Cyclic nucleotide phosphodiesterase activity of human normal and carcinomatous lung tissue.
The activity of the phosphodiesterase enzyme(s) responsible for the degradation of cylic adenosine monophosphate (CA.M.P.) and cyclic guanosine monophosphate (CG.M.P. (in human normal and carcinomatous lung tissue has been investigated. Enzyme activities were 3-5 times greater in normal than in carcinomatous lung. This is compatible with the known higher concentrations of these cyclic nucleotides in normal tissues. It is suggested that cancer chemotherapy designed to block the phosphodiesterase activity, and thus promote accretion of CA.M.P and CG.M.P., may provide a means of normalising cancerous tissue. Both phosphodiesterase activities in both types of tissue were inhibited by methylxanthines at 10(-3) mol/l, but some enzyme potentiation was observed at lower concentration.
D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002110:Caffeine / Q000494:pharmacology; D002294:Carcinoma, Squamous Cell / Q000201:enzymology*; D000242:Cyclic AMP / Q000378:metabolism; D006152:Cyclic GMP / Q000378:metabolism; D005260:Female; D006801:Humans; D008168:Lung / Q000201:enzymology* / Q000378:metabolism; D008175:Lung Neoplasms / Q000201:enzymology*; D008875:Middle Aged; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D013806:Theophylline / Q000494:pharmacology
D002110:Caffeine; D013806:Theophylline; D000242:Cyclic AMP; D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases; D010727:Phosphoric Diester Hydrolases; D006152:Cyclic GMP