In situ inhibition of tyrosine protein kinase by erbstatin.
Erbstatin inhibited the kinase activity of the receptor for epidermal growth factor in cultured A431 cells, while it did not alter turnover of the receptor protein. It also inhibited autophosphorylation of the src gene product p60src in Rous sarcoma virus-infected normal rat kidney cells. Erbstatin did not inhibit the binding of epidermal growth factor to its receptor but did inhibit internalization of epidermal growth factor-receptor complexes. It did not inhibit the epidermal growth factor-stimulated phosphatidylinositol turnover in A431 cells. Thus, erbstatin inhibited two oncogene product-related tyrosine protein kinases in situ and thus is a useful tool to study the role of tyrosine protein kinase.
D000818:Animals; D002478:Cells, Cultured; D004815:Epidermal Growth Factor / Q000494:pharmacology; D066246:ErbB Receptors / Q000378:metabolism; D006873:Hydroquinones / Q000494:pharmacology*; D010716:Phosphatidylinositols / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000037:antagonists & inhibitors*; D051381:Rats
D006873:Hydroquinones; D010716:Phosphatidylinositols; D010743:Phospholipids; D004815:Epidermal Growth Factor; D066246:ErbB Receptors; D011505:Protein-Tyrosine Kinases; C048212:erbstatin