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Titolo:
Phosphorylation of MARCKS in Alzheimer disease brains
Autore:
Kimura, T; Yamamoto, H; Takamatsu, J; Yuzuriha, T; Miyamoto, E; Miyakawa, T;
Indirizzi:
Kumamoto Univ, Sch Med, Dept Neuropsychiat, Kumamoto 8608556, Japan Kumamoto Univ Kumamoto Japan 8608556 ropsychiat, Kumamoto 8608556, Japan Kumamoto Univ, Sch Med, Dept Pharmacol, Kumamoto 8608556, Japan Kumamoto Univ Kumamoto Japan 8608556 Pharmacol, Kumamoto 8608556, Japan Natl Kikuchi Hosp, Div Clin Res, Kumamoto 8611116, Japan Natl Kikuchi Hosp Kumamoto Japan 8611116 in Res, Kumamoto 8611116, Japan Hizen Natl Mental Hosp, Ctr Emot & Behav Disorders, Saga 8420104, Japan Hizen Natl Mental Hosp Saga Japan 8420104 Disorders, Saga 8420104, Japan
Titolo Testata:
NEUROREPORT
fascicolo: 4, volume: 11, anno: 2000,
pagine: 869 - 873
SICI:
0959-4965(20000320)11:4<869:POMIAD>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; AMYLOID BETA-PROTEIN; CELLULAR-REGULATION; ACTIVATION; RECEPTOR; FAMILY; CELLS; INVOLVEMENT; SUBSTRATE; PRECURSOR;
Keywords:
Alzheimer disease; amyloid beta-protein; amyloid beta-protein precursor; dystrophic neurites; MARCKS; microglia; neurons; phosphorylation; protein kinase C;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Kimura, T Kumamoto Univ, Sch Med, Dept Neuropsychiat, Honjo 1-1-1, Kumamoto 8608556,Japan Kumamoto Univ Honjo 1-1-1 Kumamoto Japan 8608556 8608556,Japan
Citazione:
T. Kimura et al., "Phosphorylation of MARCKS in Alzheimer disease brains", NEUROREPORT, 11(4), 2000, pp. 869-873

Abstract

Activation of the amyloid beta-protein precursor, secretary pathway through alpha-secretase has been reported to increase the secretion of neuroprotective amyloid precursor protein and preclude the formation of amyloid beta-protein. Activation of protein kinase C has been shown to accelerate this secretory pathway. These results prompted us to focus on a potential links between protein kinase C and the amyloid beta-protein-related pathology of Alzheimer disease (AD). Although protein kinase C is reported to occur in senile plaques, its catalytic activity has not been investigated. As the phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) has been used as a marker for activation of protein kinase C in vivo, we examined its phosphorylation in brain tissues obtained from seven AD patients and five non-demented subjects using an antibody that specifically recognized MARCKS phosphorylated by protein kinase C. Phosphorylation of MARCKS in cortical neurons in AD brains was weaker than that in control brains. Interestingly, however, phosphorylation of MARCKS was detected in microglia and dystrophic neurites within neuritic plaques, a mature form of amyloid beta-protein deposits. These results suggest that protein kinase C alteration is associated with AD pathology and that protein kinase C is activated in microglia and dystrophic neurites by amyloid beta-protein in AD brains. NeuroReport 11:869-873 (C) 2000 Lippincott Williams & Wilkins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/20 alle ore 15:59:58