Regulation of the Ca2+ pump atpase by cAMP‐dependent phosphorylation of phospholamban
- 1 May 1989
- Vol. 10 (5) , 157-163
- https://doi.org/10.1002/bies.950100505
Abstract
Ca2+ transients in myocardial cells are modulated by cyclic AMP‐dependent phosphorylation of a protein in the sarcoplasmic reticulum. This protein, termed phospholamban, serves to regulate the Ca2+ pump ATPase of this membrane, thus altering the mode of Ca2+ transients and the myocardial contractile response. Elucidating the structure of phospholamban and its intimate interaction with the Ca2+ pump ATPase should provide the basis for understanding, at the molecular level, how the cAMP system contributes to excitation‐contraction coupling in muscle cells.Keywords
This publication has 53 references indexed in Scilit:
- Localization of phospholamban in smooth muscle using immunogold electron microscopy.The Journal of cell biology, 1988
- Rabbit cardiac and slow‐twitch muscle express the same phospholamban geneFEBS Letters, 1988
- Partial purification and characterization of thrombolamban, A 22,000 dalton cAMP-dependent protein kinase substrate in plateletsBiochemical and Biophysical Research Communications, 1987
- Complete complementary DNA-derived amino acid sequence of canine cardiac phospholamban.Journal of Clinical Investigation, 1987
- Proteolytic activation of the canine cardiac sarcoplasmic reticulum calcium pumpBiochemistry, 1986
- Characterization of structural unit of phospholamban by amino acid sequencing and electrophoretic analysisBiochemical and Biophysical Research Communications, 1986
- Two Ca2+ ATPase genes: Homologies and mechanistic implications of deduced amino acid sequencesCell, 1986
- Phospholamban phosphorylation in the perfused rat heart is not solely dependent on β-adrenergic stimulationFEBS Letters, 1980
- Phosphodiesterase protein activator stimulates calcium transport in cardiac microsomal preparations enriched in sarcoplasmic reticulumBiochemical and Biophysical Research Communications, 1978