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The 180000 molecular weight plasma membrane insulin receptor substrate is a protein tyrosine phosphatase and is elevated in diabetic plasma membranes

Goren, H.J.; Boland, D.

Biochemical and Biophysical Research Communications 180(2): 463-469

1991

ISSN/ISBN: 0006-291X
PMID: 1953718
Document Number: 379372
Wheat germ agglutinin-purified non-diabetic human placenta membranes were or were not depleted of EGF receptor with monoclonal anti-EGF receptor antibody B1D8, and subsequently phosphorylated. Phosphorylated insulin receptor .beta.-subunit was lower and pp180 was higher in diabetic placenta membranes than in non-diabetic membranes. Phosphorylated-.beta.-subunit was also lower in diabetic (streptozotocin-induced) rat liver whereas the amount of pp180 was dependent on membrane protein concentration. When rat liver tyrosine-phosphorylated proteins were incubated 30 min, 4.degree. C with EDTA-terminated 32P-phosphorylation reaction mixtures of wheat germ agglutinin-purified rat liver proteins, less phosphorylated proteins were immunoprecipitated with antiphosphotyrosine. The decrease in tyrosine-phosphorylated products suggested that pp180 was a protein tyrosine phosphatase. Taken together, the results suggest that diabetic plasma membranes contain more tyrosine phosphatase than non-diabetic membranes.

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