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Titolo:
Hck enhances the adherence of lipopolysaccharide-stimulated macrophages via Cbl and phosphatidylinositol 3-kinase
Autore:
Scholz, G; Cartledge, K; Dunn, AR;
Indirizzi:
Royal Melbourne Hosp, Ludwig Inst Canc Res, Mol Biol Lab, Melbourne, Vic 3050, Australia Royal Melbourne Hosp Melbourne Vic Australia 3050 ne, Vic 3050, Australia
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 19, volume: 275, anno: 2000,
pagine: 14615 - 14623
SICI:
0021-9258(20000512)275:19<14615:HETAOL>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE KINASE; TOLL-LIKE RECEPTOR-2; INTEGRIN SIGNALING PATHWAY; CELL ANTIGEN RECEPTOR; C-CBL; BACTERIAL LIPOPOLYSACCHARIDE; IN-VIVO; PROTOONCOGENE PRODUCT; SH3 DOMAIN; ADAPTER PROTEINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
58
Recensione:
Indirizzi per estratti:
Indirizzo: Scholz, G Royal Melbourne Hosp, Ludwig Inst Canc Res, Mol Biol Lab, POB 2008, Melbourne, Vic 3050, Australia Royal Melbourne Hosp POB 2008 Melbourne Vic Australia 3050 ralia
Citazione:
G. Scholz et al., "Hck enhances the adherence of lipopolysaccharide-stimulated macrophages via Cbl and phosphatidylinositol 3-kinase", J BIOL CHEM, 275(19), 2000, pp. 14615-14623

Abstract

Src family tyrosine kinases have previously been proposed to mediate some of the biological effects of lipopolysaccharide on macrophages, Accordingly, we have sought to identify substrates of Src family kinases in lipopolysaccharide-stimulated macrophages. Stimulation of Bac1.2F5 macrophage cells with lipopolysaccharide was found to induce gradual and persistent tyrosine phosphorylation of Cbl in an Src family kinase-dependent manner. Immunoprecipitation experiments revealed that Cbl associates with Hck in Bac1.2F5 cells, while expression of an activated form of Hck in Bac1.2F5 cells induces tyrosine phosphorylation of Cbl in the absence of lipopolysaccharide stimulation. The Src homology 3 domain of Hck can directly bind Cbl, and this interaction is important for phosphorylation of Chi. Association of the p85 subunit of phosphatidylinositol (PI) 3-kinase with Cbl is enhanced following lipopolysaccharide stimulation of Bac1.2F5 cells, and transient expression experiments indicate that phosphorylation of Cbl by Hck can facilitate the association of p85 with Cbl, Lipopolysaccharide treatment also stimulates the partial translocation of lick to the cytoskeleton of Bac1.2F5 cells. Notably, lipopolysaccharide enhances the adherence of Bac1.2F5 cells, an effect that is dependent on the activity of Src family kinases and PI 3-kinase. Thus, we postulate that Hck enhances the adherence of lipopolysaccharide-stimulated macrophages, at least in part, via Cbl and PI 3-kinase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 07:02:01