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Role of Individual MARK Isoforms in Phosphorylation of Tau at Ser(262) in Alzheimer's Disease
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för immunologi, genetik och patologi, Molekylära verktyg. Uppsala universitet, Science for Life Laboratory, SciLifeLab.
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för immunologi, genetik och patologi, Molekylära verktyg. Uppsala universitet, Science for Life Laboratory, SciLifeLab.
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för immunologi, genetik och patologi, Molekylära verktyg. Uppsala universitet, Science for Life Laboratory, SciLifeLab.
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2013 (engelsk)Inngår i: Neuromolecular medicine, ISSN 1535-1084, E-ISSN 1559-1174, Vol. 15, nr 3, s. 458-469Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The microtubule-affinity regulating kinase (MARK) family consists of four highly conserved members that have been implicated in phosphorylation of tau protein, causing formation of neurofibrillary tangles in Alzheimer's disease (AD). Understanding of roles by individual MARK isoform in phosphorylating tau has been limited due to lack of antibodies selective for each MARK isoform. In this study, we first applied the proximity ligation assay on cells to select antibodies specific for each MARK isoform. In cells, a CagA peptide specifically and significantly inhibited tau phosphorylation at Ser(262) mediated by MARK4 but not other MARK isoforms. We then used these antibodies to study expression levels of MARK isoforms and interactions between tau and individual MARK isoforms in postmortem human brains. We found a strong and significant elevation of MARK4 expression and MARK4-tau interactions in AD brains, correlating with the Braak stages of the disease. These results suggest the MARK4-tau interactions are of functional importance in the progression of AD and the results also identify MARK4 as a promising target for AD therapy.

sted, utgiver, år, opplag, sider
2013. Vol. 15, nr 3, s. 458-469
Emneord [en]
Alzheimer's disease, MARK, Phosphorylation, Proximity ligation, Tau
HSV kategori
Identifikatorer
URN: urn:nbn:se:uu:diva-206553DOI: 10.1007/s12017-013-8232-3ISI: 000322722300002OAI: oai:DiVA.org:uu-206553DiVA, id: diva2:644947
Tilgjengelig fra: 2013-09-02 Laget: 2013-09-02 Sist oppdatert: 2017-12-06bibliografisk kontrollert

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Gu, Gucci JijuanWu, DiBlokzijl, AndriesClasson, ChristinaLandegren, UlfKamali-Moghaddam, Masood
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