Phosphorylation of tau at serine 416 by Ca2+/calmodulin-dependent protein kinase II in neuronal soma in brain.

Phosphorylation of tau at serine 416 by Ca2+/calmodulin-dependent protein kinase II in neuronal soma in brain. Research Abstract Details 

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Phosphorylation of tau at serine 416 by Ca2+/calmodulin-dependent protein kinase II in neuronal soma in brain. Abstract Text:

Hideyuki Yamamoto,Yukari Hiragami,Miyuki Murayama,Koko Ishizuka,Masahiro Kawahara,Akihiko Takashima,Hideyuki Yamamoto,Yukari Hiragami,Miyuki Murayama,Koko Ishizuka,Masahiro Kawahara,Akihiko Takashima,

It is well known that tau is a good in vitro substrate for Ca2+/calmodulin-dependent protein kinase II (CaM kinase II). However, it is not clear at present whether CaM kinase II phosphorylates tau in vivo or not. Serine 416, numbered according to the longest human tau isoform, has been reported to be one of the major phosphorylation sites by CaM kinase II in vitro. In this study, we produced a specific antibody against tau phosphorylated at serine 416 (PS416-tau). Immunoblot analysis revealed that the antibody reacted with tau in the rat brain extract which was prepared in the presence of protein phosphatase inhibitors. Developmental study indicated that serine 416 was strongly phosphorylated at early developmental stages in rat brain. We examined the localization of PS416-tau in primary cultured hippocampal neurons and the immortalized GnRH neurons (GT1-7 cells), which were stably transfected with CaM kinase IIalpha cDNA. Immunostaining of these cells indicated that tau was phosphorylated mainly in neuronal soma. Interestingly, tau in neuronal soma in Alzheimer's disease (AD) brain was strongly immunostained by the antibody. These results suggest that CaM kinase II is involved in the accumulation of tau in neuronal soma in AD brain.

Phosphorylation of tau at serine 416 by Ca2+/calmodulin-dependent protein kinase II in neuronal soma in brain. Publishing Authors By Initials

H Yamamoto,Y Hiragami,M Murayama,K Ishizuka,M Kawahara,A Takashima,H Yamamoto,Y Hiragami,M Murayama,K Ishizuka,M Kawahara,A Takashima,

For similar microtubule-associated proteins: tau proteins research abstracts see: microtubule-associated proteins: tau proteins research

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Phosphorylation of tau at serine 416 by Ca2+/calmodulin-dependent protein kinase II in neuronal soma in brain. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of neurochemistry

VOLUME: 94

Page Numbers: 1438-47

Journal Abbreviation: J. Neurochem.

ISSN: 0022-3042

DAY: 5

MONTH: 07

YEAR: 2005

Phosphorylation of tau at serine 416 by Ca2+/calmodulin-dependent protein kinase II in neuronal soma in brain. Information

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LANGUAGE: eng

NlmUniqueID: 2985190

Phosphorylation of tau at serine 416 by Ca2+/calmodulin-dependent protein kinase II in neuronal soma in brain. Keywords Mesh Terms:

KEYWORDS: tau Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Phosphorylation of tau at serine 416 by Ca2+/calmodulin-dependent protein kinase II in neuronal soma in brain. Information

Substance Name: Camk2a protein, rat

Registry Number: EC 2.7.11.17

Grant and Affiliation Information for Phosphorylation of tau at serine 416 by Ca2+/calmodulin-dependent protein kinase II in neuronal soma in brain.

AFFILIATION: Department of Molecular Pharmacology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan. hideyuki@gpo.kumamoto-u.ac.jp

Country: England

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MEDLINETA: J Neurochem

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