Prostaglandin regulation of adenylate kinases purifed from liver, skeletal muscle, and hepatoma.
Adenylate kinases, purified from adult rat liver and skeletal muscle and from a fast growing hepatoma, were examined in the presence of a series of prostaglandins. Prostaglandins A1, A2, E1, E2 and F2alpha stimulated liver adenylate kinase 27% to 149%. All of these protaglandins stimulated the skeletal muscle enzyme from 47% to 82%. While prostaglandins A2 and E2 stimulated, prostaglandins A1 and F2alpha inhibited, and prostaglandin E1 was without effect on the hepatoma adenylate kinase.
D000263:Adenylate Kinase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D006528:Carcinoma, Hepatocellular / Q000201:enzymology*; D008099:Liver / Q000201:enzymology*; D008113:Liver Neoplasms / Q000201:enzymology*; D009132:Muscles / Q000201:enzymology*; D009374:Neoplasms, Experimental / Q000201:enzymology; D010770:Phosphotransferases / Q000378:metabolism*; D011453:Prostaglandins / Q000494:pharmacology*; D051381:Rats; D013268:Stimulation, Chemical
D011453:Prostaglandins; D010770:Phosphotransferases; D000263:Adenylate Kinase