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Titolo:
Calpain function in the modulation of signal transduction molecules
Autore:
Sato, K; Kawashima, S;
Indirizzi:
Tokyo Metropolitan Inst Med Sci, Dept Biol Mol, Tokyo 1138613, Japan TokyoMetropolitan Inst Med Sci Tokyo Japan 1138613 Tokyo 1138613, Japan
Titolo Testata:
BIOLOGICAL CHEMISTRY
fascicolo: 5, volume: 382, anno: 2001,
pagine: 743 - 751
SICI:
1431-6730(200105)382:5<743:CFITMO>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACTIVATED NEUTRAL PROTEASE; CALCIUM-DEPENDENT PROTEASE; KINASE-C; HUMAN PLATELETS; DOWN-REGULATION; RAT-BRAIN; LIMITED PROTEOLYSIS; CALPASTATIN SYSTEM; CRYSTAL-STRUCTURE; FOCAL ADHESIONS;
Keywords:
G-protein; integrin; protein kinase C; tyrosine kinase;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
69
Recensione:
Indirizzi per estratti:
Indirizzo: Sato, K Tokyo Metropolitan Inst Med Sci, Dept Biol Mol, Tokyo 1138613, Japan Tokyo Metropolitan Inst Med Sci Tokyo Japan 1138613 38613, Japan
Citazione:
K. Sato e S. Kawashima, "Calpain function in the modulation of signal transduction molecules", BIOL CHEM, 382(5), 2001, pp. 743-751

Abstract

Calpains are cytosolic cysteine proteases that are activated by a rise in intracellular Ca2+, and are believed to function in stimulating Ca2+ signaling on cell activation, leading the cell to differentiation, proliferation and death, In this review, we focus on the implication of calpains in signal transduction in molecules such as growth factors, T cell receptor, and integrin, Calpains are downstream molecules of hormone receptors, membrane-type tyrosine kinases and adhesion molecules, and proteolyze many signaling-related substrates. The substrates, protein kinase C (PKC), ( subunit of G-proteins, and protein tyrosine phosphatases, are cleaved at interdomain site(s) and their activities are sustained or upregulated, while the fragments of focal adhesion kinase and the tyrosine kinase src family lose their activity. In the integrin cascade, calpains are upstream molecules of the Rho GTPase family, Rac1 or RhoA, and allow the lamellipodia formation. The significant activation of calpain suggests that calpain activity is regulated not only by an increase in intracellular Ca2+, but also by signaling that include the PKC-, tyrosine kinase- or the adhesion molecule-derived cascade, We have summarized these interesting phenomena, and speculate on the function and location of calpain in the signaling cascades.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 00:17:18