Journal
ACTA PHARMACOLOGICA SINICA
Volume 27, Issue 7, Pages 888-894Publisher
ACTA PHARMACOLOGICA SINICA
DOI: 10.1111/j.1745-7254.2006.00386.x
Keywords
Ca2+ release channel; ryanodine receptor; hydrogen peroxide; reactive oxygen; redox-sensitive ion channel
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Aim: To elucidate the molecular nature of sulfhydryl modification by hydrogen peroxide on type 1 ryanodine receptor (RyR1). Methods: Rabbit skeletal muscle sarcoplasmic reticulum was treated with hydrogen peroxide, then RyR1 complex was isolated. The proteins in the complex were analysed by electrophoresis, Western blot and electron microscopy. Results: (1) Hydrogen peroxide induces inter-subunit cross-linking within the tetrameric RyR1 molecule; (2) in parallel to inter-subunit cross-linking, the RyR1 molecule changes morphology; (3) the chemical and morphological changes are reversible: upon reduction by reducing agents, the RyR1 molecule regains its original state. Conclusion: These findings suggest that the molecular mechanism of RyR1 channel activity in sarcoplasmic reticulum regulated by hydrogen peroxide is through inter-subunit cross-linking within the tetrameric RyR1 molecule, which in turn induces structural changes of RyR1.
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