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Titolo:
AGONIST-SPECIFIC TYROSINE PHOSPHORYLATION OF CBL IN HUMAN NEUTROPHILS
Autore:
NACCACHE PH; GILBERT C; BARABE F; ALSHAMI A; MAHANA W; BOURGOIN SG;
Indirizzi:
CHUL,CTR RECH,CTR RECH RHUMATOL & IMMUNOL,2705 BLVD LAURIER ST FOY PQG1V 4G2 CANADA UNIV LAVAL,FAC MED,DEPT MED ST FOY PQ G1K 7P4 CANADA UNIV LAVAL,FAC MED,DEPT PHYSIOL ST FOY PQ G1K 7P4 CANADA NIAID,IMMUNOGENET LAB BETHESDA MD 20892
Titolo Testata:
Journal of leukocyte biology
fascicolo: 6, volume: 62, anno: 1997,
pagine: 901 - 910
SICI:
0741-5400(1997)62:6<901:ATPOCI>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
COLONY-STIMULATING FACTOR; TUMOR-NECROSIS-FACTOR; ELECTROPERMEABILIZED HUMAN-NEUTROPHILS; METHIONYL-LEUCYL-PHENYLALANINE; RABBIT PERITONEAL NEUTROPHILS; HUMAN INTERLEUKIN-8 RECEPTOR; ACTIVATED PROTEIN-KINASES; EPIDERMAL GROWTH-FACTOR; FC-GAMMA RECEPTORS; C-CBL;
Keywords:
PHAGOCYTIC PARTICLES; CHEMOTACTIC FACTORS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
76
Recensione:
Indirizzi per estratti:
Citazione:
P.H. Naccache et al., "AGONIST-SPECIFIC TYROSINE PHOSPHORYLATION OF CBL IN HUMAN NEUTROPHILS", Journal of leukocyte biology, 62(6), 1997, pp. 901-910

Abstract

The effects of soluble and particulate agonists on the tyrosine phosphorylation levels of the proto-oncogene Cbl in human neutrophils were examined, Experimental conditions allowing the maintenance of Cbl as well as of its tyrosine phosphorylation status were first established, Their use allowed us to observe that Cbl was tyrosine phosphorylated in response to some (Fc gamma RII ligation, opsonized bacteria and zymosan, granulocyte-macrophage colony-stimulating factor, monosodium urate, and calcium pyrophosphate microcrystals), but not all (fMet-Leu-Phe, interleukin-8) neutrophil agonists, Cbl was also shown to account for a varying proportion of the 120-kDa phosphoprotein(s) observed In response to the above stimuli, These data establish that Cbl is present in human neutrophils and that its level of tyrosine phosphorylation ismodulated by some of these cells' agonists, and in particular by phagocytic particles, Furthermore, the signaling pathways activated by chemotactic factors and the other neutrophil stimuli tested in this investigation diverge at or downstream from the tyrosine phosphorylation ofCbl.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 12:26:37