[Changes in the cAMP-dependent phosphorylation system of myocardial sarcoplasmic reticulum components during circulatory hypoxia].
The dissociation of the holoenzyme of the cAMP-dependent protein kinase was induced by the adrenaline-stimulated endogenous cAMP synthesis. This dissociation was impaired in a hypoxic muscle. The elevated proteolytic activity in the hypoxic area was found to be associated with the reduction of the 33P incorporation into phospholamban in the presence of 10(-6) M cAMP. No changes were observed when protein kinase was added to the incubation mixture. A correlation between the degree of phospholamban phosphorylation and its susceptibility to proteolysis was demonstrated.
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D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002135:Calcium-Binding Proteins / Q000494:pharmacology; D003327:Coronary Disease / Q000201:enzymology / Q000209:etiology / Q000378:metabolism*; D000242:Cyclic AMP / Q000378:metabolism*; D004285:Dogs; D008861:Microsomes / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D012519:Sarcoplasmic Reticulum / Q000201:enzymology; D012769:Shock / Q000150:complications / Q000201:enzymology / Q000378:metabolism*; D014357:Trypsin / Q000494:pharmacology; D000099211:Phospholamban
D000255:Adenosine Triphosphate; D002135:Calcium-Binding Proteins; D000242:Cyclic AMP; D011494:Protein Kinases; D014357:Trypsin; D000099211:Phospholamban
Izmeneniia v sisteme cAMP-zavisimogo fosforilirovaniia komponentov sarkoplazmaticheskogo retikuluma miokarda pri tsirkuliatornoĭ gipoksii.