title: Epidermal growth factor stimulates phosphorylation of pig epidermal keratin protein.
abstract: Endogenous protein phosphorylation of pig epidermis by epidermal growth factor (EGF) was studied to elucidate biologic roles of EGF on epidermal cells. EGF stimulated phosphorylation of keratin proteins (Mr: 65,000, 60,000, 56,000, and 51,000) identified by the Ouchterlony immunodiffusion analysis, a low Mr protein (16,000 dalton) of the urea-SDS-mercaptoethanol soluble fraction, and a 30,000 dalton Tris-HCl soluble protein. The phosphorylated epidermal proteins such as keratin proteins and a 30,000 dalton protein of the Tris-HCl soluble fraction were slightly dephosphorylated following the addition of unlabeled phosphate. Anti-EGF serum eliminated the EGF-stimulated phosphorylation of keratin proteins, a low Mr protein, and a 30,000 dalton Tris-HCl soluble protein. The overall results indicate that EGF specifically stimulated phosphorylation of several epidermal proteins, one of which was keratin protein.
mesh_terms: D000818:Animals; D001345:Autoradiography; D004591:Electrophoresis, Polyacrylamide Gel; D004815:Epidermal Growth Factor / Q000494:pharmacology*; D004817:Epidermis / Q000187:drug effects / Q000378:metabolism*; D066298:In Vitro Techniques; D007633:Keratins / Q000378:metabolism*; D010766:Phosphorylation; D013552:Swine
chemical_list: D004815:Epidermal Growth Factor; D007633:Keratins