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Biochemical and biophysical research communications

The hydrophilic domain of phospholamban inhibits the Ca(2+)-ATPase--the importance of the method of assay.


PMID 7488032

Abstract

The peptide MEKVQYLTRSAIRRASTIEMPQQAR-Cys representing residues 1-25 of phospholamban (PLN) decreases by 40% the maximal state rate of ATP hydrolysis by the Ca(2+)-ATPase of skeletal muscle sarcoplasmic reticulum (SR), measured at saturating concentrations of Ca2+. The pattern of Ca2+ uptake by SR vesicles in the presence of oxalate is complex, with an initial fast phase being followed by a lag phase and a second, slower phase of Ca2+ accumulation. PLN(1-25) reduces the rate of the slower phase of Ca2+ accumulation by 30%. However, if the level of accumulation of Ca2+ is measured after 2 min., the effect of PLN(1-25) is much less marked. It is concluded that PLN(1-25) inhibits the ATPase, but that the effects of this inhibition are not apparent under some assay conditions.