Temperature and RyR1 regulate the activation rate of store-operated Ca²+ entry current in myotubes.

ABSTRACT: Store-operated calcium entry (SOCE) is an important Ca(2+) entry pathway in skeletal muscle. However, direct electrophysiological recording and full characterization of the underlying SOCE current in skeletal muscle cells (I(SkCRAC)) has not been reported. Here, we characterized the biophysical properties, pharmacological profile, and molecular identity of I(SkCRAC) in skeletal myotubes, as well as the regulation of its rate of activation by temperature and the type I ryanodine receptor (RyR1). I(SkCRAC) exhibited many hallmarks of Ca(2+) release activated Ca(2+) currents (I(CRAC)): store dependence, strong inward rectification, positive reversal potential, limited cesium permeability, and sensitivity to SOCE channel blockers. I(SkCRAC) was reduced by siRNA knockdown of stromal interaction

SUBMITTER: Yarotskyy V 

PROVIDER: S-EPMC3400782 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature