Protein tyrosine kinase and protein phosphotyrosine phosphatase in normal and psoriatic skin.
Protein tyrosine kinase and protein phosphotyrosine phosphatase activities were measured in extracts of skin samples from patients with psoriasis. Both kinase and phosphatase activities were significantly greater in samples taken from an involved area, characterized by epidermal hyperproliferation, than from adjacent skin of normal appearance. Samples from skin of non-psoriatic individuals were indistinguishable from the normal-appearing skin of psoriatic patients. There was no detectable change in the apparent Km for either ATP or casein of the protein tyrosine activity in plaques compared with controls. Phosphorylation of endogenous proteins was also increased about 2-fold in plaque extracts compared with controls. Both epidermal growth factor and platelet-derived growth factor stimulated endogenous protein tyrosine phosphorylation in particulate fractions of plaque biopsies but not in solubilized extracts nor in any control fractions. Our data suggest that increased protein tyrosine phosphorylation and dephosphorylation activity and growth factor sensitivity are important factors in non-malignant hyperplastic cell growth.
D004247:DNA / Q000032:analysis; D004815:Epidermal Growth Factor / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010982:Platelet-Derived Growth Factor / Q000494:pharmacology; D011494:Protein Kinases / Q000378:metabolism*; D011505:Protein-Tyrosine Kinases; D011565:Psoriasis / Q000201:enzymology*; D012867:Skin / Q000201:enzymology*
D010982:Platelet-Derived Growth Factor; D004815:Epidermal Growth Factor; D004247:DNA; D011494:Protein Kinases; D011505:Protein-Tyrosine Kinases; D010749:Phosphoprotein Phosphatases