Protein kinases activated by cAMP in the genital tract of spayed mice treated with oestradiol-17beta.
The cAMP-dependent protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37), has been studied in the vaginal epithelium, vaginal stroma, endometrium, and whole uterus of spayed mice treated with oestradiol-17 beta, and in the vaginal epithelium and uterus of spayed mice. Two protein kinase isoenzymes (PK I and PK II) were found in whole uterus, endometrium, and vaginal stroma. Vaginal epithelium contained only one isoenzyme (PK II). Oestradiol treatment increased PK I relative to PK II in the uterus. The isoenzyme pattern in the vaginal epithelium was unaltered after such treatment. The total protein kinase activity was 70% higher in uterine extracts (cytosol) than in extracts from vaginal epithelium. Oestradiol treatment did not influence the total protein kinase activity in either tissue.
D000818:Animals; D002369:Castration; D000242:Cyclic AMP / Q000494:pharmacology*; D004717:Endometrium / Q000201:enzymology; D004789:Enzyme Activation; D004848:Epithelium / Q000201:enzymology; D004958:Estradiol / Q000494:pharmacology*; D005260:Female; D005836:Genitalia, Female / Q000201:enzymology*; D007527:Isoenzymes / Q000378:metabolism; D051379:Mice; D011494:Protein Kinases / Q000378:metabolism*; D014599:Uterus / Q000201:enzymology; D014621:Vagina / Q000201:enzymology
D007527:Isoenzymes; D004958:Estradiol; D000242:Cyclic AMP; D011494:Protein Kinases