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Evidence of myofibrillar protein oxidation induced by postischemic reperfusion in isolated rat hearts

¹Dipartimento di Chimica Biologica and ²Sezione Biomembrane, Istituto di Neuroscienze del Consiglio Nazionale delle Ricerca, Università di Padova, 35121 Padova, Italy; and ³Departments of Physiology and Biochemistry, Queen's University, Kingston, Ontario, Canada K7L 3N6

Submitted 24 July 2003 ; accepted in final form 3 November 2003

Although the contribution of reactive oxygen species to myocardial ischemia is well recognized, the possible intracellular targets, especially at the level of myofibrillar proteins (MP), are not yet fully characterized. To assess the maximal extent of oxidative degradation of proteins, isolated rat hearts were perfused with 1 mM H₂O₂. Subsequently, the MP maximally oxidative damage was compared with the effects produced by 1) 30 min of no-flow ischemia (I) followed in other hearts by 3 min of reperfusion (I/R); and 2) I/R in the presence of a potent antioxidant N-(2-mercaptopropionyl)glycine (MPG). Samples from the H₂O₂ group electrophoresed under nonreducing conditions and probed with actin, desmin, or tropomyosin monoclonal antibodies showed high-molecular mass complexes indicative of disulfide cross-bridges along with splitting and thickening of tropomyosin and actin bands, respectively. Only these latter changes could be detected in I/R samples and were prevented by MPG. Carbonyl groups generated by oxidative stress on MP were detected by Western blot analysis (oxyblot) under optimized conditions. The analyses showed one major band corresponding to oxidized actin, the density of which increased 1.2-, 2.8-, and 6.8-fold in I, I/R, and H₂O₂ groups, respectively. The I/R-induced increase was significantly reduced by MPG. In conclusion, oxidative damage of MP occurs on reperfusion, although at a lower extent than in H₂O₂ perfused hearts, whereas oxidative modifications could not be detected in ischemic hearts. Furthermore, the inhibition of MP oxidation by MPG might underlie the protective efficacy of antioxidants.

actin; tropomyosin; oxidative stress; protein carbonylation; free radicals

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