Glucose autoxidation and protein modification The potential role of ‘autoxidative glycosylation’ in diabetes

Glucose autoxidation and protein modification The potential role of ‘autoxidative glycosylation’ in diabetes

1987 | Simon P. WOLFF* and Roger T. DEAN
The study explores the potential role of "autoxidative glycosylation" in diabetes, focusing on the impact of glucose autoxidation on protein modification. Monosaccharide autoxidation, a metal-catalyzed process that generates H₂O₂ and ketoaldehydes, is found to contribute to protein modification in vitro. The metal-chelating agent DETAPAC, which inhibits glucose autoxidation, also reduces the covalent attachment of glucose to bovine serum albumin (BSA). The extent of inhibition of metal-catalyzed glycosylation correlates with the inhibition of chromophore and fluorophore development. Ketoaldehydes produced by glucose autoxidation bind avidly to albumin and accelerate browning reactions. The study suggests that a component of protein glycosylation depends on glucose autoxidation and subsequent covalent attachment of ketoaldehydes. The process of glucose autoxidation and its products appear to be important in chromophoric and fluorophoric alterations. The concept of "autoxidative glycosylation" is discussed in relation to oxidative stress in diabetes mellitus.The study explores the potential role of "autoxidative glycosylation" in diabetes, focusing on the impact of glucose autoxidation on protein modification. Monosaccharide autoxidation, a metal-catalyzed process that generates H₂O₂ and ketoaldehydes, is found to contribute to protein modification in vitro. The metal-chelating agent DETAPAC, which inhibits glucose autoxidation, also reduces the covalent attachment of glucose to bovine serum albumin (BSA). The extent of inhibition of metal-catalyzed glycosylation correlates with the inhibition of chromophore and fluorophore development. Ketoaldehydes produced by glucose autoxidation bind avidly to albumin and accelerate browning reactions. The study suggests that a component of protein glycosylation depends on glucose autoxidation and subsequent covalent attachment of ketoaldehydes. The process of glucose autoxidation and its products appear to be important in chromophoric and fluorophoric alterations. The concept of "autoxidative glycosylation" is discussed in relation to oxidative stress in diabetes mellitus.
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