Regulatory role of phospholamban in the efficiency of cardiac sarcoplasmic reticulum Ca2+ transport

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@article{b1d4e6749b774425a49640193a14b5f7,
title = "Regulatory role of phospholamban in the efficiency of cardiac sarcoplasmic reticulum Ca2+ transport",
abstract = "Phospholamban is an inhibitor of the sarcoplasmic reticulum Ca2+ transport apparent affinity for Ca2+ in cardiac muscle. This inhibitory effect of phospholamban can be relieved through its phosphorylation or ablation. To better characterize the regulatory mechanism of phospholamban, we examined the initial rates of Ca2+-uptake and Ca2+-ATPase activity under identical conditions, using sarcoplasmic reticulum-enriched preparations from phospholamban-deficient and wild-type hearts. The apparent coupling ratio, calculated by dividing the initial rates of Ca2+ transport by ATP hydrolysis, appeared to increase with increasing [Ca2+] in wild-type hearts. However, in the phospholamban-deficient hearts, this ratio was constant, and it was similar to the value obtained at high [Ca2+] in wild-type hearts. Phosphorylation of phospholamban by the catalytic subunit of protein kinase A in wild-type sarcoplasmic reticulum also resulted in a constant value of the apparent ratio of Ca2+ transported per ATP hydrolyzed, which was similar to that present in phospholamban-deficient hearts. Thus, the inhibitory effects of dephosphorylated phospholamban involve decreases in the apparent affinity of sarcoplasmic reticulum Ca2+ transport for Ca2+ and the efficiency of this transport system at low [Ca2+], both leading to prolonged relaxation in myocytes.",
author = "K. Frank and C. Tilgmann and Shannon, {T. R.} and Bers, {D. M.} and Kranias, {E. G.}",
year = "2000",
month = "11",
day = "21",
doi = "10.1021/bi001049k",
language = "English",
volume = "39",
pages = "14176--14182",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "The American Chemical Society (ACS)",
number = "46",

}