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Tyrosine phosphorylation is an early and requisite signal induced by interferon‐γ in HL‐60 cells
Author(s) -
Offermanns Stefan,
Schultz Günter
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81344-l
Subject(s) - tyrosine phosphorylation , phosphorylation , tyrosine , interferon , protein tyrosine phosphatase , chemistry , microbiology and biotechnology , interferon γ , protein phosphorylation , biochemistry , interferon gamma , biology , immunology , in vitro , protein kinase a
Interferon‐γ (IFNγ) is a potent immunomodulatory cytokine. However, the early mechanisms which mediate the pleiotropic effects of IFNγ on different cells are as yet poorly understood. Therefore, we tested the role of tyrosine phosphorylation in signalling induced by IFNγ. IFNγ was found to induce rapid tyrosine phosphorylation of several proteins in HL‐60 cells. This effect was detectable by 2 min, reached a maximum by about 4–16 min and thereafter declined. Tyrosine phosphorylation was dependent on receptor occupation and was maximally stimulated by 10 ng/ml IFNγ. Treatment of HL‐60 cells with the tyrosine kinase inhibitors, genistein and herbimycin A, inhibited both IFNγ‐stimulated tyrosine phosphorylation and IFNγ‐induced Fc receptor expression. Thus, increased tyrosine phosphorylation appears to be an obligatory early and proximal signal mediating at least some of the later cellular responses induced by IFNγ in HL‐60 cells.