Adenylate cyclase, cyclic nucleotide phosphodiesterase, and phosphorylase activity of cardiomyopathic hamster hearts.
Activities of adenylate cyclase in homogenates were reduced, whereas those of phosphodiesterases were elevated in hearts of myopathic hamsters (BIO 82.62). Affinities for either Mg2+ or ATP of cyclase were unaffected in myopathy. Ca2+ stimulation particulate phosphodiesterases was not observed in myopathy. Although the cardiac phosphorylase content was reduced at the advanced stages of myopathy,-AMP/+AMP ratios remained similar to those found in normal hearts.
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000378:metabolism*; D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000378:metabolism*; D000262:Adenylyl Cyclases / Q000378:metabolism*; D000375:Aging; D000818:Animals; D009202:Cardiomyopathies / Q000201:enzymology*; D006224:Cricetinae; D004837:Epinephrine / Q000494:pharmacology; D006321:Heart / Q000254:growth & development; D008647:Mesocricetus; D009124:Muscle Proteins / Q000378:metabolism; D009206:Myocardium / Q000201:enzymology*; D006005:Phosphorylases / Q000378:metabolism*
D009124:Muscle Proteins; D006005:Phosphorylases; D015105:3',5'-Cyclic-AMP Phosphodiesterases; D015106:3',5'-Cyclic-GMP Phosphodiesterases; D000262:Adenylyl Cyclases; D004837:Epinephrine