Diverse mitogenic agents induce the phosphorylation of two related 42,000-dalton proteins on tyrosine in quiescent chick cells - PubMed (original) (raw)

Comparative Study

J A Cooper et al. Mol Cell Biol. 1984 Jan.

Abstract

Incubation of quiescent chicken embryo cells with platelet-derived growth factor, epidermal growth factor, or serum was found to stimulate phosphorylation of two proteins of ca. 42,000 daltons on tyrosine. These proteins are structurally related to each other and to two proteins phosphorylated on tyrosine under similar conditions in mitogen-treated mouse fibroblasts. Three other very different mitogenic agents, the protease trypsin and the chemically unrelated tumor promoters 12-O-tetradecanoyl-phorbol-13-acetate and teleocidin, stimulated phosphorylation of the same proteins. In all cases, phosphotyrosine was detected in these phosphoproteins. Although additional changes in protein phosphorylation were evident, no other proteins were observed by two-dimensional gel electrophoresis which contained increased amounts of phosphotyrosine in mitogen-treated chicken embryo cells. One of these 42,000-dalton proteins was shown previously to be phosphorylated on tyrosine in chicken embryo cells transformed with various retroviruses whose transforming proteins possess tyrosine protein kinase activity. Phosphorylation of the 42,000-dalton proteins could be important in the regulation of cell division.

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References

    1. J Cell Physiol. 1972 Oct;80(2):167-73 - PubMed
    1. Proc Natl Acad Sci U S A. 1964 Jan;51:66-73 - PubMed
    1. Proc Natl Acad Sci U S A. 1973 Sep;70(9):2702-6 - PubMed
    1. Proc Natl Acad Sci U S A. 1973 Oct;70(10):2964-8 - PubMed
    1. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1207-10 - PubMed

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