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Titolo:
Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase
Autore:
Itoh, Y; Kajita, M; Kinoh, H; Mori, H; Okada, A; Seiki, M;
Indirizzi:
Univ Tokyo, Inst Med Sci, Dept Canc Cell Res, Minato Ku, Tokyo 1088639, Japan Univ Tokyo Tokyo Japan 1088639 Cell Res, Minato Ku, Tokyo 1088639, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 48, volume: 274, anno: 1999,
pagine: 34260 - 34266
SICI:
0021-9258(19991126)274:48<34260:MT4MM(>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
TUMOR-NECROSIS-FACTOR; UROKINASE PLASMINOGEN-ACTIVATOR; MOLECULAR-CLONING; CELL-SURFACE; TISSUE DISTRIBUTION; RECEPTOR; IDENTIFICATION; DOMAIN; CDNA; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Seiki, M Univ Tokyo, Inst Med Sci, Dept Canc Cell Res, Minato Ku, 4-6-1 Shirokanedai, Tokyo 1088639, Japan Univ Tokyo 4-6-1 Shirokanedai Tokyo Japan1088639 1088639, Japan
Citazione:
Y. Itoh et al., "Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase", J BIOL CHEM, 274(48), 1999, pp. 34260-34266

Abstract

Among the five membrane-type matrix metalloproteinases (MT-MMPs), MT1-, MT2-, MT3-, and MT5-MMPs have about a 20-amino acid cytoplasmic tail following the transmembrane domain. In contrast, a putative transmembrane domain ofMT4-MMP locates at the very C-terminal end, and the expected cytoplasmic tail is very short or nonexistent, Such sequences often act as a glycosylphosphatidylinositol (GPI) anchoring signal rather than as a transmembrane domain, We thus examined the possibility that MT4-MMP is a GPI-anchored proteinase, Our results showed that [H-3]ethanolamine, which can be incorporated into the GPI unit, specifically labeled the MT4-MMP C-terminal end in a sequence-dependent manner. In addition, phosphatidylinositol-specific phospholipase C treatment released the MT4-MMP from the surface of transfected calls. These results indicate that MT4-MMP is the first GPI-anchored proteinasein the MMP family, During cultivation of the transfected cells, MT4-MMP appeared to be shed from the cell surface by the action of an endogenous metalloproteinase. GPI anchoring of MT4-MMP on the cell surface indicates a unique biological function and character for this proteinase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/07/20 alle ore 05:50:55