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Titolo:
Tyrosine phosphorylation of the linker for activator of T cells in mast cells by stimulation with the high affinity IgE receptor
Autore:
Kimura, T; Hisano, M; Inoue, Y; Adachi, M;
Indirizzi:
Showa Univ, Sch Med, Dept Internal Med 1, Shinagawa Ku, Tokyo 1428666, Japan Showa Univ Tokyo Japan 1428666 Med 1, Shinagawa Ku, Tokyo 1428666, Japan
Titolo Testata:
IMMUNOLOGY LETTERS
fascicolo: 2, volume: 75, anno: 2001,
pagine: 123 - 129
SICI:
0165-2478(20010101)75:2<123:TPOTLF>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
BASOPHILIC LEUKEMIA-CELLS; PROTEIN-KINASE-C; SIGNAL-TRANSDUCTION; ANTIGEN RECEPTOR; PHOSPHOLIPASE C-GAMMA-1; RBL-2H3 CELLS; PHOSPHATIDYLINOSITOL 3-KINASE; HISTAMINE-RELEASE; SH2 DOMAIN; SYK;
Keywords:
signal transduction; mast cell; Fc receptor; IgE; allergy;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Kimura, T Showa Univ, Sch Med, Dept Internal Med 1, Shinagawa Ku, 1-5-8 Hatanodai, Tokyo 1428666, Japan Showa Univ 1-5-8 Hatanodai Tokyo Japan 1428666 o 1428666, Japan
Citazione:
T. Kimura et al., "Tyrosine phosphorylation of the linker for activator of T cells in mast cells by stimulation with the high affinity IgE receptor", IMMUNOL LET, 75(2), 2001, pp. 123-129

Abstract

Aggregation of the high affinity IgE receptors (Fc epsilon RI) on basophils and mast cells, members of the immune receptor family, initiates a cascade of events that result in the release of inflammatory mediators. This pathway involves the activation of several protein-tyrosine kinases, including Lyn, Syk, Btk, and Fak that induce the tyrosine phosphorylation of various proteins. The linker for activation of T cells (LAT), was originally found as a ZAP-70 tyrosine kinase substrate that linked T cell receptors to cellular activation, and was expressed in T cells, NK cells and mast cells. Herewe show that LAT expressed in the RBL-2H3 rat mast cell line is tyrosine-phosphorylated after aggregation of Fc epsilon RI. The tyrosine phosphorylation of the LAT was dramatically enhanced after receptor aggregation. Furthermore, a tyrosine-phosphorylated 80-kDa protein associated with LAT transiently after receptor aggregation. GST fusion proteins containing parts of PLC gamma or PI3 kinase can bind LAT. These results suggest that LAT plays animportant role not only in T cell, but also in mast cell activation, and that the association among these signaling molecules is critical for Fc epsilon RI-mediated intracellular signal transduction in mast cells. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/04/20 alle ore 09:14:54