A Novel Histone-stimulated Protein Kinase in Normal and Psoriatic Epidermis
| Autor: | Gary J. Fisher, John J. Voorhees, Hideaki Takematsu |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
Kinase
Cyclin-dependent kinase 2 Autophosphorylation Cell Biology Dermatology Biology Mitogen-activated protein kinase kinase Molecular biology Biochemistry Chromatography DEAE-Cellulose MAP2K7 Histones biology.protein Chromatography Gel Phosphorylation Humans Psoriasis Electrophoresis Polyacrylamide Gel Epidermis Protein kinase A Protein Kinases Molecular Biology Protein kinase C |
| Zdroj: | Journal of Investigative Dermatology. 92(3):385-390 |
| ISSN: | 0022-202X |
| DOI: | 10.1111/1523-1747.ep12277226 |
| Popis: | During the course of studies on protein kinases in psoriatic epidermis, a novel histone-activated protein kinase activity was identified. This activity (referred to as PK-II because it was the second peak of protein kinase activity eluted from a DEAE column) was partially purified from the supernatant of an epidermal homogenate by DEAE-cellulose column chromatography. Although histone was not a substrate for phosphorylation, in the presence of histone, endogenous proteins of Mr 105 and 95 kDa were phosphorylated. Activity was not affected by Ca2+/phospholipid, cAMP, cGMP, cAMP-dependent kinase inhibitor, spermine, spermidine, calmodulin, EGF, or phorbol ester. Phosphorylation was specific for serine and threonine residues. A major peak of PK-II activity eluted from sepharose 6B with an apparent Mr of 100 kDa, suggesting that histone may stimulate autophosphorylation. The properties of PK-II resemble those recently described for a class of polypeptide-dependent protein kinases isolated from placenta, Ehrlich ascites tumor cells, and bakers' yeast. PK-II was significantly higher in psoriatic involved epidermis (32.6 +/- 11.6 pmol/min/mg protein) compared to psoriatic uninvolved epidermis (5.7 +/- 0.6 pmol/min/mg; p = 0.03) and normal epidermis (9.5 +/- 2.2 pmol/min/mg; p = 0.05). The function of histone stimulated protein kinase in epidermal function and its role in the pathophysiology of psoriasis remain to be explored. |
| Databáze: | OpenAIRE |
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