Role of membrane integrity and cation interaction for heart sarcolemmal adenylate cyclase and Na+-K+ ATPase.
The adenylate cyclase and Na+ -K+ ATPase activities decreased on storage at 4 degrees C as well as on freezing and thawing of the rat heart sarcolemma. Treatment of the sarcolemmal fraction with phospholipase C and trypsin also depressed the adenylate cyclase and Na+ -K+ ATPase activities; the Na+ -K+ ATPase was more sensitive to these treatments than the adenylate cyclase. When the sarcolemmal enzyme activities were determined in the presence of different concentrations of some cations the adenylate cyclase activity was enhanced and the Na+ -K+ ATPase activity was depressed by monovalent cations (Na+, K+, Rb+, Cs+, Li+, and NH+4). Divalent cations such as Sr2+, Ba2+, Co2+, and Mn2+ had biphasic or no effects on the adenylate cyclase activity but inhibited the Na+ -K+ ATPase activity. Although Ca2+, Ni2+, Cd2+, Cu2+, Hg2+, and Zn2+ depressed both Na+ -K+ ATPase and adenylate cyclase activities, the degree of inhibition of these enzymes was different. These results reveal the role of membrane integrity for full expression of the adenylate cyclase and Na+ -K+ ATPase activities, whereas both monovalent and divalent cations appear to regulate sarcolemma-bound enzyme activities.
D000262:Adenylyl Cyclases / Q000378:metabolism*; D000818:Animals; D004573:Electrolytes / Q000378:metabolism; D007473:Ion Channels / Q000201:enzymology*; D008565:Membrane Proteins / Q000378:metabolism; D009206:Myocardium / Q000201:enzymology*; D010743:Phospholipids / Q000378:metabolism; D051381:Rats; D012508:Sarcolemma / Q000201:enzymology*; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*
D004573:Electrolytes; D007473:Ion Channels; D008565:Membrane Proteins; D010743:Phospholipids; D000262:Adenylyl Cyclases; D000254:Sodium-Potassium-Exchanging ATPase