Change search
Refine search result
1 - 15 of 15
CiteExportLink to result list
Permanent link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Rows per page
  • 5
  • 10
  • 20
  • 50
  • 100
  • 250
Sort
  • Standard (Relevance)
  • Author A-Ö
  • Author Ö-A
  • Title A-Ö
  • Title Ö-A
  • Publication type A-Ö
  • Publication type Ö-A
  • Issued (Oldest first)
  • Issued (Newest first)
  • Created (Oldest first)
  • Created (Newest first)
  • Last updated (Oldest first)
  • Last updated (Newest first)
  • Disputation date (earliest first)
  • Disputation date (latest first)
  • Standard (Relevance)
  • Author A-Ö
  • Author Ö-A
  • Title A-Ö
  • Title Ö-A
  • Publication type A-Ö
  • Publication type Ö-A
  • Issued (Oldest first)
  • Issued (Newest first)
  • Created (Oldest first)
  • Created (Newest first)
  • Last updated (Oldest first)
  • Last updated (Newest first)
  • Disputation date (earliest first)
  • Disputation date (latest first)
Select
The maximal number of hits you can export is 250. When you want to export more records please use the Create feeds function.
  • 1.
    Bailly-Chouriberry, Ludovic
    et al.
    Laboratoire des Courses Hippiques (LCH), France.
    Cormant, Florence
    Laboratoire des Courses Hippiques (LCH), France.
    Garcia, Patrice
    Laboratoire des Courses Hippiques (LCH), France.
    Lönnberg, Maria
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Szwandt, Simon
    Thermo Fisher Scientific, Hemel Hempstead, UK.
    Bondesson, Ulf
    Dept. of Chemistry, Environment and Feed Hygiene, The National Veterinary Institute (SVA), Uppsala, Sweden.
    Popot, Marie-Agnes
    Laboratoire des Courses Hippiques (LCH), France.
    Bonnaire, Yves
    Laboratoire des Courses Hippiques (LCH), France.
    A new analytical method based on anti-EPO monolith column and LC-FAIMS-MS/MS for the detection of rHuEPOs in horse plasma and urine samples2012In: The Analyst, ISSN 0003-2654, E-ISSN 1364-5528, Vol. 137, no 10, p. 2445-2453Article in journal (Refereed)
    Abstract [en]

    Recombinant human erythropoietin (rHuEPO) is a 30-34 kDa glycoprotein banned by the racing authorities. For some years this molecule has been detected in race horses in USA and in Europe, and even in racing camels. Although direct methods to differentiate horse endogenous EPO and rHuEPO have been developed either by LC-MS/MS or by isoelectric focusing (IEF) with double-blotting, the short confirmation time of such prohibited hormone in plasma remains a problem for horseracing doping control laboratories. In order to improve the rHuEPOs confirmation process in horse plasma or urine in terms of reliability and delay, a small anti-EPO monolith membrane contained in a disposable column (anti-EPO monolith column) has been successfully used and validated (n = 10). This new sample preparation, combined with LC-FAIMS-MS/MS, has been performed on plasma and urine samples collected from one horse which received an Eprex[registered sign] treatment during six consecutive days and a second one with a single injection of Aranesp[registered sign]. This inventive technology allowed the possibility to confirm the presence of rHuEPO within one day with a limit of detection validated for both urine and plasma at 250 pg mL-1 by means of a disposable, ready to use immunoaffinity column. The lower limit of detection (LLOD) obtained for each matrix was 100 pg mL-1. These results provide an important improvement for rHuEPO doping control in horseracing especially the possibility to confirm these banned molecules in both matrices, urine and plasma, with a confidence of two specific target peptides.

  • 2. Dehnes, Yvette
    et al.
    Lamon, Severine
    Lönnberg, Maria
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry.
    Erythropoietin (EPO) immunoaffinity columns-A powerful tool for purifying EPO and its recombinant analogues2010In: Journal of Pharmaceutical and Biomedical Analysis, ISSN 0731-7085, E-ISSN 1873-264X, Vol. 53, no 4, p. 1028-1032Article in journal (Refereed)
    Abstract [en]

    The sample preparation method preceding the urinary erythropoietin (EPO) doping test is based on several concentration and ultrafiltration steps. In order to improve the quality of isoelectric focusing (IEF) gel results and therefore, the sensitivity of the EPO test, new sample preparation methods relying on affinity purification were recently proposed. This article focuses on the evaluation and validation of disposable immunoaffinity columns targeting both endogenous and recombinant EPO molecules in two World Anti-Doping Agency (WADA) accredited anti-doping laboratories. The use of the columns improved the resolution of the IEF profiles considerably when compared with the classical ultrafiltration method, and the columns' ability to ensure the isoform integrity of the endogenous and exogenous EPO molecules was confirmed. Immunoaffinity columns constitute therefore a potent and reliable tool for the preparation of urine samples and their use will significantly improve the sensitivity and specificity of the actual urinary EPO test.

  • 3.
    Emami Khoonsari, Payam
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Cancer Pharmacology and Computational Medicine.
    Haggmark, Anna
    KTH Royal Inst Technol, Sch Biotechnol, Affin Prote, Sci Life Lab, Stockholm, Sweden..
    Lönnberg, Maria
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Mikus, Maria
    KTH Royal Inst Technol, Sch Biotechnol, Affin Prote, Sci Life Lab, Stockholm, Sweden..
    Kilander, Lena
    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.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Ingelsson, Martin
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Public Health and Caring Sciences, Geriatrics.
    Nilsson, Peter
    KTH Royal Inst Technol, Sch Biotechnol, Affin Prote, Sci Life Lab, Stockholm, Sweden..
    Kultima, Kim
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Cancer Pharmacology and Computational Medicine.
    Shevchenko, Ganna
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala Univ, Dept Chem BMC, Analyt Chem, Uppsala, Sweden..
    Analysis of the Cerebrospinal Fluid Proteome in Alzheimer's Disease2016In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 11, no 3, article id e0150672Article in journal (Refereed)
    Abstract [en]

    Alzheimer's disease is a neurodegenerative disorder accounting for more than 50% of cases of dementia. Diagnosis of Alzheimer's disease relies on cognitive tests and analysis of amyloid beta, protein tau, and hyperphosphorylated tau in cerebrospinal fluid. Although these markers provide relatively high sensitivity and specificity for early disease detection, they are not suitable for monitor of disease progression. In the present study, we used label-free shotgun mass spectrometry to analyse the cerebrospinal fluid proteome of Alzheimer's disease patients and non-demented controls to identify potential biomarkers for Alzheimer's disease. We processed the data using five programs (DecyderMS, Maxquant, OpenMS, PEAKS, and Sieve) and compared their results by means of reproducibility and peptide identification, including three different normalization methods. After depletion of high abundant proteins we found that Alzheimer's disease patients had lower fraction of low-abundance proteins in cerebrospinal fluid compared to healthy controls (p<0.05). Consequently, global normalization was found to be less accurate compared to using spiked-in chicken ovalbumin for normalization. In addition, we determined that Sieve and OpenMS resulted in the highest reproducibility and PEAKS was the programs with the highest identification performance. Finally, we successfully verified significantly lower levels (p<0.05) of eight proteins (A2GL, APOM, C1QB, C1QC, C1S, FBLN3, PTPRZ, and SEZ6) in Alzheimer's disease compared to controls using an antibody-based detection method. These proteins are involved in different biological roles spanning from cell adhesion and migration, to regulation of the synapse and the immune system.

  • 4. Franco Fraguas, L
    et al.
    Carlsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Lönnberg, Maria
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Lectin affinity chromatography as a tool to differentiate endogenous and recombinant erythropoietins2008In: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 1212, no 1-2, p. 82-88Article in journal (Refereed)
    Abstract [en]

    This work exploits the combination of the lectin affinity chromatography (LAC) with an ultra-sensitive immunochromatographic assay to differentiate several types of erythropoietin (EPO). The chromatographic behaviours of different commercial types of recombinant human EPO (rhEPO), EPO analogues (Aranesp) and urine human EPO (uhEPO) from healthy individuals on eight lectin-Sepharose columns, have been worked out. Results show that when using wheat germ agglutinin (WGA)-Sepharose columns, a careful desorption regime starting with very low concentration (2mM) of the competitive sugar N-acetylglucosamine (GlcNAc) makes it possible to efficiently distinguish endogenous EPO from recombinant EPO and EPO analogues.

  • 5. Franco Fraguas, Laura
    et al.
    Carlsson, Jan
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Lönnberg, Maria
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Lectin Affinity Chromatography as a Tool to Differentiate Erythropoietin (EPO) and its analogues: abstract2004In: Trends in Glycoscience and Glycotechnology, Vol. 16, p. 63-Article in journal (Refereed)
  • 6.
    Lönnberg, Maria
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Andrén, Maria
    MAIIA Diagnostics, Uppsala Sweden.
    Birgegård, Gunnar
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Haematology.
    Drevin, Malin
    MAIIA Diagnostics, Uppsala Sweden.
    Garle, Mats
    Doping Control Laboratory, Karolinska University Hospital, Stockholm Sweden.
    Carlsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    Rapid detection of erythropoiesis-stimulating agents in urine and serum2012In: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 420, no 2, p. 101-114Article in journal (Refereed)
    Abstract [en]

    A rapid and easy-to-use test kit, EPO WGA MAIIA, which can be used for distinguishing various endogenous human erythropoietins (hEPO) and several recombinant hEPOs and EPO analogues, has been evaluated. The test is based on chromatographic separation of the glycosylated isoforms of EPO using wheat germ agglutinin (WGA), and a sensitive immunoassay utilizing anti-EPO carbon black nanostrings and image scanning for quantification. All the reactions take place along the porous layer of a lateral flow micro-column containing WGA and anti-EPO zones. The presence of molecules resembling hEPO, like Mircera, was detected by the aberrant affinity interaction with the antibody zone on the strip. It was possible to distinguish nine recombinant hEPO expressed in hamster and human cell-lines, and also Aranesp and Mircera, from endogenous urine hEPO. The required amount of EPO in the samples, a few pg, is very low compared to other methods for EPO isoform identification. This EPO isoform determination method opens the possibility to monitor recombinant EPO therapy for clinical research and seems to be a valuable candidate to the arsenal of EPO doping control tests.

  • 7.
    Lönnberg, Maria
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bondesson, Ulf
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Analytical Pharmaceutical Chemistry.
    Cormant, Florence
    L.C.H., Laboratoire des Courses Hippiques, France.
    Garcia, Patrice
    L.C.H., Laboratoire des Courses Hippiques, France.
    Bonnaire, Yves
    L.C.H., Laboratoire des Courses Hippiques, France.
    Carlsson, Jan
    MAIIA Diagnostics, Uppsala, Sweden.
    Popot, Marie-Agnes
    L.C.H., Laboratoire des Courses Hippiques, France.
    Rollborn, Niclas
    MAIIA Diagnostics, Uppsala, Sweden.
    Råsbo, Kristina
    Bailly-Chouriberry, Ludovic
    L.C.H., Laboratoire des Courses Hippiques, France.
    Detection of recombinant human EPO administered to horses using MAIIA lateral flow isoform test2012In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 403, no 6, p. 1619-1628Article in journal (Refereed)
    Abstract [en]

    Doping of horses with recombinant human erythropoietin (rHuEPO) to illegally enhance their endurance capacity in horseracing has been reported during the last years. This leads to increased blood viscosity which can result in sudden death and is of concern for the horse welfare. Additionally, the horse can start production of rHuEPO antibodies, which cross-reacts with endogenous equine EPO and can lead to severe anaemia and even death. In this study, a novel micro-chromatographic method, EPO WGA MAIIA, has been tested for the capability in plasma and urine samples to detect administration of erythropoiesis-stimulating agents, like the rHuEPO glycoprotein varieties Eprex and Aranesp, to horses. After administration of 40 IU Eprex kg −1 day −1 to seven horses during 6 days, the presence of Eprex in horse plasma was detected up to 2–5 days after last injection. In urine samples collected from two horses, Eprex was detected up to 3 days. A single injection of Aranesp (0.39 μg/kg) was detected up to 9 days in plasma and up to 8 days, the last day of testing, in the urine sample. The LC-FAIMS-MS/MS system, with 1 day reporting time, confirmed the presence of Eprex up to 1 day after last injection for six out of seven horses and the presence of Aranesp up to 5 days after last injection in plasma samples. The MAIIA system showed to be a promising tool with high sensitivity and extremely short reporting time (1 h).

  • 8.
    Lönnberg, Maria
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Carlsson, J
    Chromatographic performance of a thin microporous bed of nitrocellulose2001In: JOURNAL OF CHROMATOGRAPHY B, ISSN 0378-4347, Vol. 763, no 1-2, p. 107-120Article in journal (Refereed)
    Abstract [en]

    Chromatography along thin (125 mum) porous beds of nitrocellulose, layered on top of an polyester backing, shows good separation efficiency with plate heights of 10-20 mum. Flow is controlled by capillary forces and shows low rate variations between the i

  • 9.
    Lönnberg, Maria
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Carlsson, J
    Quantitative detection in the attomole range for immunochromatographic tests by means of a flatbed scanner2001In: ANALYTICAL BIOCHEMISTRY, ISSN 0003-2697, Vol. 293, no 2, p. 224-231Article in journal (Refereed)
    Abstract [en]

    This work describes the use of the combination of carbon black as an antibody label, a membrane-based immunochromatographic device, and a flatbed scanner as a quantitative test system. The scanner detected 0.4-345 ng carbon black/mm(2) on a nitrocellulose

  • 10.
    Lönnberg, Maria
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Carlsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Lab-on-a-chip technology for determination of protein isoform profiles2006In: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 1127, no 1-2, p. 175-182Article in journal (Refereed)
    Abstract [en]

    A novel lab-on-a-chip technique for rapid (<15 min) and quantitative isoform-profile determination is presented. Ion-exchange chromatographic separation of protein-isoforms and a sensitive immunoassay detection are combined in a porous monolith chip. Thin lines of immobilized antibodies are used for specific capturing of target molecules, which can be detected by the reaction with antibodies bound to carbon black nano-strings. The bound carbon black is quantified by the use of an image scanner. As demonstrated with transferrin isoforms, differing only by 0.1 pH unit in their pI, this technology can distinguish minor differences in protein carbohydrate structure and enable specific determination of proteins in a complex environment, requiring only a few picogram of isoform for detection.

  • 11.
    Lönnberg, Maria
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Carlsson Jan,
    Membrane assisted isoform immunoassay - A rapid method for the separation and determination of protein isoforms in an integrated immunoassay2000In: JOURNAL OF IMMUNOLOGICAL METHODS, ISSN 0022-1759, Vol. 246, no 1-2, p. 25-36Article in journal (Refereed)
    Abstract [en]

    Proteins often exist as isoforms with structural microheterogenity due to, for example, small variations in their carbohydrate structure. This can give rise to differences in biological activity. Measurements of low concentrations of such isoforms are usu

  • 12.
    Lönnberg, Maria
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Dehnes, Yvette
    Drevin, Malin
    Garle, Mats
    Lamon, Severine
    Leuenberger, Nicolas
    Quach, Trikien
    Carlsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Rapid affinity purification of erythropoietin from biological samples using disposable monoliths2010In: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 1217, no 45, p. 7031-7037Article in journal (Refereed)
    Abstract [en]

    Identification of post-translational modifications of proteins in biological samples often requires access to preanalytical purification and concentration methods In the purification step high or low molecular weight substances can be removed by size exclusion filters and high abundant proteins can be removed or low abundant proteins can be enriched by specific capturing tools In this paper is described the experience and results obtained with a recently emerged and easy-to-use affinity purification kit for enrichment of the low amounts of EPO found in urine and plasma specimens The kit can be used as a pre-step in the EPO doping control procedure as an alternative to the commonly used ultrafiltration for detecting aberrantly glycosylated isoforms The commercially available affinity purification kit contains small disposable anti-EPO monolith columns (6 mu L volume theta 7 mm length 0 15 mm) together with all required buffers A 24-channel vacuum manifold was used for simultaneous processing of samples The column concentrated EPO from 20 mL urine down to 55 mu L eluate with a concentration factor of 240 times while roughly 997% of non-relevant urine proteins were removed The recoveries of Neorecormon (epoetin beta) and the EPO analogues Aranesp and Mircera applied to buffer were high 76% 67% and 57% respectively The recovery of endogenous EPO from human urine was 65% High recoveries were also obtained when purifying human mouse and equine EPO from serum and human EPO from cerebrospinal fluid Evaluation with the accredited EPO doping control method based on isoelectric focusing (IEF) showed that the affinity purification procedure did not change the isoform distribution for rhEPO Aranesp Mircera or endogenous EPO The kit should be particularly useful for applications in which it is essential to avoid carry-over effects a problem commonly encountered with conventional particle-based affinity columns The encouraging results with EPO propose that similar affinity monoliths with the appropriate antibodies should constitute useful tools for general applications in sample preparation not only for doping control of EPO and other hormones such as growth hormone and insulin but also for the study of post-translational modifications of other low abundance proteins in biological and clinical research and for sample preparation prior to in vitro diagnostics.

  • 13.
    Lönnberg, Maria
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Analytical Chemistry.
    Drevin, Malin
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry.
    Carlsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Physical Chemistry.
    Ultra-sensitive immunochromatographic assay for quantitative determination of erythropoietin2008In: JIM - Journal of Immunological Methods, ISSN 0022-1759, E-ISSN 1872-7905, Vol. 339, no 2, p. 236-244Article in journal (Refereed)
    Abstract [en]

    An ultra-sensitive quantitative EPO (erythropoietin) lateral flow immunochromatographic test with a detection limit of 1.2 fM (10(-15) M), 0.035 ng EPO/L, which is 50-100 times more sensitive than a corresponding enzyme based immunoassay, is presented. In comparison with commercial lateral flow tests for other analytes, like cardiac troponins that also require high sensitivity, the detection limit achieved in the presented test is about three orders of magnitude lower. The thin zone for capture and concentration of the analyte, the carbon black nano-strings used as label and the use of a conventional image scanner for the quantitative determination are the key components that enable the high sensitivity obtained. The convective flow in the lateral flow monolith creates short diffusion distances between immobilised antibody, analyte and labelled antibody thus enhancing the binding efficiency. This rapid and sensitive EPO test procedure can be used both to process hundreds of samples in 1 h and be utilized as a 15-minute dipstick test for single determinations. The technique is demonstrated by measuring EPO in urine. EPO, like many of the other urine proteins, is often found in the urine precipitates and the specimens are therefore treated with a urine precipitate dissolvation buffer before analysis. It is shown that EPO in urine from normal individuals occurs in low concentration in a wide range between 1.7 and 51 ng/L. The concentration is however subjected to a wide variation during the day due to the EPO production variation and the urine concentration by the kidneys. It is also shown that the presented lateral flow device can be used as a miniaturized affinity column to distinguish an analyte (EPO) from its analogue (darbepoetin), directly by comparing the affinity profiles obtained after interaction with the immobilised antibody. The method for measuring the amount of EPO present in urine, the possibility to rapidly check the amount of EPO after a pre-treatment concentration step, and the potential to identify affinity differences between EPO and its analogues should make the presented method a valuable tool in the fight against EPO doping.

  • 14.
    Lönnberg, Maria
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Garle, Mats
    Doping Control Laboratory, Karolinska University Hospital, Stockholm, Sweden.
    Lönnberg, Lina
    Department of Ecology, Swedish University of Agricultural Sciences, Uppsala, Sweden.
    Birgegård, Gunnar
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Haematology.
    Patients with anaemia can shift from kidney to liver production of erythropoietin as shown by glycoform analysis2013In: Journal of Pharmaceutical and Biomedical Analysis, ISSN 0731-7085, E-ISSN 1873-264X, Vol. 81-82, p. 187-192Article in journal (Refereed)
    Abstract [en]

    The primary production site of erythropoietin (EPO) is shifted from the liver to the kidney shortly after birth. Under conditions of lost or reduced kidney production, it is valuable to measure the production capacity of the liver. However, there is a lack of urine or serum based methods that can distinguish endogenous EPO produced in different cell types. Here is presented a method based on chromatographic interaction with the lectin wheat germ agglutinin (WGA) that can distinguish presumably liver-produced EPO, found in anaemic patients receiving epoetin and darbepoetin, from kidney-produced EPO found in healthy individuals.

    All the tested samples from haemodialysis patients with end-stage renal disease showed a presence of liver EPO. In some samples, the liver-produced EPO made up 90–100% of total EPO at a concentration of 8–10 ng/L in urine, which indicates that the liver has a quite high production capacity, although not adequate for the degree of anaemia.

    This glycoform analysis has made it possible to affirm that some anaemic patients can increase their liver-production of EPO. The use of such a method can give better insight into the regulation of non-renal endogenous EPO production, a potential source of EPO intended to replace administration of exogenous EPO.

  • 15.
    Lönnberg, Maria
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Lundby, Carsten
    Center for Integrative Human Physiology (ZIHP), Institute of Physiology, University of Zurich, Switzerland.
    Detection of EPO injections using a rapid lateral flow isoform test2013In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 405, no 30, p. 9685-9691Article in journal (Refereed)
    Abstract [en]

    Misuse of recombinant human erythropoietin (rhEPO) is a major concern in competitive sports, and the implementation of tests allowing for higher detection rates than what current tests are capable of is required. In this study, a novel lateral flow EPO isoform test kit, EPO WGA MAIIA, is evaluated on the basis of plasma and urine samples obtained from eight healthy males in connection with a 28-day rhEPO injection period. rhEPO was injected every other day during the first 14 days of the study, and the method proved to be 100 % effective in detecting rhEPO in the concomitantly obtained samples. Seven days after the last injection, three positive (>99.99 % confidence limit (CL)) subjects were found. When using 99 % CL as the cut-off limit, six of the eight subjects (75 %) were found to be suspected of doping. Samples obtained 14 and 21 days after the last injection showed no detectable trace of rhEPO. A previous study using indirect methods to determine EPO doping on the same samples indicated only that two of the subjects had suspicious values 7-21 days after the last injection. We propose implementing the easy to-use EPO WGA MAIIA test as an initial screening procedure in anti-doping work to (1) increase the detection rate of potential rhEPO doping athletes and (2) allow for a 10- to 20-fold higher analytical rate than what is possible today.

1 - 15 of 15
CiteExportLink to result list
Permanent link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf