Early presence of phospholamban in developing a chick heart.
Phosphorylation of phospholamban and development of reticular Ca2+ transport were studied in crude membrane preparations of embryonic, newborn and adult chick heart. Maximal phosphorylation of phospholamban by added catalytic subunit of cyclic AMP-dependent protein kinase increases from embryonic day 4-15. It decreases with further development. In the same membrane preparations active Ca2+-uptake into vesicles of sarcoplasmic reticulum rises from day 4-7 and decreases then slightly until day 20. A several-fold increase in Ca2+-transport activity occurs at the time of hatching. The data indicate separate genetic control for synthesis of phospholamban and sarcoplasmic reticulum Ca2+-ATPase.
D000375:Aging; D000818:Animals; D001692:Biological Transport; D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000302:isolation & purification*; D002642:Chick Embryo; D002645:Chickens; D006321:Heart / Q000196:embryology / Q000254:growth & development*; D009206:Myocardium / Q000378:metabolism*; D010766:Phosphorylation; D000099211:Phospholamban
D002118:Calcium; D002135:Calcium-Binding Proteins; D000099211:Phospholamban