Original Article

Molecular nature of sulfhydryl modification by hydrogen peroxide on type 1 ryanodine receptor

Authors: Hong-mei Han, Ri-sheng Wei, Anthony F Lai, Chang-cheng Yin

Abstract

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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