Abstract
The cardiac sarco/endoplasmic reticulum Ca2+-ATPase (SERCA2a) plays a critical role in both contraction and relaxation of the heart by sequestering intracellular Ca2+ in the sarcoplasmic reticulum (SR). SERCA transport activity is tightly regulated to adjust cardiac performance for exercise and rest. The principal regulator of SERCA is phospholamban (PLB), which binds to the pump and reduces its affinity for Ca2+. We previously demonstrated that the PLB-SERCA binding equilibrium shifts slightly in response to sustained Ca2+ elevations, with a modest decrease in PLB-SERCA affinity in high Ca2+.
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