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Zinc stimulates tau S214 phosphorylation by the activation of Raf/mitogen-activated protein kinase-kinase/extracellular signal-regulated kinase pathway

Authors
 Insook Kim  ;  Eun Ji Park  ;  Jeho Seo  ;  Suk Jin Ko  ;  Jinu Lee  ;  Chul Hoon Kim 
Citation
 Neuroreport, Vol.22(16) : 839-844, 2011 
Journal Title
 Neuroreport 
ISSN
 0959-4965 
Issue Date
2011
Abstract
Hyperphosphorylated tau is a main component of neurofibrillary tangles, a pathological hallmark of Alzheimer's disease (AD). There is evidence that various protein kinases are involved in tau hyperphosphorylation. However, little is known about AD-related stimuli that activates tau kinases. We investigated the role of zinc, a metal involved in AD pathology, in tau phosphorylation. Zinc increased the phosphorylation of serine 214 (S214) in tau protein in human wild-type tau1-441-expressing SH-SY5Y cells. The phosphorylation was inhibited by suppressing the Ras-Raf/mitogen-activated protein kinase kinase/extracellular signal-regulated kinase (ERK) pathway. Mutation of serine to alanine at residue 214 of tau reduced microtubule polymerization impairment by ERK phosphorylation. These data suggest that zinc induces S214 phosphorylation in tau through ERK activation and interferes with microtubule polymerization
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/93986
DOI
10.1097/WNR.0b013e32834c0a2d
Appears in Collections:
1. Journal Papers (연구논문) > 1. College of Medicine (의과대학) > Dept. of Pharmacology (약리학교실)
Yonsei Authors
김철훈(Kim, Chul Hoon)
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http://ovidsp.ovid.com/ovidweb.cgi?T=JS&CSC=Y&NEWS=N&PAGE=fulltext&AN=00001756-201111160-00011&LSLINK=80&D=ovft
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