
    Pettersson, Jean
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Edström, Kristina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Nyholm, Leif
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Lithium Trapping in Alloy forming Electrodes and Current Collectors for Lithium based Batteries2018Conference paper (Other academic)
    Abstract [en]

    The next generation of lithium based batteries can be expected to be based on lithium alloy forming anode materials which can store up to ten times more charge than the currently used graphite anodes. This increase in the charge storage capability has motivated significant research towards the commercialization of anode materials such as Si, Sn and Al. These alloy forming anode materials are, however, known to exhibit significant capacity losses during cycling. This is typically ascribed to the volume expansion associated with the formation of the lithium alloys (the volume expansion is e.g. about 280 % for Li3.75Si) resulting in electrode pulverization as well as continuous solid electrolyte interphase (SEI) layer formation [1-3]. While significant progress has been made to decrease the volume expansion problems by the use of e.g. nanoparticles, nanorods and thin films, and/or capacity limitations [1-3], capacity losses are still generally seen [4,5]. This and previously published data suggest that the phenomenon may be due to another effect and that this in fact could stem from lithium trapping in the electrodes [6-8].

    In the present work it is demonstrated (based on e.g. elemental analyses of cycled Sn, Al and Si electrodes) that lithium trapping can account for the capacity losses seen when alloy forming anode materials are cycled versus lithium electrodes, see Figure 1. It is shown that small amounts of elemental lithium are trapped within the electrode material during the cycling as a result of a two-way diffusion process [8] causing the lithium to move into the bulk material even during the delithiation step. This phenomenon, which can be explained by the lithium concentration profiles in the electrodes, makes a complete delithiation process very time consuming. As a result of the lithium trapping effect, the lithium concentration in the electrode increases continuously during the cycling. The experimental results also show that a similar effect can be seen also for commonly used current collector metals such as Cu, Ni and Ti. The latter means that these metals are unsuitable as current collector materials for lithium alloy forming materials in the absence of a thin layer of boron doped diamond serving as a lithium diffusion barrier layer [8].

    References

    1    M. N. Obrovac and V. L. Chevrier, Chem. Rev., 2014, 114, 11444.

    2    X. Su, Q. Wu, J. Li, X. Xiao, A. Lott, W. Lu, B. W. Sheldon and J. Wu, Adv. Energy Mater., 2014, 4, 1300882.

    3    J. R. Szczech and S. Jin, Energy Environ. Sci., 2011, 4, 56.

    4    G. Zheng, S. W. Lee, Z. Liang, H-W. Lee, K. Yan, H. Yao, H. Wang, W. Li, S. Chu and Y. Cui, Nat. Nanotechnol., 2014, 9, 618.

    5    K. Yan, H-W. Lee, T. Gao, G. Zheng, H. Yao, H. Wang, Z. Lu, Y. Zhou, Z. Liang, Z. Liu, S. Chu and Y. Cui, Nano Letters, 2014, 14, 6016.

    6    G. Oltean, C-W. Tai, K. Edström and L. Nyholm, J. Power Sources, 2014, 269, 266.

    7    A. L. Michan, G. Divitini, A. J. Pell, M. Leskes, C. Ducati and C. P. Grey, J. Am. Chem. Soc., 2016, 138, 7918.

    8    D. Rehnlund, F. Lindgren, S. Böhme, T. Nordh, Y. Zou, J. Pettersson, U. Bexell, M. Boman, K. Edström and L. Nyholm, Energy Environ. Sci., 10 (2017) 1350.

     

  • 314.
    Rehnlund, David
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Pettersson, Jean
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Edström, Kristina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Nyholm, Leif
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Lithium trapping in microbatteries based on lithium- and Cu2O-coated copper nanorods2018In: ChemistrySelect, E-ISSN 2365-6549, Vol. 3, no 8, p. 2311-2314Article in journal (Refereed)
    Abstract [en]

    Microbatteries based on three-dimensional (3D) electrodes composed of thin films of Li and Cu2O coated on Cu nanorod current collectors by electrodeposition and spontaneous oxidation, respectively, are described and characterised electrochemically. High-resolution scanning electron microscopy (HR-SEM) data indicate that the Li electrodeposition resulted in a homogenous coverage of the Cu nanorods and elemental analyses were also used to determine the amount of lithium in the Li-coated electrodes. The results show that 3D Cu2O/Cu electrodes can be cycled versus 3D Li/Cu electrodes but that the capacity decreased during the cycling due to Li trapping in the Cu current collector of the 3D Li/Cu electrode. These findings highlight the problem of using copper current collectors together with metallic lithium as the formation of a solid solution yields considerable losses of electroactive lithium and hence capacity.

  • 315.
    Rehnlund, David
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Pettersson, Jean
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Edström, Kristina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Structural Chemistry.
    Nyholm, Leif
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Microbatteries based on 3D Li and Cu2O coated Cu nanorodsManuscript (preprint) (Other academic)
  • 316.
    Reijmar Brunnström, Karin
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Development of lipodisks as carriers for cationic amphiphilic peptides2016Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    Antibiotics have made a tremendous contribution to mankind. They are one of the most successful medicines in human history. However, more and more bacterial strains develop resistance and the risk to public health can hardly be overstated. New types of antibiotics are urgently needed. Antimicrobial peptides (AMPs) have emerged as potential antibiotics because of their broad-spectrum activities and non-conventional mechanism of action. More recently, they have also received attention as promising anticancer agents. The clinical and commercial development of AMPs as a new generation of antibiotics and anticancer drugs is hampered, however, by issues concerning the toxicity, specificity and stability of the peptides.

    The aim of this thesis has been to explore if formulation in a novel type of nanocarriers, referred to as lipodisks, can be used to increase the therapeutic potential of AMPs as antimicrobial and anticancer agents. Focus has been on AMPs classified as cationic amphiphilic peptides.

    Encouragingly, the data presented suggests that the therapeutic potential of the AMP melittin as an antimicrobial and anticancer agent can be substantially increased by formulation in lipodisks. When formulated in the lipodisk, melittin is protected against enzymatic degradation. The lipodisk also offer a slow-release effect that sustains the bacterial cell-killing effect. We also show that specific delivery of melittin to tumour cells can be obtained by formulating the peptide in small EGF-targeting lipodisks.

    Melittin contains a tryptophan residue and its interaction with lipodisks can be characterized by means of fluorimetric binding assays. In order to investigate the binding behavior also for peptides that lack intrinsic fluorescence, we developed a method based on measurements using the QCM-D technique. Studies using this, and other techniques, confirmed that it is a general behavior for cationic amphiphilic peptides to preferentially bind to the highly curved rim of lipodisks. Results of our binding studies show that the peptide to lipid ratio in the lipodisks can be tuned and optimized by varying the size and charge of the disks.

    Taken together, the findings in this thesis point towards PEG-stabilized lipodisks as promising nanocarriers for antibacterial and anticancer peptides.

  • 317.
    Reijmar, Karin
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Edwards, Katarina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Andersson, Karl
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Medical Radiation Science. Ridgeview Instruments AB, Skillsta 4, 740 20 Vänge, Sweden.
    Agmo Hernández, Víctor
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Characterizing and controlling the loading and release of cationic amphiphilic peptides onto and from PEG-stabilized lipodisks2016In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 32, no 46, p. 12091-12099Article in journal (Refereed)
    Abstract [en]

    Recent studies have identified PEG-stabilized lipid nanodisks (lipodisks) as promising carriers for cationic amphiphilic peptides with antimicrobial and anticancer activity. Using fluorimetric and nanogravimetric methods, we have in this work characterized the parameters describing and controlling the binding of three selected peptides (melittin, LL37, and magainin 2) onto lipodisks. It was found that the affinity of melittin for lipodisks is independent of the disk size and rim charge. On the other hand, the number of binding sites is strongly dependent on both parameters, with the highest loading being obtained for small disks with a negatively charged rim. An optimized composition of the lipodisks was utilized to study the loading of antimicrobial peptides magainin 2 and human LL37. It was observed that although magainin 2 can be loaded in large amounts, it is released very fast upon dilution, which limits future therapeutic applications. In contrast, LL37 can be loaded at relevant concentrations and the formulation is stable. This opens up for applications of LL37-loaded lipodisks as antibiotics and in anticancer treatments.

  • 318.
    Reinert, Jochim
    et al.
    Univ Gottingen, Univ Med Ctr UMG, Div Mol Psychiat, D-37075 Gottingen, Germany..
    Richard, Bernhard C.
    Univ Gottingen, Univ Med Ctr UMG, Div Mol Psychiat, D-37075 Gottingen, Germany..
    Klafki, Hans W.
    Univ Gottingen, Univ Med Ctr UMG, Dept Psychiat & Psychotherapy, Von Siebold Str 5, D-37075 Gottingen, Germany..
    Friedrich, Beate
    Synapt Syst, Gottingen, Germany..
    Bayer, Thomas A.
    Univ Gottingen, Univ Med Ctr UMG, Div Mol Psychiat, D-37075 Gottingen, Germany.;Univ Gottingen, Univ Med Ctr UMG, Dept Psychiat & Psychotherapy, Von Siebold Str 5, D-37075 Gottingen, Germany..
    Wiltfang, Jens
    Univ Gottingen, Univ Med Ctr UMG, Dept Psychiat & Psychotherapy, Von Siebold Str 5, D-37075 Gottingen, Germany..
    Kovacs, Gabor G.
    Med Univ Vienna, Inst Neurol, Vienna, Austria..
    Ingelsson, Martin
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Public Health and Caring Sciences, Geriatrics.
    Lannfelt, Lars
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Public Health and Caring Sciences, Geriatrics.
    Paetau, Anders
    Univ Helsinki, Dept Pathol, Helsinki, Finland.;Univ Helsinki Hosp, Helsinki, Finland..
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Wirths, Oliver
    Univ Gottingen, Univ Med Ctr UMG, Div Mol Psychiat, D-37075 Gottingen, Germany.;Univ Gottingen, Univ Med Ctr UMG, Dept Psychiat & Psychotherapy, Von Siebold Str 5, D-37075 Gottingen, Germany..
    Deposition of C-terminally truncated A beta species A beta 37 and A beta 39 in Alzheimer's disease and transgenic mouse models2016In: Acta neuropathologica communications, E-ISSN 2051-5960, Vol. 4, article id 24Article in journal (Refereed)
    Abstract [en]

    In Alzheimer's disease (AD) a variety of amyloid beta-peptides (A beta) are deposited in the form of extracellular diffuse and neuritic plaques (NP), as well as within the vasculature. The generation of A beta from its precursor, the amyloid precursor protein (APP), is a highly complex procedure that involves subsequent proteolysis of APP by beta-and gamma-secretases. Brain accumulation of A beta due to impaired A beta degradation and/or altered ratios between the different A beta species produced is believed to play a pivotal role in AD pathogenesis. While the presence of A beta 40 and A beta 42 in vascular and parenchymal amyloid have been subject of extensive studies, the deposition of carboxyterminal truncated A beta peptides in AD has not received comparable attention. In the current study, we for the first time demonstrate the immunohistochemical localization of A beta 37 and A beta 39 in human sporadic AD (SAD). Our study further included the analysis of familial AD (FAD) cases carrying the APP mutations KM670/671NL, E693G and I716F, as well as a case of the PSEN1 Delta Exon9 mutation. A beta 37 and A beta 39 were found to be widely distributed within the vasculature in the brains of the majority of studied SAD and FAD cases, the latter also presenting considerable amounts of A beta 37 containing NPs. In addition, both peptides were found to be present in extracellular plaques but only scarce within the vasculature in brains of a variety of transgenic AD mouse models. Taken together, our study indicates the importance of C-terminally truncated A beta in sporadic and familial AD and raises questions about how these species are generated and regulated.

  • 319.
    Richard, B. C.
    et al.
    Charite Univ Med Berlin, Dept Neuropathol AG Heppner, Campus Mitte,Charitapl 1, DE-10117 Berlin, Germany;Univ Med Gottingen, Dept Psychiat & Psychotherapy, von Siebold Str 5, DE-37075 Gottingen, Germany.
    Bayer, T. A.
    Charite Univ Med Berlin, Dept Neuropathol AG Heppner, Campus Mitte,Charitapl 1, DE-10117 Berlin, Germany;Univ Med Gottingen, Dept Psychiat & Psychotherapy, von Siebold Str 5, DE-37075 Gottingen, Germany.
    Lind, Sara
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Shevchenko, Ganna
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    A simplified and sensitive immunoprecipitation mass spectrometry protocol for the analysis of amyloid-beta peptides in brain tissue2019In: CLINICAL MASS SPECTROMETRY, ISSN 2376-9998, Vol. 14, p. 83-88Article in journal (Refereed)
    Abstract [en]

    In the field of Alzheimer's disease, there is an urgent need for novel analytical tools to identify disease-specific biomarkers and to evaluate therapeutics. Preclinical trials commonly employ amyloid beta (A beta) peptide signatures as a read-out. In this paper, we report a simplified and detailed protocol for robust immunoprecipitation of A beta in brain tissue prior to mass spectrometric detection exemplified by a study using transgenic mice. The established method employed murine monoclonal and rabbit polyclonal antibodies and was capable of yielding well-reproducible peaks of high intensity with low background signal intensities corresponding to various A beta forms.

  • 320.
    Rodiouchkina, Katerina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Naturhistorisk Riksmuseet.
    Development of a multi-collector inductively coupled plasma massspectrometry method for measurement of stable sulphur isotope ratios in aerosol sulphate2018Independent thesis Advanced level (degree of Master (Two Years)), 20 credits / 30 HE creditsStudent thesis
    Abstract [en]

    Sulphur stable isotope ratios are useful tracers in geological and environmental studies. They can for example be used to trace the origin of atmospheric sulphate aerosols, because anthropogenic sulphate and natural sulphate have distinguishable δ34S-values (δ34S value of approximately +0 to +8 ‰ for anthropogenic and approximately +12 to +19 ‰ for natural). This is useful for climate modelling research, due to the net cooling effect of aerosol sulphate. In the present study a Nu Plasma II (Nu Instruments) multi collector inductively coupled plasma mass spectrometer (MC-ICP-MS) method for measuring stable sulphur isotope ratios in low sulphur content samples, such as sulphate aerosols, was developed. The method was then applied to a sulphate aerosol sample collected in the Maldives.Most of the measurements were performed at high resolution, due to the interferences on 33S. Heated spray chamber coupled to a desolvating membrane, Aridus II (Cetac), increased the sensitivity and reduced interferences notably compared to wet plasma mode. Aridus II gave more stable measurements than DSN-100 (Nu Instruments). Determinations of δ34S for IAEA S1, S3, and S4 were accurate and the determined δ34S-value of the CIT #39 seawater standard (21.05 ± 0.36 ‰, 2SD, n=42) was comparable with published data. In general, Si internal standardization correction increased precision ~2.5 times compared to non-corrected values. The δ34S-value for the sulphate aerosol sample was determined to 3.82 ±0.41 ‰ (2SD, n=40). Repeatability of ~62 nmol introduced sulphur (2 μg/mL) was generally 0.15 ‰ (2SD, n=5) for the SW and 0.19 ‰ (2SD, n=5) for the sulphate aerosol sample. Comparable results for the SW (20.61±0.09 ‰, 2SD, n=4) and sulphate aersosol sample (3.77 ± 0.08 ‰, 2SD, n=8) were obtained with the method applied to Neptune Plus (Thermo Fischer Scientific) MC-ICP-MS in a different laboratory. The determined aerosol sulphate δ34S-value indicated that the sampled sulphate aerosol originated from anthropogenic sources.

  • 321. Rodriguez-Meizoso, I.
    et al.
    Werner, Oskar
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Quan, C.
    Knez, Z.
    Turner, C.
    Phase-behavior of alkyl ketene dimmer (AKD) in supercritical carbon dioxide: The implications of using different solubility measurement methods2012In: Journal of Supercritical Fluids, ISSN 0896-8446, E-ISSN 1872-8162, Vol. 61, p. 25-33Article in journal (Refereed)
    Abstract [en]

    In this work, three different methods were used to determine the phase behavior of alkyl ketene dimer (AKD) in supercritical carbon dioxide (SC-CO2). Rough values for the total solubility of AKD in SC-CO2 were obtained. The solubility ranges from 1 to 14 mg AKD/g CO2 at temperatures from 40 to 80 degrees C and pressures from 10 to 30 MPa. A significant increase in solubility was observed in the region above 50 degrees C and 20 MPa. A region of improved solubility was found, without the presence of a cross-over pressure point. The fact that different solubility methods gave different results was discussed and the importance of data interpretation was highlighted. H-1 NMR and MALDI-TOF MS analyses were utilized to chemically characterize the AKD wax. Its special behavior and the influence of data interpretation on the design of a RESS process were discussed.

  • 322.
    Ronquist, Göran
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Biochemial structure and function.
    Ek, Bo
    Uppsala University, Science for Life Laboratory, SciLifeLab. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Stavreus-Evers, Anneli
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Women's and Children's Health, Obstetrics and Gynaecology.
    Larsson, Anders
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Biochemial structure and function.
    Ronquist, Gunnar
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences.
    Human Prostasomes Express Glycolytic Enzymes with Capacity for ATP Production2013In: Andrology, ISSN 2047-2919, Vol. 1, no S2, p. 76-76Article in journal (Other academic)
  • 323.
    Ronquist, Göran K
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Biochemial structure and function.
    Ek, Bo
    Uppsala University, Science for Life Laboratory, SciLifeLab. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Ronquist, Gunnar
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Biochemial structure and function.
    Morrell, Jane
    Carlsson, Lena
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Biochemial structure and function.
    Larsson, Anders
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Biochemial structure and function.
    Biochemical characterization of stallion prostasomes and comparison to their human counterparts2013In: Systems biology in reproductive medicine, ISSN 1939-6376, Vol. 59, no 6, p. 297-303Article in journal (Refereed)
    Abstract [en]

    Release of nanometer-sized prostasomes into human and equine semen suggests essential functions in their relationships with sperm cells and the fertilization process. The two types of prostasomes displayed ultrastructural similarities, albeit the human prostasomes were somewhat larger than the stallion prostasomes. A high ratio of saturated fatty acids was characteristic for the two prostasome types. Electrophoretic separation systems revealed an equine prostasomal pattern different from that of human. The 21 distinctive low molecular weight protein spots in the 2D-gel (with no counterparts in human prostasomes) were identified via peptide mass fingerprinting, several of which may be different isoforms. Out of the three high molecular weight bands characteristic for human prostasomes (CD10, CD13, and CD26), CD10 and CD13 were retrieved in equine prostasomes. We present some new proteins of horse prostasomes not found in their human counterparts. Further studies are warranted to reveal the function of these proteins.

  • 324.
    Ronquist, K Göran
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Biochemial structure and function.
    Ek, Bo
    Uppsala University, Science for Life Laboratory, SciLifeLab. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Morrell, Jane
    Stavreus-Evers, Anneli
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Women's and Children's Health, Obstetrics and Gynaecology.
    Ström Holst, Bodil
    Humblot, Patrice
    Ronquist, Gunnar
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Biochemial structure and function.
    Larsson, Anders
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Biochemial structure and function.
    Prostasomes from four different species are able to produce extracellular adenosine triphosphate (ATP)2013In: Biochimica et Biophysica Acta - General Subjects, ISSN 0304-4165, E-ISSN 1872-8006, Vol. 1830, no 10, p. 4604-4610Article in journal (Refereed)
    Abstract [en]

    BACKGROUND:

    Prostasomes are extracellular vesicles. Intracellularly they are enclosed by another larger vesicle, a so called "storage vesicle" equivalent to a multivesicular body of late endosomal origin. Prostasomes in their extracellular context are thought to play a crucial role in fertilization.

    METHODS:

    Prostasomes were purified according to a well worked-out schedule from seminal plasmas obtained from human, canine, equine and bovine species. The various prostasomes were subjected to SDS-PAGE separation and protein banding patterns were compared. To gain knowledge of the prostasomal protein systems pertaining to prostasomes of four different species proteins were analyzed using a proteomic approach. An in vitro assay was employed to demonstrate ATP formation by prostasomes of different species.

    RESULTS:

    The SDS-PAGE banding pattern of prostasomes from the four species revealed a richly faceted picture with most protein bands within the molecular weight range of 10-150kDa. Some protein bands seemed to be concordant among species although differently expressed and the number of protein bands of dog prostasomes seemed to be distinctly fewer. Special emphasis was put on proteins involved in energy metabolic turnover. Prostasomes from all four species were able to form extracellular adenosine triphosphate (ATP). ATP formation was balanced by ATPase activity linked to the four types of prostasomes.

    CONCLUSION:

    These potencies of a possession of functional ATP-forming enzymes by different prostasome types should be regarded against the knowledge of ATP having a profound effect on cell responses and now explicitly on the success of the sperm cell to fertilize the ovum.

    GENERAL SIGNIFICANCE:

    This study unravels energy metabolic relationships of prostasomes from four different species.

  • 325.
    Ronquist, K Göran
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Clinical Chemistry.
    Ek, Bo
    Uppsala University, Science for Life Laboratory, SciLifeLab. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Stavreus-Evers, Anneli
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Women's and Children's Health, Obstetrics and Gynaecology.
    Larsson, Anders
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Clinical Chemistry.
    Ronquist, Gunnar
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Clinical Chemistry.
    Human prostasomes express glycolytic enzymes with capacity for ATP production2013In: American Journal of Physiology. Endocrinology and Metabolism, ISSN 0193-1849, E-ISSN 1522-1555, Vol. 304, no 6, p. E576-E582Article in journal (Refereed)
    Abstract [en]

    Prostasomes are prostate-derived, exosome-like microvesicles that transmit signaling complexes between the acinar epithelial cells of the prostate and sperm cells. A vast majority of prostasomes has a diameter of 30 - 200 nm and they are generally surrounded by a classical membrane bilayer. Using a selected proteomic approach, it became increasingly clear that prostasomes harbor distinct subsets of proteins that may be linked to adenosine triphosphate (ATP) metabolic turnover that in turn might be of importance in the role of prostasomes as auxiliary instruments in the fertilization process. Among the 21 proteins identified most of the enzymes of anaerobic glycolysis were represented and three of the glycolytic enzymes present are among the ten top proteins found in most exosomes, once again linking prostasomes to the exosome family. Other prostasomal enzymes involved in ATP turnover were adenylate kinase, ATPase, 5'-nucleotidase and hexose transporters. The identified enzymes in their prostasomal context were operational for ATP formation when supplied with substrates. The net ATP production was low due to a high prostasomal ATPase activity that could be partially inhibited by vanadate that was utilized in order to profile the ATP forming ability of prostasomes. Glucose and fructose were equivalent as glycolytic substrates for prostasomal ATP formation and the enzymes involved were apparently surface-located on prostasomes, since an alternative substrate not being membrane-permeable (glyceraldehyde 3-phosphate) was operative, too. There is no clear cut function linked to this subset of prostasomal proteins but some possible roles are discussed.

  • 326.
    Roomp, Kirsten
    et al.
    Univ Luxembourg, Luxembourg Ctr Syst Biomed, Esch Belval, Luxembourg..
    Kristinsson, Hjalti
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Schvartz, Domitille
    Univ Geneva, Human Prot Sci Dept, Ctr Med Univ, Geneva, Switzerland..
    Ubhayasekera, Kumari
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Sargsyan, Ernest
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Manukyan, Levon
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Chowdhury, Azazul Islam
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Manell, Hannes
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Satagopam, Venkata
    Univ Luxembourg, Luxembourg Ctr Syst Biomed, Esch Belval, Luxembourg..
    Groebe, Karlfried
    Pivot Biomed Sci GmbH, Trier, Germany..
    Schneider, Reinhard
    Univ Luxembourg, Luxembourg Ctr Syst Biomed, Esch Belval, Luxembourg..
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Sanchez, Jean-Charles
    Univ Geneva, Human Prot Sci Dept, Ctr Med Univ, Geneva, Switzerland..
    Bergsten, Peter
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Combined lipidomic and proteomic analysis of isolated human islets exposed to palmitate reveals time-dependent changes in insulin secretion and lipid metabolism2017In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 12, no 4, article id e0176391Article in journal (Refereed)
    Abstract [en]

    Studies on the pathophysiology of type 2 diabetes mellitus (T2DM) have linked the accumulation of lipid metabolites to the development of beta-cell dysfunction and impaired insulin secretion. In most in vitro models of T2DM, rodent islets or beta-cell lines are used and typically focus is on specific cellular pathways or organs. Our aim was to, firstly, develop a combined lipidomics and proteomics approach for lipotoxicity in isolated human islets and, secondly, investigate if the approach could delineate novel and/or confirm reported mechanisms of lipotoxicity. To this end isolated human pancreatic islets, exposed to chronically elevated palmitate concentrations for 0, 2 and 7 days, were functionally characterized and their levels of multiple targeted lipid and untargeted protein species determined. Glucosestimulated insulin secretion from the islets increased on day 2 and decreased on day 7. At day 7 islet insulin content decreased and the proinsulin to insulin content ratio doubled. Amounts of cholesterol, stearic acid, C16 dihydroceramide and C24: 1 sphingomyelin, obtained from the lipidomic screen, increased time-dependently in the palmitate-exposed islets. The proteomic screen identified matching changes in proteins involved in lipid biosynthesis indicating up-regulated cholesterol and lipid biosynthesis in the islets. Furthermore, proteins associated with immature secretory granules were decreased when palmitate exposure time was increased despite their high affinity for cholesterol. Proteins associated with mature secretory granules remained unchanged. Pathway analysis based on the protein and lipid expression profiles implicated autocrine effects of insulin in lipotoxicity. Taken together the study demonstrates that combining different omics approaches has potential in mapping of multiple simultaneous cellular events. However, it also shows that challenges exist for effectively combining lipidomics and proteomics in primary cells. Our findings provide insight into how saturated fatty acids contribute to islet cell dysfunction by affecting the granule maturation process and confirmation in human islets of some previous findings from rodent islet and cell-line studies.

  • 327.
    Rossel, Pamela E.
    et al.
    Max Planck Inst, HGF MPG Grp Deep Sea Ecol & Technol, Bremen, Germany; Helmholtz Ctr Polar & Marine Res, Alfred Wegener Inst, Bremerhaven, Germany; Carl von Ossietzky Univ Oldenburg, Inst Chem & Biol Marine Environm ICBM, Res Grp Marine Geochem, ICBM MPI Bridging Grp, Oldenburg, Germany.
    Stubbins, Aron
    Univ Georgia, Dept Marine Sci, Skidaway Inst Oceanog, Savannah, GA USA.
    Rebling, Tammo
    Univ Appl Sci, Hsch Osnabruck, Lab Proc Engn, Osnabruck, Germany.
    Koschinsky, Andrea
    Jacobs Univ Bremen, Dept Phys & Earth Sci, Campus Ring, Bremen, Germany.
    Hawkes, Jeffrey A.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Dittmar, Thorsten
    Carl von Ossietzky Univ Oldenburg, Inst Chem & Biol Marine Environm ICBM, Res Grp Marine Geochem, ICBM MPI Bridging Grp, Oldenburg, Germany.
    Corrigendum to “Thermally altered marine dissolved organic matter in hydrothermal fluids” [Organ. Geochem. 110 (2017) 73–86]2018In: Organic Geochemistry, ISSN 0146-6380, E-ISSN 1873-5290, Vol. 117, p. 70-70Article in journal (Other academic)
  • 328.
    Rossel, Pamela E.
    et al.
    Max Planck Inst, HGF MPG Grp Deep Sea Ecol & Technol, Bremen, Germany; Helmholtz Ctr Polar & Marine Res, Alfred Wegener Inst, Bremerhaven, Germany; Carl von Ossietzky Univ Oldenburg, Inst Chem & Biol Marine Environm ICBM, Res Grp Marine Geochem, ICBM MPI Bridging Grp, Oldenburg, Germany.
    Stubbins, Aron
    Univ Georgia, Dept Marine Sci, Skidaway Inst Oceanog, Savannah, GA USA.
    Rebling, Tammo
    Univ Appl Sci, Hsch Osnabruck, Lab Proc Engn, Osnabruck, Germany.
    Koschinsky, Andrea
    Jacobs Univ Bremen, Dept Phys & Earth Sci, Campus Ring, Bremen, Germany.
    Hawkes, Jeffrey A.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Dittmar, Thorsten
    Carl von Ossietzky Univ Oldenburg, Inst Chem & Biol Marine Environm ICBM, Res Grp Marine Geochem, ICBM MPI Bridging Grp, Oldenburg, Germany.
    Thermally altered marine dissolved organic matter in hydrothermal fluids2017In: Organic Geochemistry, ISSN 0146-6380, E-ISSN 1873-5290, Vol. 110, p. 73-86Article in journal (Refereed)
    Abstract [en]

    Hydrothermal vent fluids contain thermally modified dissolved organic matter (DOM) originally entrained from sediments and seawater. We hypothesized that in hydrothermal systems DOM molecular composition is modulated by (i) fluid contribution, (ii) thermal decomposition and pH, and (iii) aspects particular to the vent system. Hence, solid phase extracted (SPE) DOM samples collected along the Mid-Atlantic Ridge (MAR) were molecularly characterized via 15 Tesla Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR-MS). The molecular character of an oceanic DOM sample was also determined before and after thermal (300 °C) decomposition at acidic and neutral pH. Multivariate statistical analysis indicated that DOM composition was strongly influenced by fluid contribution (Mg2+ concentration between 12 and 54 mM), which correlated positively with measured temperature (between 8 and 375 °C). In comparison, pH of the fluids (between 2.5 and 6.9) had a minor influence. Seafloor pressure, used as a theoretical maximum fluid temperature at the seafloor, separated the fluids collected at Menez Gwen from deeper locations, due to the higher abundance of peptide, carboxyl-rich alicyclic (CRAM) and aromatic molecular formulae at Menez Gwen. Compared with seawater DOM, thermally decomposed DOM had on average lower molecular mass, lower O/C ratios, fewer double bond equivalents, and fewer CRAM formulae but higher aromaticity - the same molecular features displayed by MAR hydrothermal fluids. The study provides evidence that thermal reworking plays a major role in shaping DOM mixtures from hydrothermal fluids along the MAR, which partly represent thermally reworked marine DOM that survived hydrothermal circulation.

  • 329.
    Rostvall, Ande
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Evaluation of sorption materials for the removal of organic micropollutants in domestic wastewater and their potential infiltration in groundwater2017Independent thesis Advanced level (degree of Master (Two Years)), 30 credits / 45 HE creditsStudent thesis
  • 330.
    Rydfjord, Jonas
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Organic Pharmaceutical Chemistry.
    Svensson, Fredrik
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Organic Pharmaceutical Chemistry.
    Trejos, Alejandro
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Organic Pharmaceutical Chemistry.
    Sjöberg, Per J. R.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Sköld, Christian
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Organic Pharmaceutical Chemistry.
    Sävmarker, Jonas
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Organic Pharmaceutical Chemistry.
    Odell, Luke R.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Organic Pharmaceutical Chemistry.
    Larhed, Mats
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Organic Pharmaceutical Chemistry.
    Decarboxylative Palladium(II)-Catalyzed Synthesis of Aryl Amidines from Aryl Carboxylic Acids: Development and Mechanistic Investigation2013In: Chemistry - A European Journal, ISSN 0947-6539, E-ISSN 1521-3765, Vol. 19, no 41, p. 13803-13810Article in journal (Refereed)
    Abstract [en]

    A fast and convenient synthesis of aryl amidines starting from carboxylic acids and cyanamides is reported. The reaction was achieved by palladium(II)-catalysis in a one-step microwave protocol using [Pd(O2CCF3)(2)], 6-methyl-2,2-bipyridyl and trifluoroacetic acid (TFA) in N-methylpyrrolidinone (NMP), providing the corresponding aryl amidines in moderate to excellent yields. The protocol is very robust with regards to the cyanamide coupling partner but requires electron-rich ortho-substituted aryl carboxylic acids. Mechanistic insight was provided by a DFT investigation and direct ESI-MS studies of the reaction. The results of the DFT study correlated well with the experimental findings and, together with the ESI-MS study, support the suggested mechanism. Furthermore, a scale-out (scale-up) was performed with a non-resonant microwave continuous-flow system, achieving a maximum throughput of 11mmolh(-1) by using a glass reactor with an inner diameter of 3mm at a flow rate of 1mLmin(-1).

  • 331.
    Salah, Heba
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Clinical Neurophysiology. Karolinska Inst, Dept Physiol & Pharmacol, SE-17777 Stockholm, Sweden..
    Li, Meishan
    Karolinska Inst, Dept Physiol & Pharmacol, SE-17777 Stockholm, Sweden..
    Cacciani, Nicola
    Karolinska Inst, Dept Physiol & Pharmacol, SE-17777 Stockholm, Sweden..
    Gastaldello, Stefano
    Karolinska Inst, Dept Physiol & Pharmacol, SE-17777 Stockholm, Sweden..
    Ogilvie, Hannah
    Karolinska Inst, Dept Physiol & Pharmacol, SE-17777 Stockholm, Sweden..
    Akkad, Hazem
    Karolinska Inst, Dept Physiol & Pharmacol, SE-17777 Stockholm, Sweden..
    Namuduri, Arvind Venkat
    Karolinska Inst, Dept Physiol & Pharmacol, SE-17777 Stockholm, Sweden..
    Morbidoni, Valeria
    Univ Padua, Dept Womens & Childrens Hlth, Clin Genet Unit, I-35128 Padua, Italy..
    Artemenko, Konstantin A.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Balogh, Gabor
    Hungarian Acad Sci, Biol Res Ctr, Inst Biochem, H-6726 Szeged, Hungary..
    Martinez-Redondo, Vicente
    Karolinska Inst, Dept Physiol & Pharmacol, SE-17777 Stockholm, Sweden..
    Jannig, Paulo
    Karolinska Inst, Dept Physiol & Pharmacol, SE-17777 Stockholm, Sweden..
    Hedström, Yvette
    Karolinska Inst, Dept Physiol & Pharmacol, SE-17777 Stockholm, Sweden..
    Dworkin, Barry
    Karolinska Inst, Dept Physiol & Pharmacol, SE-17777 Stockholm, Sweden.;Penn State Univ, Dept Neurosci, Hershey, PA 17033 USA..
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab. Univ Utah, Sch Med, Dept Pathol, Salt Lake City, UT 84112 USA.;Binzhou Med Univ, Precis Med, Yantai 264003, Shandong, Peoples R China..
    Ruas, Jorge
    Karolinska Inst, Dept Physiol & Pharmacol, SE-17777 Stockholm, Sweden..
    Vigh, Laszlo
    Hungarian Acad Sci, Biol Res Ctr, Inst Biochem, H-6726 Szeged, Hungary..
    Salviati, Leonardo
    Univ Padua, Dept Womens & Childrens Hlth, Clin Genet Unit, I-35128 Padua, Italy..
    Larsson, Lars
    Karolinska Inst, Dept Physiol & Pharmacol, SE-17777 Stockholm, Sweden.;Penn State Univ, Dept Biobehav Hlth, University Pk, PA 16802 USA.;Karolinska Inst, Clin Neurophysiol, Dept Clin Neurosci, SE-17777 Stockholm, Sweden..
    The chaperone co-inducer BGP-15 alleviates ventilation-induced diaphragm dysfunction2016In: Science Translational Medicine, ISSN 1946-6234, E-ISSN 1946-6242, Vol. 8, no 350, article id 350ra103Article in journal (Refereed)
    Abstract [en]

    Ventilation-induced diaphragm dysfunction (VIDD) is a marked decline in diaphragm function in response to mechanical ventilation, which has negative consequences for individual patients' quality of life and for the health care system, but specific treatment strategies are still lacking. We used an experimental intensive care unit (ICU) model, allowing time-resolved studies of diaphragm structure and function in response to long-term mechanical ventilation and the effects of a pharmacological intervention (the chaperone co-inducer BGP-15). The marked loss of diaphragm muscle fiber function in response to mechanical ventilation was caused by post-translational modifications (PTMs) of myosin. In a rat model, 10 days of BGP-15 treatment greatly improved diaphragm muscle fiber function (by about 100%), although it did not reverse diaphragm atrophy. The treatment also provided protection from myosin PTMs associated with HSP72 induction and PARP-1 inhibition, resulting in improvement of mitochondrial function and content. Thus, BGP-15 may offer an intervention strategy for reducing VIDD in mechanically ventilated ICU patients.

  • 332. Samgina, Tatiana Y.
    et al.
    Vorontsov, Egor A.
    Gorshkov, Vladimir A.
    Artemenko, Konstantin A.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Zubarev, Roman A.
    Ytterberg, Jimmy A.
    Lebedev, Albert T.
    Collision-Induced Dissociation Fragmentation Inside Disulfide C-Terminal Loops of Natural Non-Tryptic Peptides2013In: Journal of the American Society for Mass Spectrometry, ISSN 1044-0305, E-ISSN 1879-1123, Vol. 24, no 7, p. 1037-1044Article in journal (Refereed)
    Abstract [en]

    Collision-induced dissociation (CID) spectra of long non-tryptic peptides are usually quite complicated and rather difficult to interpret. Disulfide bond formed by two cysteine residues at C-terminus of frog skin peptides precludes one to determine sequence inside the forming loop. Thereby, chemical modification of S-S bonds is often used in "bottom up" sequencing approach. However, low-energy CID spectra of natural non-tryptic peptides with C-terminal disulfide cycle demonstrate an unusual fragmentation route, which may be used to elucidate the "hidden" C-terminal sequence. Low charge state protonated molecules experience peptide bond cleavage at the N-terminus of C-terminal cysteine. The forming isomeric acyclic ions serve as precursors for a series of b-type ions revealing sequence inside former disulfide cycle. The reaction is preferable for peptides with basic lysine residues inside the cycle. It may also be activated by acidic protons of Asp and Glu residues neighboring the loop. The observed cleavages may be quite competitive, revealing the sequence inside disulfide cycle, although S-S bond rupture does not occur in this case.

  • 333.
    Samgina, Tatiana Yu
    et al.
    Moscow MV Lomonosov State Univ, Dept Chem, Leninskie Gori 1-3, Moscow 119991, Russia..
    Artemenko, Konstantin A.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Trebse, Polonca
    Univ Ljubljana, Fac Hlth Sci, Zdravstvena Pot 5, Ljubljana 1000, Slovenia..
    Torkar, Gregor
    Univ Ljubljana, Fac Educ, Kardeljeva Ploscad 16, Ljubljana 1000, Slovenia..
    Tolpina, Miriam D.
    Moscow MV Lomonosov State Univ, Dept Chem, Leninskie Gori 1-3, Moscow 119991, Russia..
    Lebedev, Albert T.
    Moscow MV Lomonosov State Univ, Dept Chem, Leninskie Gori 1-3, Moscow 119991, Russia..
    Differentiation of frogs from two populations belonging to the Pelophylax esculentus complex by LC-MS/MS comparison of their skin peptidomes2017In: Analusis, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 409, no 7, p. 1951-1961Article in journal (Refereed)
    Abstract [en]

    LC-MS/MS was applied to establish the composition of the skin peptidome of a Slovenian green frog belonging to the Pelophylax esculentus complex. As this was similar to the peptidome of the Moscow population of Pelophylax ridibundus, it allowed us to identify the Slovenian frog from the Pelophylax esculentus complex as Pelophylax ridibundus. The sequences of six new peptides from the brevinin 2 family are reported for the first time on the basis of manual interpretation of their tandem mass spectra. The structural similarity of the brevinin 2 peptides from the Moscow and Slovenian populations of Pelophylax ridibundus enables peptides from this family to be utilized as biomarkers for Pelophylax ridibundus inter- and intraspecies differentiation, and the proposed approach can be used as an analytical tool for differentiating the corresponding species and populations. The potential biological activities of the novel peptides were estimated by 2D mass mapping. The results allowed us to classify all of the available peptides belonging to the brevinin 2 family.

  • 334.
    Samgina, Tatiana Yu.
    et al.
    Moscow MV Lomonosov State Univ, Dept Chem, Moscow, Russia..
    Tolpina, Miriam D.
    Moscow MV Lomonosov State Univ, Dept Chem, Moscow, Russia..
    Trebse, Polonca
    Univ Ljubljana, Ljubljana, Slovenia..
    Torkar, Gregor
    Univ Ljubljana, Ljubljana, Slovenia..
    Artemenko, Konstantin A.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Lebedev, Albert T.
    Moscow MV Lomonosov State Univ, Dept Chem, Moscow, Russia..
    LTQ Orbitrap Velos in routine de novo sequencing of non-tryptic skin peptides from the frog Rana latastei with traditional and reliable manual spectra interpretation2016In: Rapid Communications in Mass Spectrometry, ISSN 0951-4198, E-ISSN 1097-0231, Vol. 30, no 2, p. 265-276Article in journal (Refereed)
    Abstract [en]

    RATIONALE: Mass spectrometry has shown itself to be the most efficient tool for the sequencing of peptides. However, de novo sequencing of novel natural peptides is significantly more challenging in comparison with the same procedure applied for the tryptic peptides. To reach the goal in this case it is essential to select the most efficient methods of triggering fragmentation and combine all the possible complementary techniques. METHODS: Collision-induced dissociation (CID), high-energy collision dissociation (HCD), and electron-transfer dissociation (ETD) tandem mass spectra recorded with a LTQ Orbitrap Velos instrument were used for the elucidation of the sequence of the natural non-tryptic peptides from the skin secretion of Rana latastei. Manual interpretation of the spectra was applied. RESULTS: The combined approach using CID, HCD, and ETD tandem mass spectra of the multiprotonated peptides in various charge states, as well as of their proteolytic fragments, allowed the sequences of seven novel peptides from the skin secretion of Rana latastei to be established. CONCLUSIONS: Manual mass spectrometry sequencing of natural non-tryptic peptides from the skin secretion of Rana latastei provided the opportunity to work successfully with these species and demonstrated once again its advantage over automatic approaches.

  • 335.
    Samgina, Tatiana Yu
    et al.
    Moscow MV Lomonosov State Univ, Dept Organ Chem, Moscow 119991, Russia..
    Tolpina, Miriam I.
    Moscow MV Lomonosov State Univ, Dept Organ Chem, Moscow 119991, Russia..
    Hakalehto, Elias
    Univ Eastern Finland, Dept Environm Sci, POB 1627, Kuopio 70211, Finland..
    Artemenko, Konstantin A.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Lebedev, Albert T.
    Moscow MV Lomonosov State Univ, Dept Organ Chem, Moscow 119991, Russia..
    Proteolytic degradation and deactivation of amphibian skin peptides obtained by electrical stimulation of their dorsal glands2016In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 408, no 14, p. 3761-3768Article in journal (Refereed)
    Abstract [en]

    Amphibians are among the oldest creatures on our planet. Their only defensive weapon efficient against microorganisms and predators involves their skin secretion. The wide range of biological activities of the peptides in the skin secretion of amphibians makes these compounds rather interesting for generation of prospective pharmaceuticals. The first step in studying these molecules requires their structures to be established. Mass spectrometry is the most powerful tool for this purpose. The sampling and sample preparation stages preceding mass spectrometry experiments appear to be rather crucial. The results obtained here demonstrate that these preparation procedures might lead to partial or complete loss of the bioactive peptides in the secretion. Five minutes in water was enough to completely destroy all of the bioactive peptides in the skin secretion of the marsh frog (Rana ridibunda); even immediate addition of methanol to the water solution of the peptides did not prevent partial destruction. Concerted effort should be directed towards development of the most efficient procedure to keep the secreted peptides intact.

  • 336. Samgina, Tatyana Yu.
    et al.
    Gorshkov, Vladimir A.
    Artemenko, Konstantin A.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Vorontsov, Egor A.
    Klykov, Oleg V.
    Ogourtsov, Sergey V.
    Zubarev, Roman A.
    Lebedev, Albert T.
    LC-MS/MS with 2D mass mapping of skin secretions' peptides as a reliable tool for interspecies identification inside Rana esculenta complex2012In: Peptides, ISSN 0196-9781, E-ISSN 1873-5169, Vol. 34, no 2, p. 296-302Article in journal (Refereed)
    Abstract [en]

    Identification of species constituting Rana esculenta complex represents a certain problem as two parental species Rana ridibunda and Rana lessonae form their hybrid R. esculenta, while external signs and sizes of the members of this complex are intersected. However the composition of skin secretion consisting mainly of peptides is different for the species of the complex. LC-MS/MS is an ideal analytical tool for the quantitative and qualitative analysis of these peptides. The results covering elemental composition of these peptides, their levels in the secretion, as well as their belonging to a certain family of peptides may be visualized by means of 2D mass maps. The proposed approach proved itself to be a perspective tool for the reliable identification of all 3 species constituting R. esculenta complex. Easy distinguishing between the species may be achieved using 2D maps as fingerprints. Besides this approach may be used to study hybridogenesis and mechanisms of hemiclonal transfer of genetic information, when rapid and reliable identification of species involved in the process is required.

  • 337. Samgina, Tatyana Yu
    et al.
    Vorontsov, Egor A
    Gorshkov, Vladimir A
    Artemenko, Konstantin A
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Zubarev, Roman A
    Lebedev, Albert T
    Mass spectrometric de novo sequencing of natural non-tryptic peptides: comparing peculiarities of collision-induced dissociation (CID) and high energy collision dissociation (HCD)2014In: Rapid Communications in Mass Spectrometry, ISSN 0951-4198, E-ISSN 1097-0231, Vol. 28, no 23, p. 2595-2604Article in journal (Refereed)
    Abstract [en]

    RATIONALE: Mass spectrometry has shown itself as the most efficient tool for the sequencing of peptides. However, de novo sequencing of novel natural peptides is significantly more challenging in comparison with the same procedure applied for the tryptic peptides. To reach the goal in this case it is essential to select the most useful methods of triggering fragmentation and combine complementary techniques.

    METHODS: Comparison of low-energy collision-induced dissociation (CID) and higher energy collision-induced dissociation (HCD) modes for sequencing of the natural non-tryptic peptides with disulfide bonds and/or several proline residues in the backbone was achieved using an LTQ FT Ultra Fourier transform ion cyclotron resonance (FTICR) mass spectrometer (Thermo Fisher Scientific, Bremen, Germany) equipped with a 7 T magnet and an LTQ Orbitrap Velos ETD (Thermo Fisher Scientific, Bremen, Germany) instrument. Peptide fractions were obtained by high-performance liquid chromatography (HPLC) separation of frog skin secretion samples from ten species of Rana temporaria, caught in the Kolomna district of Moscow region (Russia).

    RESULTS: HCD makes the b/y series longer and more pronounced, thus increasing sequence coverage. Fragment ions due to cleavages at the C-termini of proline residues make the sequencing more reliable and may be used to detect missed cleavages in the case of tryptic peptides. Another HCD peculiarity involves formation of pronounced inner fragment ions (secondary yn bm ion series formed from the abundant primary y-ions). Differences in de novo sequencing of natural non-tryptic peptides with CID and HCD, involving thorough manual expert interpretation of spectra and two automatic sequencing algorithms, are discussed.

    CONCLUSIONS: Although HCD provides better results, a combination of CID and HCD data may notably increase reliability of de novo sequencing. Several pairs of b2 /a2 -ions may be formed in HCD, complicating the spectra. Automatic de novo sequencing with the available programs remains less efficient than the manual one, independently of the collision energy.

  • 338.
    Sandh, Gustaf
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Ramström, Margareta
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Stensjö, Karin
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Analysis of the early heterocyst Cys-proteome in the multicellular cyanobacterium Nostoc punctiforme reveals novel insights into the division of labor within diazotrophic filaments2014In: BMC Genomics, ISSN 1471-2164, E-ISSN 1471-2164, Vol. 15, article id 1064Article in journal (Refereed)
    Abstract [en]

    BACKGROUND:

    In the filamentous cyanobacterium Nostoc punctiforme ATCC 29133, removal of combined nitrogen induces the differentiation of heterocysts, a cell-type specialized in N2 fixation. The differentiation involves genomic, structural and metabolic adaptations. In cyanobacteria, changes in the availability of carbon and nitrogen have also been linked to redox regulated posttranslational modifications of protein bound thiol groups. We have here employed a thiol targeting strategy to relatively quantify the putative redox proteome in heterocysts as compared to N2-fixing filaments, 24 hours after combined nitrogen depletion. The aim of the study was to expand the coverage of the cell-type specific proteome and metabolic landscape of heterocysts.

    RESULTS:

    Here we report the first cell-type specific proteome of newly formed heterocysts, compared to N2-fixing filaments, using the cysteine-specific selective ICAT methodology. The data set defined a good quantitative accuracy of the ICAT reagent in complex protein samples. The relative abundance levels of 511 proteins were determined and 74% showed a cell-type specific differential abundance. The majority of the identified proteins have not previously been quantified at the cell-type specific level. We have in addition analyzed the cell-type specific differential abundance of a large section of proteins quantified in both newly formed and steady-state diazotrophic cultures in N. punctiforme. The results describe a wide distribution of members of the putative redox regulated Cys-proteome in the central metabolism of both vegetative cells and heterocysts of N. punctiforme.

    CONCLUSIONS:

    The data set broadens our understanding of heterocysts and describes novel proteins involved in heterocyst physiology, including signaling and regulatory proteins as well as a large number of proteins with unknown function. Significant differences in cell-type specific abundance levels were present in the cell-type specific proteomes of newly formed diazotrophic filaments as compared to steady-state cultures. Therefore we conclude that by using our approach we are able to analyze a synchronized fraction of newly formed heterocysts, which enabled a better detection of proteins involved in the heterocyst specific physiology.

  • 339.
    Sandin, Peter
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Department of Chemistry, University of Florence and CSGI, Florence, Italy.
    Bombelli, Francesca Baldelli
    Centro Europeo di Nanomedicina c/o Dipartimento di Chimica,Materiali e Ingegneria Chimica G. Natta, Politecnico di Milano, Italy AND School of Pharmacy, University of East Anglia, Norwich, UK.
    Castroflorio, Benedetta
    Department of Chemistry, University of Florence and CSGI, Florence, Italy.
    Muller, Christoph
    Heidelberg Pharma GmbH, Schriesheimer Strasse 101, 68526 Ladenburg, Germany.
    Obermeier, Jurgen
    Heidelberg Pharma GmbH, Schriesheimer Strasse 101, 68526 Ladenburg, Germany.
    Karlsson, Göran
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Edwards, Katarina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Baglioni, Piero
    Department of Chemistry, University of Florence and CSGI, Florence, Italy.
    Berti, Debora
    Department of Chemistry, University of Florence and CSGI, Florence, Italy.
    Diastereoselective self-assembly of clofarabine lipids2014In: New Journal of Chemistry, ISSN 1144-0546, E-ISSN 1369-9261, Vol. 38, no 11, p. 5247-5253Article in journal (Refereed)
    Abstract [en]

    Clofarabine is a nucleosidic chemotherapeutic approved for the treatment of acute lymphoblastic leukemia, currently undergoing clinical trials for the treatment of solid tumors. Like for many others, lipidic derivatization of this drug improves pharmacokinetics and relieves the heavy side effects. Since the self-assembly pattern can modulate the bioactivity profile, a precise knowledge of the aggregation behavior of these nucleolipids and of the microstructure of the aggregates is central to design formulations that efficiently provide sufficient bioavailability. In this contribution we investigate the self-assembly behavior of two Clofarabine dioxy-ether derivatives, the diastereomers (1-2S and 1-2R). These clofarabine lipid derivatives showed an unexpected diastereoselective self-assembly effect, which we have monitored by observing the time evolution of self-assemblies and their microstructural response to thermal treatment. Dynamic Light Scattering and Circular Dichroism provide an ensemble of results which correlate with the occurrence of a hierarchical association of wormlike aggregates, imaged using Electron Microcopy. A strikingly different behavior for the two diastereomers was observed. This behavior can be crucial for the different bioavailability observed in vivo.

  • 340.
    Santos-Neto, Alvaro J.
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Markides, Karin
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Sjöberg, Per
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Lancas, Fernando M.
    Capillary Column Switching Restricted-Access Media-Liquid Chromatography-Electrospray Ionization-Tandem Mass Spectrometry System for Simultaneous and Direct Analysis of Drugs in Biofluids2007In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 79, no 16, p. 6359-6367Article in journal (Refereed)
    Abstract [en]

    Capillary online restricted-access media-liquid chromatography-electrospray ionization-tandem mass spectrometry (RAM-LC-ESI-MS/MS) for direct analysis of drugs and metabolites spiked in biological fluids was developed. Using a column switching setup it was possible to perform effective sample preparation and analysis of raw biological fluids (plasma and urine) without matrix effects in the electrospray mass spectrometric detection step. The peak focusing efficiency of the extraction column was more effective in backflush compared to foreflush mode. The system was able to concentrate diminished samples of polar drugs and their metabolites reaching quantifiable results as low as 1 ng/mL utilizing a sample volume of only 333 nL of biofluids. New column hardware was developed to circumvent clogging problems experienced with plasma injections. The glass fiber filter frit, which is commonly used, was replaced with a short piece of 20 μm i.d. fused silica capillary. The extraction columns were able to handle up to 60 injections and showed a high loading capacity, making the saturation of the MS detector the limiting factor on the linear dynamic range. The simultaneous separation and detection of 10 drugs and metabolites was obtained in 8 min of analysis, including the online sample preparation and enrichment step.

  • 341.
    Sargsyan, Ernest
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Artemenko, Konstantin A.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Manukyan, Levon
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bergsten, Peter
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Oleate protects beta cells from the toxic effect of palmitate by restoring pro-survival pathways of the ER stress response2016In: Diabetologia, ISSN 0012-186X, E-ISSN 1432-0428, Vol. 59, p. S212-S213Article in journal (Refereed)
  • 342.
    Sargsyan, Ernest
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Artemenko, Konstantin
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Manukyan, Levon
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Bergsten, Peter
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Oleate protects beta-cells from the toxic effect of palmitate by activating pro-survival pathways of the ER stress response2016In: Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, ISSN 1388-1981, E-ISSN 1879-2618, Vol. 1861, no 9, p. 1151-1160Article in journal (Refereed)
    Abstract [en]

    Long-term exposure of beta cells to saturated fatty acids impairs insulin secretion and increases apoptosis. In contrast, unsaturated fatty acids protect beta-cells from the long-term negative effects of saturated fatty acids. We aimed to identify the mechanisms underlying this protective action of unsaturated fatty acids. To address the aim, insulin-secreting MINE cells were exposed to palmitate in the absence or presence of oleate and analyzed by using nano-LC MS/MS based proteomic approach. Important findings were validated by using alternative approaches. Proteomic analysis identified 34 proteins differentially expressed in the presence of palmitate compared to control samples. These proteins play a role in insulin processing, mitochondrial function, metabolism of biomolecules, calcium homeostasis, exocytosis, receptor signaling, ER protein folding, antioxidant activity and anti-apoptotic function. When oleate was also present during culture, expression of 15 proteins was different from the expression in the presence of palmitate alone. Most of the proteins affected by oleate are targets of the ER stress response and play a pro-survival role in beta cells such as protein folding and antioxidative defence. We conclude that restoration of pro-survival pathways of the ER stress response is a major mechanism underlying the protective effect of unsaturated fatty acids in beta-cells treated with saturated fatty acids.

  • 343.
    Sari, Gulce
    et al.
    Marmara Univ, Fac Med, Med Biochem, Istanbul, Turkey..
    Musuruni, Sravani
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Wicher, Grzegorz
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Neuro-Oncology.
    Mi, Jia
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Karademir, Betul
    Marmara Univ, Fac Med, Med Biochem, Istanbul, Turkey..
    Heat shock proteins in proteasome inhibitor related neuropathy2015In: Free Radical Biology & Medicine, ISSN 0891-5849, E-ISSN 1873-4596, Vol. 86, no Suppl. 1, p. S27-S27Article in journal (Other academic)
  • 344.
    Sari-Kaplan, Gulce
    et al.
    Marmara Univ, Dept Biochem, Fac Med, Genet & Metab Dis Res & Invest Ctr, Istanbul, Turkey.;Okan Univ, Dept Genet & Bioengn, Fac Engn, Istanbul, Turkey..
    Musunuri, Sravani
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Wicher, Grzegorz
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Neuro-Oncology.
    Jung, Tobias
    German Inst Human Nutr Potsdam Rehbrucke, Dept Mol Toxicol, Potsdam, Germany..
    Mi, Jia
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Hacioglu-Bay, Husniye
    Marmara Univ, Fac Med, Dept Anat, Istanbul, Turkey..
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Grune, Tilman
    German Inst Human Nutr Potsdam Rehbrucke, Dept Mol Toxicol, Potsdam, Germany..
    Karademir, Betul
    Marmara Univ, Dept Biochem, Fac Med, Genet & Metab Dis Res & Invest Ctr, Istanbul, Turkey..
    Peripheral neuropathy as the side effect of proteasome inhibitors bortezomib and carfilzomib2016In: Free Radical Biology & Medicine, ISSN 0891-5849, E-ISSN 1873-4596, Vol. 96, p. S17-S17Article in journal (Other academic)
  • 345.
    Sawadjoon, Supaporn
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Orthaber, Andreas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Sjöberg, Per J. R.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Eriksson, Lars
    Samec, Joseph S. M.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Equilibrium Study of Pd(dba)2 and P(OPh)3 in the Pd-Catalyzed Allylation of Aniline by Allyl Alcohol2014In: Organometallics, ISSN 0276-7333, E-ISSN 1520-6041, Vol. 33, no 1, p. 249-253Article in journal (Refereed)
    Abstract [en]

    Reaction of Pd(dba)2 and P(OPh)3 shows a unique equilibrium where the Pd[P(OPh)3]3 complex is favored over both Pd(dba)[P(OPh)3]2 and Pd[P(OPh)3]4 complexes at room temperature. At a lower temperature, Pd[P(OPh)3]4 becomes the most abundant complex in solution. X-ray studies of Pd[P(OPh)3]3 and Pd(dba)[P(OPh)3]2 complexes show that both complexes have a trigonal geometry with a Pd–P distance of 2.25 Å due to the π-acidity of the phosphite ligand. In solution, pure Pd(dba)[P(OPh)3]2 complex equilibrates to the favored Pd[P(OPh)3]3 complex, which is the most stable complex of those studied, and also forms the most active catalytic species. This catalyst precursor dissociates one ligand to give the reactive Pd[P(OPh)3]2, which performs an oxidative addition of nonmanipulated allyl alcohol to generate the π-allyl-Pd[P(OPh)3]2 intermediate according to ESI-MS studies.

  • 346.
    Sawadjoon, Supaporn
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Synthetical Organic Chemistry.
    Sjöberg, Per J R
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Orthaber, Andreas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
    Matsson, Olle
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Physical Organic Chemistry.
    Samec, Joseph S M
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Synthetical Organic Chemistry.
    Mechanistic Insights into the Pd-Catalyzed Direct Amination of Allyl Alcohols: Evidence for an Outer-sphere Mechanism Involving a Palladium Hydride Intermediate2014In: Chemistry - A European Journal, ISSN 0947-6539, E-ISSN 1521-3765, Vol. 20, no 6, p. 1520-1524Article in journal (Refereed)
    Abstract [en]

    The mechanism of direct amination of allyl alcohol by a palladium triphenylphosphite complex has been explored. Labelling studies show that the reaction proceeds through a π-allylpalladium intermediate. A second-order dependence of reaction rate on allyl alcohol concentration was observed. Kinetic isotope effect studies and ESI-MS studies are in agreement with a reaction proceeding through a palladium hydride intermediate in which both O-H bond and C-O bond cleavages are involved in rate-determining steps. A stereochemical study supports an outer-sphere nucleophilic attack of the π-allylpalladium intermediate giving complete chiral transfer from starting material to product.

  • 347.
    Scholtysek, Peggy
    et al.
    Institute of Chemistry - Physical Chemistry, Martin-Luther-University Halle-Wittenberg, Germany.
    Achilles, Anja
    Institute of Physics - NMR, Martin-Luther-University Halle-Wittenberg, Germany.
    Hoffmann, Claudia-Viktoria
    Institute of Chemistry - Physical Chemistry, Martin-Luther-University Halle-Wittenberg, Germany.
    Lechner, Bob-Dan
    Institute of Chemistry - Physical Chemistry, Martin-Luther-University Halle-Wittenberg, Germany.
    Meister, Annette
    ZIK HALOmem, Martin-Luther-University Halle-Wittenberg, Germany.
    Tschierske, Carsten
    Institute of Chemistry - Organic Chemistry, Martin-Luther-University Halle-Wittenberg, Germany.
    Saalwächter, Kay
    Institute of Physics - NMR, Martin-Luther-University Halle-Wittenberg, Germany.
    Edwards, Katarina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Blume, Alfred
    Institute of Chemistry - Physical Chemistry, Martin-Luther-University Halle-Wittenberg, Germany.
    A T-Shaped Amphiphilic Molecule Forms Closed Vesicles in Water and Bicelles in Mixtures with a Membrane Lipid2012In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 116, no 16, p. 4871-4878Article in journal (Refereed)
    Abstract [en]

    The T-shaped amphiphilic molecule A6/6 forms a columnar hexagonal liquid-crystalline phase between the crystalline and the isotropic liquid when studied in bulk (Chen et al., 2005). Because of the hydrophilic and flexible oligo(oxyethylene) side chain terminated by a 1-acylamino-1-deoxy-d-sorbitol moiety attached to a rigid terphenyl core with terminal hexyloxy alkyl chains, it was expected that also formation of lyotropic phases could be possible. We therefore studied the behavior of A6/6 in water and also in mixtures with bilayer-forming phospholipids, such as dipalmitoyl-phosphatidylcholine (DPPC), using differential scanning calorimetry (DSC), transmission electron microscopy (TEM), cryo-transmission electron microscopy (cryo-TEM), dynamic light scattering (DLS), and solid-state nuclear magnetic resonance (ssNMR). DSC showed for the pure A6/6 suspended in water a phase transition at ca. 23 °C. TEM and cryo-TEM showed vesicular as well as layered structures for pure A6/6 in water below and above this phase transition. By atomic force microscopy (AFM), the thickness of the layer was found to be 5?6 nm. This leads to a model for a bilayer formed by A6/6 with the laterally attached polar side chains shielding the hydrophobic layer built up by the terphenyl core with the terminal alkyl chains of the molecules. For DPPC:A6/6 mixtures (10:1), the DSC curves indicated a stabilization of the lamellar gel phase of DPPC. Negative staining TEM and cryo-TEM images showed planar bilayers with hexagonal morphology and diameters between 50 and 200 nm. The hydrodynamic radius of these aggregates in water, investigated by dynamic light scattering (DLS) as a function of time and temperature, did not change indicating a very stable aggregate structure. The findings lead to the proposition of a new bicellar structure formed by A6/6 with DPPC. In this model, the bilayer edges are covered by the T-shaped amphiphilic molecules preventing very effectively the aggregation to larger structures.

  • 348. Schutzer, Steven E.
    et al.
    Angel, Thomas E.
    Liu, Tao
    Schepmoes, Athena A.
    Xie, Fang
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Vecsei, Laszlo
    Zadori, Denes
    Camp, David G., II
    Holland, Bart K.
    Smith, Richard D.
    Coyle, Patricia K.
    Gray Matter Is Targeted in First-Attack Multiple Sclerosis2013In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 8, no 9, p. e66117-Article in journal (Refereed)
    Abstract [en]

    The cause of multiple sclerosis (MS), its driving pathogenesis at the earliest stages, and what factors allow the first clinical attack to manifest remain unknown. Some imaging studies suggest gray rather than white matter may be involved early, and some postulate this may be predictive of developing MS. Other imaging studies are in conflict. To determine if there was objective molecular evidence of gray matter involvement in early MS we used high-resolution mass spectrometry to identify proteins in the cerebrospinal fluid (CSF) of first-attack MS patients (two independent groups) compared to established relapsing remitting (RR) MS and controls. We found that the CSF proteins in first-attack patients were differentially enriched for gray matter components (axon, neuron, synapse). Myelin components did not distinguish these groups. The results support that gray matter dysfunction is involved early in MS, and also may be integral for the initial clinical presentation.

  • 349.
    Schweizer, Nadine
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Developmental Genetics.
    Viereckel, Thomas
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Functional Pharmacology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Smith-Anttila, Casey J. A.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience.
    Nordenankar, Karin
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Functional Pharmacology.
    Arvidsson, Emma
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Developmental Genetics.
    Mahmoudi, Souha
    Univ Montreal, Fac Pharm, Montreal, PQ H3T 1J4, Canada..
    Zampera, Andre
    Oramacell, F-75006 Paris, France..
    Jonsson, Hanna Wärner
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Levesque, Daniel
    Univ Montreal, Fac Pharm, Montreal, PQ H3T 1J4, Canada..
    Konradsson-Geuken, Åsa
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Andersson, Malin
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Dumas, Sylvie
    Oramacell, F-75006 Paris, France..
    Wallén-Mackenzie, Åsa
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Reduced Vglut2/Slc17a6 Gene Expression Levels throughout the Mouse Subthalamic Nucleus Cause Cell Loss and Structural Disorganization Followed by Increased Motor Activity and Decreased Sugar Consumption2016In: ENEURO, ISSN 2373-2822, Vol. 3, no 5, article id UNSP e0264Article in journal (Refereed)
    Abstract [en]

    The subthalamic nucleus (STN) plays a central role in motor, cognitive, and affective behavior. Deep brain stimulation (DBS) of the STN is the most common surgical intervention for advanced Parkinson's disease (PD), and STN has lately gained attention as target for DBS in neuropsychiatric disorders, including obsessive compulsive disorder, eating disorders, and addiction. Animal studies using STN-DBS, lesioning, or inactivation of STN neurons have been used extensively alongside clinical studies to unravel the structural organization, circuitry, and function of the STN. Recent studies in rodent STN models have exposed different roles for STN neurons in reward-related functions. We have previously shown that the majority of STN neurons express the vesicular glutamate transporter 2 gene (Vglut2/Slc17a6) and that reduction of Vglut2 mRNA levels within the STN of mice [conditional knockout (cKO)] causes reduced postsynaptic activity and behavioral hyperlocomotion. The cKO mice showed less interest in fatty rewards, which motivated analysis of reward-response. The current results demonstrate decreased sugar consumption and strong rearing behavior, whereas biochemical analyses show altered dopaminergic and peptidergic activity in the striatum. The behavioral alterations were in fact correlated with opposite effects in the dorsal versus the ventral striatum. Significant cell loss and disorganization of the STN structure was identified, which likely accounts for the observed alterations. Rare genetic variants of the human VGLUT2 gene exist, and this study shows that reduced Vglut2/Slc17a6 gene expression levels exclusively within the STN of mice is sufficient to cause strong modifications in both the STN and the mesostriatal dopamine system.

  • 350.
    Shepherd, Tyson R
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology. MIT, Dept Biol Engn, Cambridge, MA 02139 USA..
    Du, Liping
    Vanderbilt Univ, Med Ctr, Dept Pharmacol, Nashville, TN 37232 USA.;Vanderbilt Univ, Med Ctr, Ctr Quantitat Sci, Nashville, TN 37232 USA..
    Liljeruhm, Josefine
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology.
    Samudyata,
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology.
    Wang, Jinfan
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology. Stanford Univ, Sch Med, Dept Biol Struct, Stanford, CA 94305 USA..
    Sjödin, Marcus O.D.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Swedish Toxicol Sci Res Ctr Swetox, S-15136 Sodertalje, Sweden..
    Wetterhall, Magnus
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. GE Healthcare Biosci, Life Sci, S-75184 Uppsala, Sweden..
    Yomo, Tetsuya
    East China Normal Univ, Inst Biol & Informat Sci, Sch Comp Sci & Software Engn, Sch Life Sci, Shanghai 200062, Peoples R China..
    Forster, Anthony C.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology. Vanderbilt Univ, Med Ctr, Dept Pharmacol, Nashville, TN 37232 USA..
    De novo design and synthesis of a 30-cistron translation-factor module2017In: Nucleic Acids Research, ISSN 0305-1048, E-ISSN 1362-4962, Vol. 45, no 18, p. 10895-10905Article in journal (Refereed)
    Abstract [en]

    Two of the many goals of synthetic biology are synthesizing large biochemical systems and simplifying their assembly. While several genes have been assembled together by modular idempotent cloning, it is unclear if such simplified strategies scale to very large constructs for expression and purification of whole pathways. Here we synthesize from oligodeoxyribonucleotides a completely de-novo-designed, 58-kb multigene DNA. This BioBrick plasmid insert encodes 30 of the 31 translation factors of the PURE translation system, each His-tagged and in separate transcription cistrons. Dividing the insert between three high-copy expression plasmids enables the bulk purification of the aminoacyl-tRNA synthetases and translation factors necessary for affordable, scalable reconstitution of an in vitro transcription and translation system, PURE 3.0.

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