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J. Biol. Chem., Vol. 266, Issue 13, 8302-8311, May, 1991
PL Rothenberg, WS Lane, A Karasik, J Backer, M White and CR Kahn
Insulin stimulates the tyrosine phosphorylation of a 185-kDa putative
cytosolic substrate protein (pp185) in diverse cell types. After
intravenous insulin infusion into the live intact rat, pp185 and the 95-
kDa insulin receptor beta-subunit were the major proteins that tyrosine
phosphorylated in liver, skeletal muscle, and adipose tissue. Both proteins
were maximally phosphorylated within 30 s, and both increased in
phosphotyrosine content in parallel with increasing insulin dose. However,
pp185 tyrosine phosphorylation was transient, with almost complete
dephosphorylation within 2-3 min despite continued insulin stimulation. To
identify pp185 directly, we purified pp185 from insulin- stimulated rat
liver, using a denaturation-based extraction procedure that blocks
endogenous protein phosphatases and thus allows a high yield, single step
isolation of phosphotyrosyl proteins by anti- phosphotyrosine antibody
immunoaffinity absorption. From 50 rat livers, 50-100 pmol of pp185 was
isolated. Edman degradation of seven internal tryptic peptide fragments of
pp185 yielded novel amino acid sequences, indicating that pp185 is a new
protein. Antipeptide antibodies were raised which specifically recognize a
single, 185-kDa insulin- stimulated phosphotyrosyl protein in liver,
skeletal muscle, adipose tissue, and several cultured cell lines. These
results indicate that pp185 is expressed in a variety of insulin-responsive
tissues, is the major protein rapidly tyrosine phosphorylated under
physiological conditions in the intact animal, and also provide a route for
cloning the pp185 gene and elucidating the function of pp185 in insulin
signal transduction.
Purification and partial sequence analysis of pp185, the major cellular substrate of the insulin receptor tyrosine kinase
Research Division, Joslin Diabetes Center, Boston, Massachusetts.
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