Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/106195
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dc.contributor.authorMajd, S.en
dc.contributor.authorPower, J.en
dc.contributor.authorKoblar, S.en
dc.contributor.authorGrantham, H.en
dc.date.issued2016en
dc.identifier.citationEuropean Journal of Neuroscience, 2016; 44(3):1987-1997en
dc.identifier.issn0953-816Xen
dc.identifier.issn1460-9568en
dc.identifier.urihttp://hdl.handle.net/2440/106195-
dc.description.abstractAbnormal tau phosphorylation (p-tau) has been shown after hypoxic damage to the brain associated with traumatic brain injury and stroke. As the level of p-tau is controlled by Glycogen Synthase Kinase (GSK)-3β, Protein Phosphatase 2A (PP2A) and Adenosine Monophosphate Kinase (AMPK), different activity levels of these enzymes could be involved in tau phosphorylation following ischaemia. This study assessed the effects of global brain ischaemia/reperfusion on the immediate status of p-tau in a rat model of cardiac arrest (CA) followed by cardiopulmonary resuscitation (CPR). We reported an early dephosphorylation of tau at its AMPK sensitive residues, Ser(396) and Ser(262) after 2 min of ischaemia, which did not recover during the first two hours of reperfusion, while the tau phosphorylation at GSK-3β sensitive but AMPK insensitive residues, Ser(202) /Thr(205) (AT8), as well as the total amount of tau remained unchanged. Our data showed no alteration in the activities of GSK-3β and PP2A during similar episodes of ischaemia of up to 8 min and reperfusion of up to 2 h, and 4 weeks recovery. Dephosphorylation of AMPK followed the same pattern as tau dephosphorylation during ischaemia/reperfusion. Catalase, another AMPK downstream substrate also showed a similar pattern of decline to p-AMPK, in ischaemic/reperfusion groups. This suggests the involvement of AMPK in changing the p-tau levels, indicating that tau dephosphorylation following ischaemia is not dependent on GSK-3β or PP2A activity, but is associated with AMPK dephosphorylation. We propose that a reduction in AMPK activity is a possible early mechanism responsible for tau dephosphorylation.en
dc.description.statementofresponsibilityShohreh Majd, John H. T. Power, Simon A. Koblar and Hugh J. M. Granthamen
dc.language.isoenen
dc.publisherWiley-Blackwellen
dc.rights© 2016 The Authors. European Journal of Neuroscience published by Federation of European Neuroscience Societies and John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.en
dc.subjectadenosine monophosphate kinase protein; glycogen synthase kinase-3β; microtubule-associated protein; neuronal energy stress; phosphorylation; protein phosphatase 2Aen
dc.titleEarly glycogen synthase kinase-3β and protein phosphatase 2A independent tau dephosphorylation during global brain ischaemia and reperfusion following cardiac arrest and the role of the adenosine monophosphate kinase pathwayen
dc.title.alternativeEarly glycogen synthase kinase-3beta and protein phosphatase 2A independent tau dephosphorylation during global brain ischaemia and reperfusion following cardiac arrest and the role of the adenosine monophosphate kinase pathwayen
dc.typeJournal articleen
dc.identifier.rmid0030048268en
dc.identifier.doi10.1111/ejn.13277en
dc.identifier.pubid250341-
pubs.library.collectionPsychology publicationsen
pubs.library.teamDS10en
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
dc.identifier.orcidKoblar, S. [0000-0002-8667-203X]en
dc.identifier.orcidGrantham, H. [0000-0003-1700-190X]en
Appears in Collections:Psychology publications

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