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J. Biol. Chem., Vol. 259, Issue 13, 8029-8032, Jul, 1984
MA Movsesian, M Nishikawa and RS Adelstein
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.
Phosphorylation of phospholamban by calcium-activated, phospholipid- dependent protein kinase. Stimulation of cardiac sarcoplasmic reticulum calcium uptake
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