Phosphorylation of phospholamban by calcium-activated, phospholipid-dependent protein kinase. Stimulation of cardiac sarcoplasmic reticulum calcium uptake

Ca2+-activated, phospholipid-dependent protein kinase (protein kinase C) is able to catalyze the phosphorylation of phospholamban in a canine cardiac sarcoplasmic reticulum preparation. This phosphorylation is associated with a 2-fold stimulation of Ca2+ uptake by cardiac sarcoplasmic reticulum simi...

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Bibliographic Details
Published in:The Journal of biological chemistry 1984-07, Vol.259 (13), p.8029-8032
Main Authors: Movsesian, M A, Nishikawa, M, Adelstein, R S
Format: Article
Language:English
Subjects:
Animals
Calcium - metabolism
Calcium-Binding Proteins - metabolism
Calcium-Transporting ATPases - metabolism
Dogs
Myocardium - enzymology
Protein Kinase C
Protein Kinases - metabolism
Sarcoplasmic Reticulum - enzymology
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Summary:Ca2+-activated, phospholipid-dependent protein kinase (protein kinase C) is able to catalyze the phosphorylation of phospholamban in a canine cardiac sarcoplasmic reticulum preparation. This phosphorylation is associated with a 2-fold stimulation of Ca2+ uptake by cardiac sarcoplasmic reticulum similar to that seen following phosphorylation of phospholamban by an endogenous calmodulin-dependent protein kinase or by the catalytic subunit of cAMP-dependent protein kinase. Two-dimensional peptide maps of the tryptic fragments of phospholamban indicate that the three protein kinases differ in their selectivity for sites of phosphorylation. However, one common peptide appears to be phosphorylated by all three protein kinases. These findings suggest that protein kinase C may play a role similar to those played by cAMP- and calmodulin-dependent protein kinases in the regulation of Ca2+ uptake by cardiac sarcoplasmic reticulum, and raise the possibility that the effects of all three protein kinases are mediated through phosphorylation of a common peptide in phospholamban.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)39680-1