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Vol. 273, Issue 2, 1200-1207, January 9, 1998
From the Endocrinology-Reproductive Physiology Program, University
of Wisconsin, Madison, Wisconsin 53706
Previously, we have shown that prolactin inhibits
epidermal growth factor (EGF)-induced mitogenesis in mouse mammary
epithelial cells without altering the response to other growth
promoting agents. This effect has been associated with reduced
EGF-induced EGF receptor (EGFR) tyrosine phosphorylation, Grb-2
association, and Ras activation. Our current hypothesis is that
prolactin induces an alteration in EGFR kinase activity via a
phosphorylation-dependent mechanism. To test this
hypothesis, we treated normal murine mammary gland cells with or
without 100 ng/ml prolactin. EGFR isolated by wheat germ agglutinin
affinity chromatography from nontreated cells exhibited substantial
ligand-induced phosphorylation, and EGFR isolated from
prolactin-treated cells displayed minimal EGF-induced EGFR
phosphorylation, as well as decreased kinase activity toward exogenous
substrates. The observed decrease in ligand-induced EGFR
phosphorylation could not be attributed to either differential amounts
of EGFR, decreased EGF binding affinity, or the presence of a
phosphotyrosine phosphatase or ATPase. EGFR isolated from prolactin-treated cells exhibited increased phosphorylation on threonine. Removal of this phosphorylation with alkaline phosphatase restored EGFR kinase activity to levels observed in nontreated cells.
Therefore, these results suggest that prolactin antagonizes EGF
signaling by increasing EGFR threonine phosphorylation and decreasing
EGF-induced EGFR tyrosine phosphorylation.
Prolactin Decreases Epidermal Growth Factor Receptor Kinase
Activity via a Phosphorylation-dependent Mechanism
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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