Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Positive regulation of interleukin-4-mediated proliferation by the SH2-containing inositol-5 '-phosphatase
Autore:
Giallourakis, C; Kashiwada, M; Pan, PY; Danial, N; Jiang, H; Cambier, J; Coggeshall, KM; Rothman, P;
Indirizzi:
Columbia Univ Coll Phys & Surg, Dept Med, New York, NY 10032 USA Columbia Univ Coll Phys & Surg New York NY USA 10032 w York, NY 10032 USA Columbia Univ Coll Phys & Surg, Dept Microbiol, New York, NY 10032 USA Columbia Univ Coll Phys & Surg New York NY USA 10032 w York, NY 10032 USA Natl Jewish Med & Res Ctr, Dept Immunol, Denver, CO 80206 USA Natl Jewish Med & Res Ctr Denver CO USA 80206 munol, Denver, CO 80206 USA Ohio State Univ, Dept Microbiol, Columbus, OH 43210 USA Ohio State Univ Columbus OH USA 43210 t Microbiol, Columbus, OH 43210 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 38, volume: 275, anno: 2000,
pagine: 29275 - 29282
SICI:
0021-9258(20000922)275:38<29275:PROIPB>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
INOSITOL PHOSPHATASE SHIP; PROTEIN-KINASE-B; FC-GAMMA-RIIB; PHOSPHOTYROSINE-BINDING DOMAIN; INSULIN-RECEPTOR SUBSTRATE-1; TYROSINE PHOSPHORYLATION; HEMATOPOIETIC-CELLS; IL-4 RECEPTOR; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE; CYTOKINE STIMULATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
60
Recensione:
Indirizzi per estratti:
Indirizzo: Rothman, P Columbia Univ Coll Phys & Surg, Dept Med, 630 W 168th St,P&S 8-425, New York, NY 10032 USA Columbia Univ Coll Phys & Surg 630 W 168th St,P&S 8-425 New York NY USA 10032
Citazione:
C. Giallourakis et al., "Positive regulation of interleukin-4-mediated proliferation by the SH2-containing inositol-5 '-phosphatase", J BIOL CHEM, 275(38), 2000, pp. 29275-29282

Abstract

The SH2-containing inositol 5'-phosphatase (SHIP) is tyrosine-phosphorylated in response to cytokines such as interleukin (LL)-3, granulocyte-macrophage colony-stimulating factor, and macrophage colony-stimulating factor. SHIP has been shown to modulate negatively these cytokine signalings; however, a potential role in IL-4 signaling remains uncharacterized, It has been recently shown that IL-4 induces tyrosine phosphorylation of SKIP, implicating the phosphatase in IL-4 processes. Tyrosine kinases, Jak1 and Jak3, involved in IL-4 signaling can associate with SHIP, yet only Jak1 can tyrosine-phosphorylate SHIP when co-expressed. In functional studies, cells overexpressing wild type SHIP are found to be hyperproliferative in response to IL-4 in comparison to parental cells. In contrast, cells expressing catalytically inactive form, SHIP(D672A), show reduced proliferation in response to IL-4. These changes in IL-4-induced proliferation correlate with alterationsin phosphatidylinositol 3,4,5-triphosphate levels. However, no differential activation of STAT6, Akt, IRS-2, or p70(S6k), in response to IL-4, was observed in these cells. These data suggest that the catalytic activity of SHIP acts in a novel manner to influence IL-4 signaling. In addition, these data support recent findings that suggest there are uncharacterized signaling pathways downstream of phosphatidylinositol 3,4,5-triphosphate.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 09:24:44