Calcium Regulation and Sensing

Dear Colleagues,

A very large Ca²⁺ gradient is maintained between the cytosol and sarcoplasmic reticulum/extracellula matrix. Transient elevations in cytoplasmic Ca²⁺ concentrations serve as a second messenger in most eukaryotic cells. Depolarization of cardiac muscle results in the entry of extracellular Ca²⁺ through slow Ca²⁺ channels (dihydropyridine receptors or DHPRs) located in the plasma membrane and transverse tubules. Myoplasmic Ca²⁺ concentrations are then further elevated by Ca²⁺-induced Ca²⁺ release through the Ca²⁺ release channel of the SR (ryanodine receptors or RyRs). The transient elevation of Ca²⁺ activates muscle contraction through its binding to the high affinity Ca²⁺ binding protein, troponin C (TnC), located in the thin filament. Relaxation is induced by the lowering of myoplasmic Ca²⁺ concentrations through the combined action of sarco(endo)plasmic reticulum Ca²⁺ ATPases (SERCAs), which are regulated by phospholamban (PLN) and sarcolipin (SLN), plasma membrane Ca²⁺ ATPases (PMCAs), which are regulated by calmodulin (CaM), and Na⁺/Ca²⁺ exchangers (NCXs). Ca²⁺ is stored in the lumen of the sarcoplasmic reticulum as a complex with an abundant Ca²⁺ binding protein, calsequestrin (CASQ). Functional alterations in this tightly regulated process are directly responsible for many pathophysiological conditions in humans.

We wish to invite articles directly dealing fundamentals of Ca²⁺ regulation, sensing, storage, and related pathophysiologies.

Dr. Chulhee Kang
Guest Editor

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