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J. Biol. Chem., Vol. 269, Issue 48, 30085-30088, Dec, 1994
SC Souza, GP Frick, R Yip, RB Lobo, LR Tai and HM Goodman
Growth hormone (GH) produces insulin-like effects in rat adipocytes that
have been deprived of GH for at least 3 h. The effect of a saturating
concentration of GH is qualitatively and quantitatively similar to that
produced by 2-4 ng/ml insulin but differs from that of insulin in the
respect that adipocytes become refractory to prolonged or repeated
stimulation with GH. Since activation of tyrosine kinase is an early event
in the action of both hormones, we investigated the possibility that GH
stimulation of tyrosine phosphorylation of some protein in the insulin
transduction cascade might result in the similar effect of the two
hormones. Adipocytes were preincubated for 3 h in the absence of hormones
and then reincubated without or with 500 ng/ml GH or 4-400 ng/ml insulin
for 10 min. The cells were lysed with an equal volume of buffer containing
1% SDS and preheated to 100 degrees C. Proteins were separated by
electrophoresis on 7.5% polyacrylamide gels and transferred to
nitrocellulose membranes, and tyrosine- phosphorylated proteins were
detected using anti-phosphotyrosine antiserum coupled to horseradish
peroxidase and reagents to produce chemiluminescence. The faint band seen
at 185 kDa in control lanes was increased by GH treatment in five
independent experiments. Insulin produced a similar effect at a
concentration of 4 ng/ml, and phosphorylation increased in a dose-related
manner in cells treated with higher concentrations of insulin. A prominent
approximately 95-kDa band that is probably not the beta subunit of the
insulin receptor was also seen in GH-treated cells. The beta subunit of the
insulin receptor has similar electrophoretic mobility to the 95-kDa
protein, but was not phosphorylated to an extent that allowed detection
when insulin was added at concentrations below 400 ng/ml. Phosphorylation
of the 185- and 95-kDa bands was evident within 1 min after addition of GH,
persisted for at least 30 min, and was equally prominent in sensitive and
refractory cells. Antiserum to IRS-1 immunoprecipitated the
tyrosine-phosphorylated 185-kDa protein. The data suggest that IRS-1 is a
substrate for a GH-activated tyrosine kinase, possibly JAK-2, which may
account for the insulin-like effects of GH. The data further suggest that
refractoriness to insulin-like stimulation by GH may result from an
additional GH-dependent action that is distinct from phosphorylation of
IRS-1.
Growth hormone stimulates tyrosine phosphorylation of insulin receptor substrate-1
Department of Physiology, University of Massachusetts Medical School, Worcester 01655.
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