Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
UNALTERED SECRETION OF BETA-AMYLOID PRECURSOR PROTEIN IN GELATINASE A(MATRIX METALLOPROTEINASE 2)-DEFICIENT MICE
Autore:
ITOH T; IKEDA T; GOMI H; NAKAO S; SUZUKI T; ITOHARA S;
Indirizzi:
KYOTO UNIV,INST VIRUS RES,SAKYO KU,53 KAWAHARA KYOTO 60601 JAPAN KYOTO UNIV,INST VIRUS RES,SAKYO KU KYOTO 60601 JAPAN UNIV TOKYO,FAC PHARMACEUT SCI,BUNKYO KU TOKYO 113 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 36, volume: 272, anno: 1997,
pagine: 22389 - 22392
SICI:
0021-9258(1997)272:36<22389:USOBPP>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALZHEIMERS-DISEASE; NEXIN-II; CELLS; RAT; LOCALIZATION; SURFACE; DOMAIN; BRAIN; GENE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
24
Recensione:
Indirizzi per estratti:
Citazione:
T. Itoh et al., "UNALTERED SECRETION OF BETA-AMYLOID PRECURSOR PROTEIN IN GELATINASE A(MATRIX METALLOPROTEINASE 2)-DEFICIENT MICE", The Journal of biological chemistry, 272(36), 1997, pp. 22389-22392

Abstract

The beta-amyloid peptide, which forms extracellular cerebral depositsin Alzheimer's disease, is derived from a large membrane-spanning glycoprotein referred to as the beta-amyloid precursor protein (APP). TheAPP is normally cleaved within the beta-amyloid region by a putative proteinase (alpha-secretase) to generate large soluble amino-terminal derivatives of APP, and this event pre vents the beta-amyloid peptide formation. It has been suggested that the gelatinase A (matrix metalloproteinase 2, a 72-kDa type IV collagenase) may act either as alpha-secretase or as beta-secretase. Mice devoid of gelatinase A generated bygene targeting develop normally, except for a subtle delay in their growth, thus providing a useful system to examine the role of gelatinase A in the cleavage and secretion of APP in vivo. We show here that APP is cleaved within the beta-amyloid region and secreted into the extracellular milieu of brain and cultured fibroblasts without gelatinase A activity. The data suggest that gelatinase A does not play an essential role in the generation and release of soluble derivatives of APP at physiological conditions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 01:55:00