Effect and putative mechanism of action of ginseng on the formation of glycated hemoglobin in vitro

As a non-enzymatic, covalent binding between glucose and protein, glycation is a well-known cause of various forms of diabetic complications. This study was undertaken to determine the effect and mechanism of action of ginseng on the formation of glycated protein. A solution containing hemoglobin and glucose was incubated for 5 days by adding ginseng extract or glutathione. The quantitative measurement of glycated hemoglobin was determined using the ion capture component set. The anti-oxidative effect of ginseng and quercetin was determined through the TBA method. The amount of glycated hemoglobin (%GHb) significantly increased with the addition of glucose (27.8 mM) compared to the non-addition group. Nonetheless, this significantly decreased when ginseng extract (2 g/dl) was added and further dropped when glutathione (50 mM) was added. The amount of hemoglobin A(1c) (%HbA(1c)), a sub-fraction of glycated hemoglobin, was lower than that of glycated hemoglobin, but it showed a similar tendency. Compared to a non-addition group, the optical density of the organic layer that was separated through the addition of chloroform in oxidized linoleic acid significantly and dose-dependently decreased when ginseng extract or quercetin was added. These results suggest that the inhibitory effect of ginseng on the formation of glycated hemoglobin could be attributed to the anti-oxidative activity of ginseng. (C) 2003 Elsevier Ireland Ltd. All rights reserved.