[HTML][HTML] Nitric Oxide, NOC-12, and S-Nitrosoglutathione Modulate the Skeletal Muscle Calcium Release Channel/Ryanodine Receptor by Different Mechanisms: AN …
J Sun, L Xu, JP Eu, JS Stamler, G Meissner - Journal of biological chemistry, 2003 - ASBMB
The skeletal muscle Ca 2+ release channel/ryanodine receptor (RyR1) contains∼ 50 thiols
per subunit. These thiols have been grouped according to their reactivity/responsiveness
toward NO, O 2, and glutathione, but the molecular mechanism enabling redox active
molecules to modulate channel activity is poorly understood. In the case of NO, very low
concentrations (submicromolar) activate RyR1 byS-nitrosylation of a single cysteine residue
(Cys-3635), which resides within a calmodulin binding domain. S-Nitrosylation of Cys-3635 …
per subunit. These thiols have been grouped according to their reactivity/responsiveness
toward NO, O 2, and glutathione, but the molecular mechanism enabling redox active
molecules to modulate channel activity is poorly understood. In the case of NO, very low
concentrations (submicromolar) activate RyR1 byS-nitrosylation of a single cysteine residue
(Cys-3635), which resides within a calmodulin binding domain. S-Nitrosylation of Cys-3635 …