Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
PHOSPHORYLATION OF MICROTUBULE-ASSOCIATED PROTEIN-TAU ON SER-262 BY AN EMBRYONIC 100 KDA PROTEIN-KINASE
Autore:
JENKINS SM; JOHNSON GVW;
Indirizzi:
UNIV ALABAMA,DEPT PSYCHIAT & BEHAV NEUROBIOL SC1061 BIRMINGHAM AL 35294 UNIV ALABAMA,DEPT PSYCHIAT & BEHAV NEUROBIOL SC1061 BIRMINGHAM AL 35294
Titolo Testata:
Brain research
fascicolo: 2, volume: 767, anno: 1997,
pagine: 305 - 313
SICI:
0006-8993(1997)767:2<305:POMPOS>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
PAIRED HELICAL FILAMENTS; ALZHEIMERS-DISEASE; HUMAN-BRAIN; FETAL TAU; BINDING; ISOFORMS; P110(MARK); EXPRESSION; COMPONENT; SER(262);
Keywords:
ALZHEIMERS DISEASE; PAIRED HELICAL FILAMENT; NEUROFIBRILLARY TANGLE; MICROTUBULE-ASSOCIATED PROTEINS; MAP-2; MARK; CYTOSKELETON;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
S.M. Jenkins e G.V.W. Johnson, "PHOSPHORYLATION OF MICROTUBULE-ASSOCIATED PROTEIN-TAU ON SER-262 BY AN EMBRYONIC 100 KDA PROTEIN-KINASE", Brain research, 767(2), 1997, pp. 305-313

Abstract

This study examined the phosphorylation of tan on Ser 262, within thefirst microtubule-binding domain, by a developmentally regulated 100 kDa protein kinase exhibiting significantly greater activity in the embryonic rat brain than in the adult rat brain. This protein kinase co-purified with microtubules and co-immunoprecipitated with both tau andMAP-2. In addition to phosphorylating tau, MAP-2, and a Ser 262-containing peptide, the present protein kinase activity was shown to autophosphorylate as determined by the in-gel kinase assay in the absence ofany protein or peptide polymerized into the matrix. Phosphorylation of tau with this protein kinase significantly reduced the tau-microtubule interaction, and the effect was significantly greater with microtubule-associated protein (MAP) preparations from embryonic brain than with preparations from the adult. Ser 262 is phosphorylated extensively in paired helical filament (PHF) tau from Alzheimer's disease (AD) brain, to a lesser extent in fetal tau, and only to a very minor extent in biopsy-derived human tau. Because the 100 kDa protein kinase activity phosphorylates Ser 262 and is higher in the fetal brain than the adult brain, it is hypothesized that an inappropriate re-expression and/or re-activation of this or a similar developmentally regulated proteinkinase could contribute to the phosphorylation of Ser 262 in PHF-tau,and thus play a role in the pathogenesis of AD. (C) 1997 Elsevier Science B.V.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 18:26:22