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J. Biol. Chem., Vol. 262, Issue 32, 15476-15482, 11, 1987
J Shemer, M Adamo, GL Wilson, D Heffez, Y Zick and D LeRoith
Mouse neuroblastoma N18 cells contain specific high affinity insulin and
insulin-like growth factor-I (IGF-I) receptors. Insulin and IGF-I induce
phosphorylation, in intact cells, of their respective receptor beta
subunits. The insulin receptor beta subunit is represented by a 95- kDa
phosphoprotein that is recognized by a specific antiserum (B10). The IGF-I
receptor beta subunit is represented by two phosphoproteins of molecular
mass 95 and 105 kDa. The hormone-induced phosphorylation was rapid and
dose-dependent occurring on both phosphoserine and phosphotyrosine
residues. In addition, both insulin and IGF-I induced phosphorylation of an
endogenous protein of molecular mass 185 kDa (pp185). The rapidity and dose
dependency of the phosphorylation of pp185 suggested that it may represent
a common endogenous substrate for the insulin and IGF-I receptors in these
neural-derived cells. Phosphorylation was primarily on phosphoserine and
phosphotyrosine residues. pp185 did not absorb to wheat germ
agglutinin-agarose and was not stimulated by either epidermal growth factor
or platelet-derived growth factor. The finding of pp185 in these
neural-related cells as well as in non-neural tissues suggests that it may
represent a ubiquitous endogenous substrate for both the insulin and IGF-I
receptor kinases.
Insulin and insulin-like growth factor-I stimulate a common endogenous phosphoprotein substrate (pp185) in intact neuroblastoma cells
Diabetes Branch, National Institute of Diabetes, Digestive and Kidney Diseases, Bethesda, Maryland 20892.
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