3',5'-cyclic-nucleotide-dependent protein kinase of squamous cell carcinoma of the prostate.
An adenosine 3'5'-cyclic-monophosphate (Cyclic AMP)-dependent protein kinase has been identified and partially purified from the rat prostate tumor induced by 20-methylcholanthrene. This enzyme is stimulated 2- to 3-fold by the nucleotide. Equilibrium studies at pH 5.0 suggest the presence of a major class of binding site for cyclic AMP with an association constant of approximately 10(8) M-1. The concentration of binding site is about 1 pmol/mg of protein of the enzyme preparation. The enzyme is stimulated by other cyclic nucleotides as well, but only by higher concentrations. In comparing the ability of different histone subfractions, casein and protamine, to serve as substrate for this particular protein kinase, maximal cyclic-AMP-dependent enzyme activity was observed with histones. The results suggest that factors contributing to the malignant growth of the prostatic tissue do not directly involve changes in the characteristics of a cyclic-AMP-dependent protein kinase.
D000818:Animals; D002294:Carcinoma, Squamous Cell / Q000201:enzymology*; D000242:Cyclic AMP / Q000494:pharmacology*; D008297:Male; D009374:Neoplasms, Experimental / Q000201:enzymology; D009712:Nucleotides, Cyclic / Q000494:pharmacology*; D011471:Prostatic Neoplasms / Q000201:enzymology*; D011485:Protein Binding; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D013329:Structure-Activity Relationship
D009712:Nucleotides, Cyclic; D000242:Cyclic AMP; D011494:Protein Kinases