Comparison of cyclic AMP-dependent phosphorylation of sarcolemma and sarcoplasmic reticulum from rat cardiac ventricle muscle.
1. The phosphorylation by cAMP and protein kinase I of rat cardiac sarcolemma (SL) and sarcoplasmic reticulum (SR) isolated from the same homogenate, was compared. 2. In both fractions, the phosphate incorporation is strongly dependent on the ATP and the membrane protein concentration. 3. SDS-gel electrophoresis reveals that in the SL preparation a protein of Mr = 24,500 and a glycoprotein of Mr = 17,500 are mainly phosphorylated, while in the SR fraction the main phosphate incorporation is found in a protein having a Mr = 37,000. 4. Isoprenaline stimulates the phosphorylation of SL but not of SR. Propranolol abolished that stimulatory action of isoprenaline completely, suggesting that the beta-adrenoceptor is involved.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D000242:Cyclic AMP / Q000502:physiology*; D005260:Female; D006352:Heart Ventricles / Q000378:metabolism; D008297:Male; D009206:Myocardium / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D012508:Sarcolemma / Q000378:metabolism*; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*
D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D011494:Protein Kinases