[3':5'-AMP-dependent phosphorylation of muscular membrane proteins and calcium transport].
The data are presented concerning the role of cAMP-dependent phosphorylation of sarcoplasmic reticulum and sarcolemma proteins in the transport of Ca2+ through the cardiac skeletal and smooth muscle membranes. Phosphorylation of membrane proteins by soluble and membrane-bound cAMP-dependent protein kinases is shown to have a regulating effect on Mn2+-, Ca2+-ATPase activity and to change membrane permeability for Ca2+. The molecular mechanisms and the character of the interaction between the transport systems and the phosphorylating protein substrates have not been yet established.
D000818:Animals; D001692:Biological Transport; D002118:Calcium / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D000242:Cyclic AMP / Q000494:pharmacology*; D004789:Enzyme Activation; D008565:Membrane Proteins / Q000378:metabolism*; D009130:Muscle, Smooth / Q000378:metabolism; D009132:Muscles / Q000378:metabolism*; D009206:Myocardium / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D012508:Sarcolemma / Q000378:metabolism; D012519:Sarcoplasmic Reticulum / Q000378:metabolism
D008565:Membrane Proteins; D000242:Cyclic AMP; D011494:Protein Kinases; D000252:Calcium-Transporting ATPases; D002118:Calcium
3':4'-AMP-zavisimoe fosforilirovanie belkov membran myshchts i transport kal'tsiia.