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Titolo:
Phosphorylation sites in the integrin beta(3) cytoplasmic domain in intactplatelets
Autore:
Lerea, KM; Cordero, KP; Sakariassen, KS; Kirk, RI; Fried, VA;
Indirizzi:
New York Med Coll, Dept Cell Biol & Anat, Valhalla, NY 10595 USA New York Med Coll Valhalla NY USA 10595 ol & Anat, Valhalla, NY 10595 USA Univ Oslo, Dept Biol, N-0317 Oslo, Norway Univ Oslo Oslo Norway N-0317Univ Oslo, Dept Biol, N-0317 Oslo, Norway
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 4, volume: 274, anno: 1999,
pagine: 1914 - 1919
SICI:
0021-9258(19990122)274:4<1914:PSITIB>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLYCOPROTEIN-IIB-IIIA; SURFACE-BOUND FIBRINOGEN; PHOSPHATASE INHIBITORS; PROTEIN PHOSPHATASE-1; OKADAIC ACID; CALYCULIN-A; RECEPTOR; AGGREGATION; ACTIVATION; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Lerea, KM New5York Med Coll, Dept Cell Biol & Anat, Basic Sci Bldg, Valhalla, NY 1059 New York Med Coll Basic Sci Bldg Valhalla NY USA 10595 , NY 1059
Citazione:
K.M. Lerea et al., "Phosphorylation sites in the integrin beta(3) cytoplasmic domain in intactplatelets", J BIOL CHEM, 274(4), 1999, pp. 1914-1919

Abstract

Protein seryl/threonyl phosphatase inhibitors such as calyculin A block inside-out and outside-in platelet signaling. Our studies demonstrate that the addition of calyculin A blocks platelet adhesion and spreading on fibrinogen, responses that depend on integrin alpha(IIb)beta(3) signaling. We hypothesized that this reflects a change in alpha(IIb)beta(3) structure caused by a specific state of phosphorylation. We show that addition of calyculin A leads to increased phosphorylation of the beta(3) subunit, and phosphoamino acid analysis reveals that only threonine residues become phosphorylated; sequence analysis by Edman degradation established that threonine 753 became stoichiometrically phosphorylated during inhibition of platelet phosphatases by calyculin A. This region of beta(3) is linked to outside-in signaling such as platelet spreading responses. The effect of calyculin A on platelet adhesion and spreading and on the phosphorylation of T-753 in beta(3) is reversed by the calcium ionophore A23187, demonstrating that these effects of calyculin A are not generally toxic ones. We propose that phosphorylation of beta(3) on threonine 753, a region of beta(3) linked to outside-in signaling, may be a mechanism by which integrin alpha(IIb)beta(3) function is regulated.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 12:05:04