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

  
@article{APS4015,
	author = {Hong-mei Han and Ri-sheng Wei and Anthony F Lai and Chang-cheng Yin},
	title = {Molecular nature of sulfhydryl modification by hydrogen peroxide on type 1 ryanodine receptor},
	journal = {Acta Pharmacologica Sinica},
	volume = {27},
	number = {7},
	year = {2016},
	keywords = {},
	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.},
	issn = {1745-7254},	url = {http://www.chinaphar.com/article/view/4015}
}