Oxidation of myoglobin in isolated adult rat cardiac myocytes by 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid.
The oxidation of intracellular myoglobin by 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid was studied in suspensions of isolated adult rat heart cells. Myoglobin was converted to a species identified as ferrylMb by its reaction with Na2S to form ferrous sulfmyoglobin. This process was time-dependent and concentration-dependent in a manner consistent with direct accessibility of the exogenous peroxide to the cytosolic protein. The results indicate that myoglobin oxidation may be an early sign of oxidative injury and may limit myocardial function by elimination of this short-term O2 reserve.
D000818:Animals; D001095:Arachidonic Acids / Q000378:metabolism*; D066298:In Vitro Techniques; D015289:Leukotrienes; D008054:Lipid Peroxides; D008297:Male; D009206:Myocardium / Q000378:metabolism* / Q000473:pathology; D009211:Myoglobin / Q000378:metabolism*; D010084:Oxidation-Reduction; D051381:Rats; D013053:Spectrophotometry
D001095:Arachidonic Acids; D015289:Leukotrienes; D008054:Lipid Peroxides; D009211:Myoglobin; C025086:15-hydroperoxy-5,8,11,13-eicosatetraenoic acid