Regulation of the Cardiac Muscle Ryanodine Receptor by O2Tension andS-Nitrosoglutathione
Citations Over TimeTop 10% of 2008 papers
Abstract
The cardiac and skeletal muscle sarcoplasmic reticulum ryanodine receptor Ca(2+) release channels contain thiols that are potential targets of endogenously produced reactive oxygen and nitrogen intermediates. Previously, we showed that the skeletal muscle ryanodine receptor (RyR1) has O(2)-sensitive thiols; only when these thiols are in the reduced state (pO(2) approximately 10 mmHg) can physiological concentrations of NO (nanomolar) activate RyR1. Here, we report that cardiac muscle ryanodine receptor (RyR2) activity also depends on pO(2), but unlike RyR1, RyR2 was not activated or S-nitrosylated directly by NO. Rather, activation and S-nitrosylation of RyR2 required S-nitrosoglutathione. The effects of peroxynitrite were indiscriminate on RyR1 and RyR2. Our results indicate that both RyR1 and RyR2 are pO(2)-responsive yet point to different mechanisms by which NO and S-nitrosoglutathione influence cardiac and skeletal muscle sarcoplasmic reticulum Ca(2+) release.
Related Papers
- → Reduced threshold for store overload-induced Ca2+ release is a common defect of RyR1 mutations associated with malignant hyperthermia and central core disease(2017)30 cited
- → Skeletal and Cardiac Ryanodine Receptors Exhibit Different Responses to Ca2+ Overload and Luminal Ca2+(2007)36 cited
- → Two EF-hand motifs in ryanodine receptor calcium release channels contribute to isoform-specific regulation by calmodulin(2017)11 cited
- → A negatively charged region of the skeletal muscle ryanodine receptor is involved in Ca2+‐dependent regulation of the Ca2+ release channel(1999)18 cited
- → Distinct mechanisms for dysfunctions of mutated ryanodine receptor isoforms(2007)3 cited