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001-es BibID:	BIBFORM054321
035-os BibID:	PMID: 10382761
Első szerző:	Koncz Gábor (biológus, immunológus)
Cím:	Fcγ receptor-mediated inhibition of human B cell activation : the role of SHP-2 phosphatase / Gábor Koncz, Israel Pecht, János Gergely, Gabriella Sármay
Dátum:	1999
ISSN:	0014-2980
Megjegyzések:	Co-clustering of the type II receptors binding the Fc part of IgG (Fc gamma RIIb) and B cell receptors results in the translocation of cytosolic, negative regulatory molecules to the phosphorylated immunoreceptor tyrosine-based inhibitory motif (P-ITIM) of the FcyRIIb. SH2 domain-containing protein tyrosine phosphatases (SHP-1 and SHP-2), and the polyphosphoinositol 5'-phosphatase (SHIP) have been reported earlier to bind to murine Fc gamma RIIb P-ITIM. However, neither the functional substrates of these enzymes, nor the mechanism of the inhibition are fully resolved. We show here that the human Fc gamma RIIb binds SHP-2 when co-clustered with the B cell receptors, whereas its synthetic P-ITIM peptide bindes SHP-2 and SHIP in lysates of the Burkitt's lymphoma cell line BL41. The P-ITIM peptide binding enhances SHP-2 activity resulting in dephosphorylation and release of P-ITIM-bound SHIP and She. Moreover, P-ITIM-bound SHP-2 dephosphorylates synthetic peptides corresponding to the sites of tyrosine phosphorylation on SHIP and She, indicating that these proteins are its potential substrates. Thus SHP-2-induced dephosphorylation may modulate the intracellular localization and/or activity of SHIP and She, thereby inhibiting further activation pathways which they mediate.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban SHP-2 Fc gamma RIIb human B cell
Megjelenés:	European Journal of Immunology. - 29 : 6 (1999), p. 1980-1989. -
További szerzők:	Pecht, Israel Gergely János Sármay Gabriella
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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