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Titolo:
SH2-containing protein tyrosine phosphatase-1 (SHP-1) association with Jak2 in UT-7/Epo cells
Autore:
Wu, DW; Stark, KC; Dunnington, D; Dillon, SB; Yi, TL; Jones, C; Pelus, LM;
Indirizzi:
SmithKline Beecham Pharmaceut, Dept Mol Virol & Host Def, Collegeville, PAUSA SmithKline Beecham Pharmaceut Collegeville PA USA f, Collegeville, PAUSA SmithKline Beecham Pharmaceut, Dept Biomol Discovery, King Of Prussia, PA 19406 USA SmithKline Beecham Pharmaceut King Of Prussia PA USA 19406 , PA 19406 USA Cleveland Clin Fdn, Dept Canc Biol, Cleveland, OH 44195 USA Cleveland ClinFdn Cleveland OH USA 44195 c Biol, Cleveland, OH 44195 USA SmithKline Beecham Pharmaceut, Dept Prot Biochem, King Of Prussia, PA 19406 USA SmithKline Beecham Pharmaceut King Of Prussia PA USA 19406 , PA 19406 USA
Titolo Testata:
BLOOD CELLS MOLECULES AND DISEASES
fascicolo: 1, volume: 26, anno: 2000,
pagine: 15 - 24
SICI:
1079-9796(200002)26:1<15:SPTP(A>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYTOKINE-RECEPTOR SUPERFAMILY; HEMATOPOIETIC-CELLS; SH2 DOMAIN; KINASE; PHOSPHORYLATION; IDENTIFICATION; INVOLVEMENT; RECRUITMENT; ACTIVATION; PATHWAY;
Keywords:
SHP-1; Jak2; Epo-induced signaling; UT-7/Epo cells;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Pelus, LM Indiana Univ, Sch Med, Walther Oncol Ctr, 1044 W Walnut St,Room 302, Indianapolis, IN 46202 USA Indiana Univ 1044 W Walnut St,Room 302 Indianapolis IN USA 46202
Citazione:
D.W. Wu et al., "SH2-containing protein tyrosine phosphatase-1 (SHP-1) association with Jak2 in UT-7/Epo cells", BL CELL M D, 26(1), 2000, pp. 15-24

Abstract

We have investigated the interaction of the SH2-containing protein tyrosine phosphatase-1 (SHP-1) and Jak2 in an erythropoietin (Epo)-dependent humanleukemia cell line, UT-7/Epo, using reciprocal immunoprecipitation and immunoblotting. The Epo-induced kinetics and dose response on phosphorylated Jak2 in anti-SHP-1 precipitates of UT-7/Epo cell lysates were similar to those in direct anti-Jak2 precipitates, suggesting that Jak2 coprecipitated with SHP-1. Furthermore, immunoblotting with anti-Jak2 and anti-SHP-1 antibodies indicated that SHP-1 appeared to be constitutively associated with non-tyrosine-phosphorylated Jak2 in UT-7/Epo cells in the absence of Epo and without phosphorylation of the Epo receptor (EpoR). Competition studies with C-terminal SHP-1 and Jak2 peptides decreased the amounts of SHP-1 and Jak2 detected in immunoprecipitates supporting the specific coprecipitation of SHP-1 and Jak2. In the presence of a recombinant GST-fusion protein containing both the N-terminal and C-terminal SH2 domains of SHP-1, anti-GST precipitated the fusion protein but not cellular Jak2. These studies suggest thatSHP-1 and Jak2 are constitutively associated in UT-7/EPO cells. The association is not dependent upon Epo and is not mediated via SHP-1 SH2 binding. Sequential double immunoprecipitation demonstrated that only a small portion of intracellular Jak2 and SHP-1 molecules are constitutively associated. This partial association pattern may allow a more flexible and diverse regulation of Jak2 and SHP-1 activities. Whether Jak2 and SHP-1 are directly associated with each other or are part of a larger complex needs further investigation. (C) 2000 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 21:46:53