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J Biol Chem, Vol. 273, Issue 25, 15719-15726, June 19, 1998
From the Growth hormone (GH) and
prolactin (PRL) binding to their receptors, which belong to the
cytokine receptor superfamily, activate Janus kinase (JAK) 2 tyrosine
kinase, thereby leading to their biological actions. We recently showed
that GH mainly stimulated tyrosine phosphorylation of epidermal growth
factor receptor and its association with Grb2, and concomitantly
stimulated mitogen-activated protein kinase activity in liver, a major
target tissue. Using specific antibodies, we now show that GH was also
able to induce tyrosine phosphorylation of insulin receptor substrate
(IRS)-1/IRS-2 in liver. In addition, the major tyrosine-phosphorylated
protein in anti-p85 phosphatidylinositol 3-kinase (PI3-kinase)
immunoprecipitate from liver of wild-type mice was IRS-1, and IRS-2 in
IRS-1 deficient mice, but not epidermal growth factor receptor. These
data suggest that tyrosine phosphorylation of IRS-1 may be a major
mechanism for GH-induced PI3-kinase activation in physiological target
organ of GH, liver. We also show that PRL was able to induce tyrosine phosphorylation of both IRS-1 and IRS-2 in COS cells transiently transfected with PRLR and in CHO-PRLR cells. Moreover, we show that
tyrosine phosphorylation of IRS-3 was induced by both GH and PRL in COS
cells transiently transfected with IRS-3 and their cognate receptors.
By using the JAK2-deficient cell lines or by expressing a
dominant negative JAK2 mutant, we show that JAK2 is required for the
GH- and PRL-dependent tyrosine phosphorylation of IRS-1,
-2, and -3. Finally, a specific PI3-kinase inhibitor, wortmannin,
completely blocked the anti-lipolytic effect of GH in 3T3 L1
adipocytes. Taken together, the role of IRS-1, -2, and -3 in GH and PRL
signalings appears to be phosphorylated by JAK2, thereby providing
docking sites for p85 PI3-kinase and activating PI3-kinase and its
downstream biological effects.
Growth Hormone and Prolactin Stimulate Tyrosine Phosphorylation
of Insulin Receptor Substrate-1, -2, and -3, Their Association with p85
Phosphatidylinositol 3-Kinase (PI3-kinase), and Concomitantly
PI3-kinase Activation via JAK2 Kinase
,,,,
,,,, and
Third Department of Internal Medicine,
Faculty of Medicine, University of Tokyo, Tokyo 113, Japan, the
§ Department of Molecular Biology, Research Institute, The
Cleveland Clinic Foundation, Cleveland, Ohio 44195, the
¶ Imperial Cancer Research Fund, London WC2A 3PX, United Kingdom,
the Second Department of Internal Medicine, Tokyo Women's
Medical College, Tokyo 162, Japan, and the ** Institute for Diabetes
Care and Research, Asahi Life Foundation, Tokyo 100, Japan
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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