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Caspase-3-mediated cleavage of PHF-1 tau during apoptosis irrespective of excitotoxicity and oxidative stress: an implication to Alzheimer's disease.

Authors
Kang, HJ; Yoon, WJ; Moon, GJ; Kim, DY; Sohn, S; Kwon, HJ; Gwag, BJ
Citation
Neurobiology of disease, 18(3):450-458, 2005
Journal Title
Neurobiology of disease
ISSN
0969-99611095-953X
Abstract
Excitotoxicity, oxidative stress, and apoptosis have been recognized as routes to neuronal death in various neurological diseases. We examined the possibility that PHF-1 tau, a substrate for various proteases, would be selectively cleaved depending upon routes of neuronal death. Cleavage form of PHF-1 tau was not observed in cortical cell cultures exposed to excitotoxins or oxidative stress that cause neuronal cell necrosis. PHF-1 tau was cleaved within 8 h following exposure of cortical cell cultures to apoptosis-inducing agents. This cleavage was blocked by inclusion of zDEVD-fmk, an inhibitor of caspase-3, and accompanied by activation of caspase-3. Levels and cleavage of PHF-1 tau were markedly increased in AD brain compared with control. Moreover, PHF-1 tau and active caspase-3 were colocalized mostly in tangle-bearing neurons. The current findings suggest that PHF-1 tau is cleaved by caspase-3 during apoptosis and neurodegenerative process in AD.
MeSH terms
AgedAged, 80 and overAlzheimer Disease/metabolism*Alzheimer Disease/pathologyAnimalsAntibodies, Monoclonal/metabolism*Apoptosis/physiology*Caspase 3Caspases/metabolism*Cell ProliferationCells, CulturedCerebral Cortex/metabolismCerebral Cortex/pathologyHumansMaleMiceMice, Inbred ICROxidative Stress/physiology*Substrate Specificitytau Proteins/immunologytau Proteins/metabolism*
DOI
10.1016/j.nbd.2004.12.004
PMID
15755671
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Pharmacology
Journal Papers > Research Organization > Institute for Medical Sciences
Journal Papers > School of Medicine / Graduate School of Medicine > Microbiology
AJOU Authors
강, 효정손, 성향곽, 병주
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