World Journal of
Pharmaceutical and Life Sciences

MYOGLOBIN EXHIBITS INCREASED IRON RELEASE AND FREE RADICAL MEDIATED OXIDATION REACTION ON ΑLPHA-OXOALDEHYDE MODIFICATION: HEME PROTEIN AS A POTENTIAL SOURCE OF OXIDATIVE STRESS

Sauradipta Banerjee*

ABSTRACT

Post-translational modification of proteins by Maillard reaction, known as glycation, is thought to be the root cause of different complications, including oxidative stress, particularly in diabetes mellitus and age-related disorders. The reactive α-oxoaldehydes, glyoxal and methylglyoxal, increases in diabetic condition and reacts with proteins to form advanced glycation end products (AGEs) following Maillard-like reaction. In this study, we report that H2O2-induced iron release from glyoxal or methylglyoxal-incubated myoglobin is significantly higher than that from unmodified myoglobin. Further, in presence of H2O2, modified myoglobin degrades deoxyribose more efficiently than the unmodified protein. Considering the increased level of α-dicarbonyls in diabetic condition, glyoxal or methylglyoxal-induced modification of the heme protein may enhance oxidative damage via Fenton reaction and associated complications. The findings thus appear physiologically relevant with clinical implications.

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