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Agonist‐specific tyrosine phosphorylation of Cbl in human neutrophils
Author(s) -
Naccache Paul H.,
Gilbert Caroline,
Barabé Frédéric,
AlShami Amin,
Mahana Wahib,
Bourgoin Sylvain G.
Publication year - 1997
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.62.6.901
Subject(s) - tyrosine phosphorylation , phosphorylation , tyrosine , biology , protein tyrosine phosphatase , zymosan , phosphoprotein , chemotaxis , microbiology and biotechnology , biochemistry , receptor , in vitro
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 (FcγRII 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 is modulated 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 of Cbl. J. Leukoc. Biol . 62: 901–910; 1997.