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Titolo:
Calreticulin functions as a molecular chaperone for the beta-amyloid precursor protein
Autore:
Johnson, RJ; Xiao, G; Shanmugaratnam, J; Fine, RE;
Indirizzi:
Boston Univ, Sch Med, Dept Biochem, Boston, MA 02118 USA Boston Univ Boston MA USA 02118 h Med, Dept Biochem, Boston, MA 02118 USA Boston Univ, Sch Med, Dept Anat & Neurobiol, Boston, MA 02118 USA Boston Univ Boston MA USA 02118 pt Anat & Neurobiol, Boston, MA 02118 USA Edith Nourse Rogers Mem Vet Adm Hosp, Bedford, MA 01730 USA Edith Nourse Rogers Mem Vet Adm Hosp Bedford MA USA 01730 d, MA 01730 USA
Titolo Testata:
NEUROBIOLOGY OF AGING
fascicolo: 3, volume: 22, anno: 2001,
pagine: 387 - 395
SICI:
0197-4580(200105/06)22:3<387:CFAAMC>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENDOPLASMIC-RETICULUM STRESS; ALZHEIMERS-DISEASE; BINDING-PROTEIN; CALNEXIN; PEPTIDE; CELLS; EXPRESSION; GLYCOPROTEINS; SECRETION; INTERACTS;
Keywords:
beta-amyloid precursor protein; Alzheimer's disease; chaperones; calreticulin; endoplasmic reticulum; beta-amyloid;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Johnson, RJ Boston Univ, Sch Med, Dept Biochem, Boston, MA 02118 USA Boston Univ Boston MA USA 02118 Biochem, Boston, MA 02118 USA
Citazione:
R.J. Johnson et al., "Calreticulin functions as a molecular chaperone for the beta-amyloid precursor protein", NEUROBIOL A, 22(3), 2001, pp. 387-395

Abstract

Processing of the beta -amyloid precursor protein (APP) in the endoplasmicreticulum and the Golgi apparatus may be critical in generating the beta -amyloid molecules linked to the pathogenesis of Alzheimer's disease. Since chaperone molecules such as calreticulin (Crt) have been shown to be important in the maturation of many glycoproteins, we investigated the interaction between Crt and APP. We show that APP binds transiently to Crt in a manner that is pH, divalent cation, and N-linked glycosylation-dependent. Both immature APP (containing only N-linked sugars) and mature APP (containing both N-linked and O-linked sugars) bind to Crt. Both proteins are part of a complex that appears to be large enough to accommodate other proteins as well. However, while most of the immature form is associated with the complexes, very little of the mature form is. The interaction between APP and Crt is likely to be of physiological significance with respect to APP maturationsince Crt is involved in quality control of nascent glycoproteins in the secretory pathway. (C) 2001 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 15:27:03