Title : Oxygen-coupled redox regulation of the skeletal muscle ryanodine receptor/Ca2+ release channel (RyR1): sites and nature of oxidative modification.

Pub. Date : 2013 Aug 9

PMID : 23798702






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 S-Oxidation of RyR1 is coupled to muscle oxygen tension (pO2) through O2-dependent production of hydrogen peroxide by SR-resident NADPH oxidase 4. PO-2 ryanodine receptor 1 Homo sapiens
2 In isolated SR (SR vesicles), an average of six to eight Cys thiols/RyR1 monomer are reversibly oxidized at high (21% O2) versus low pO2 (1% O2), but their identity among the 100 Cys residues/RyR1 monomer is unknown. PO-2 ryanodine receptor 1 Homo sapiens
3 Here we use isotope-coded affinity tag labeling and mass spectrometry (yielding 93% coverage of RyR1 Cys residues) to identify 13 Cys residues subject to pO2-coupled S-oxidation in SR vesicles. PO-2 ryanodine receptor 1 Homo sapiens