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Uwe Kirchhefer; Gabriela Hanske; Larry R. Jones; Isabel Justus; Lars Kaestner; Peter Lipp; Wilhelm Schmitz; Joachim Neumann (Profiled Author: Larry R. Jones)
Cell Calcium. 2006;39(2):131-142.Abstract
In cardiac muscle, junctin forms a quaternary protein complex with the ryanodine receptor (RyR), calsequestrin, and triadin 1 at the luminal face of the junctional sarcoplasmic reticulum (jSR). By binding directly the RyR and calsequestrin, junctin may mediate the Ca2+ -dependent regulatory interactions between both proteins. To gain more insight into the underlying mechanisms of impaired contractile relaxation in transgenic mice with cardiac-specific overexpression of junctin (TG), we studied cellular Ca2+ handling in these mice. We found that the SR Ca2+ load was reduced by 22% in cardiomyocytes from TG mice. Consistent with this, the frequency of Ca2+ sparks was diminished by 32%. The decay of spontaneous Ca2+ sparks was prolonged by 117% in TG. This finding was associated with a lower Na+-Ca2+ exchanger (NCX) protein expression (by 67%) and a higher basal RyR phosphorylation at Ser2809 (by 64%) in TG. The shortening- and Δ[Ca]
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