Journal of Diabetes · 2015 · 30 citations · 23 references
Life SciencesBiochemistryPharmacologyDiabetologyEnzymologyRedox BiochemistryAntioxidant DefenseCarbohydrate MetabolismDiabetes MellitusDiabetes Mellitus BiochemistryDiabetes PharmacotherapyGlycemic ControlAntidiabetic ActivityAntidiabetic Drug TherapyAntioxidant Activity AssaysCatalase FunctionEnzyme ActivityEnzymesGlucose-lowering TherapyOxidative Stress In Diabetes
BACKGROUND: The aim of the present study was to examine the effect of aldehyde modification on antioxidant enzyme activity in diabetic patients. METHODS: The activity of commercially available antioxidant enzymes (catalase, glutathione peroxidase [GPx], and Cu,Zn-superoxide dismutase [SOD]) was determined in vitro prior to and after aldehyde modification. The activity of erythrocyte Cu,Zn-SOD was assayed in blood drawn from healthy donors, diabetic patients with decompensated carbohydrate metabolism, and diabetic patients after glucose-lowering therapy. RESULTS: In vitro aldehyde modification had no effect on catalase activity, but diminished GPx and Cu,Zn-SOD activity. In diabetic patients with decompensated carbohydrate metabolism, glucose-lowering therapy significantly increased Cu,Zn-SOD activity, the effect being especially pronounced after administration of metformin. CONCLUSIONS: It is likely that metformin antagonizes the aldehyde-induced inhibition of erythrocyte Cu,Zn-SOD in diabetic patients more effectively than sulfonylurea drugs.
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Metformin reduces systemic methylglyoxal levels in type 2 diabetes.
Paul J. Beisswenger, Scott K. Howell, Allison D. Touchette et al. · Diabetes · 1999 · 445 citations