Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
KINASE-INDEPENDENT POTENTIATION OF B-CELL ANTIGEN RECEPTOR-MEDIATED SIGNAL-TRANSDUCTION BY THE PROTEIN-TYROSINE KINASE SRC
Autore:
LIN JJ; TAO JX; DYER RB; HERZOG NK; JUSTEMENT LB;
Indirizzi:
UNIV ALABAMA,DEPT MICROBIOL,DIV DEV & CLIN IMMUNOL,WALLACE TUMOR INST378 BIRMINGHAM AL 35294 UNIV ALABAMA,DEPT MICROBIOL,DIV DEV & CLIN IMMUNOL,WALLACE TUMOR INST378 BIRMINGHAM AL 35294 UNIV TEXAS,MED BRANCH,DEPT MICROBIOL & IMMUNOL GALVESTON TX 77555 UNIV TEXAS,MED BRANCH,DEPT PATHOL GALVESTON TX 77555
Titolo Testata:
The Journal of immunology
fascicolo: 10, volume: 159, anno: 1997,
pagine: 4823 - 4833
SICI:
0022-1767(1997)159:10<4823:KPOBAR>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHORYLATED IG-ALPHA; NF-KAPPA-B; GTPASE-ACTIVATING PROTEIN; CROSS-LINKING; SH2 DOMAINS; PHOSPHATIDYLINOSITOL 3-KINASE; BINDING-SPECIFICITY; LYMPHOCYTE-B; FAMILY; LYN;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
J.J. Lin et al., "KINASE-INDEPENDENT POTENTIATION OF B-CELL ANTIGEN RECEPTOR-MEDIATED SIGNAL-TRANSDUCTION BY THE PROTEIN-TYROSINE KINASE SRC", The Journal of immunology, 159(10), 1997, pp. 4823-4833

Abstract

Signal transduction mediated by the B cell Ag receptor involves the activation of multiple protein tyrosine kinases that are members of theSrc family (i.e., Fyn, Lyn, Blk, Lck). To determine whether members of the Src family possess common physical and/or enzymatic properties that enable them to potentiate signal transduction via the B cell Ag receptor, we expressed the protein tyrosine kinase Src in the B lymphomacell line K46-17 mu m lambda. Based on coprecipitation analysis and two-color immunofluorescence, this heterologous Src family kinase was observed to physically associate with the B cell Ag receptor, Additional experiments demonstrated that B cell Ag receptor cross-linking results in increased tyrosine phosphorylation and activation of Src, Several parameters of B cell activation, including tyrosine phosphorylation of intracellular substrates, calcium mobilization, and transcription factor activation, were potentiated in cells that expressed Src when compared with control cells. To determine whether potentiation of Ag receptor-mediated signaling by Src was dependent on its catalytic activity, a kinase-deficient form of Src was expressed in K46-17 mu m lambda cells. Transfectants expressing kinase-deficient Src exhibited an enhanced responsiveness to stimulation through the B cell Ag receptor thatwas comparable with transfectants expressing wild-type Src. Additionally, kinase-deficient Src was observed to associate with the endogenous kinase Lyn in an activation-dependent manner. These findings indicate that members of the Src family may potentiate Ag receptor-mediated signaling via a kinase-independent mechanism(s) that involves amplification of kinase recruitment to the Ag receptor activation complex.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 08:00:57