In vitroinhibition of α-glucosidases and glycogenphosphorylase by catechingallates in greentea

Abstract

We investigated in vitroinhibition of mammalian carbohydrate-degrading enzymes by greentea extract and the component catechins, and further evaluated their inhibitory activities in cell cultures. The extract showed good inhibition toward rat intestinal maltase and rabbit glycogenphosphorylase (GP) b, with IC50 values of 45 and 7.4 μg/ml, respectively. The polyphenol components, catechin 3-gallate (CG), gallocatechin 3-gallate (GCG), epicatechin 3-gallate (ECG), and epigallocatechin 3-gallate (EGCG), were good inhibitors of maltase, with IC50 values of 62, 67, 40, and 16 μM, respectively, and EGCG also showed good inhibition toward maltase expressed on Caco-2 cells, with an IC50 value of 27 μM. The ungallated catechins, such as catechin, gallocatechin (GC), epicatechin (EC), and epigallocatechin (EGC), showed no significant inhibition toward GP b, whereas the gallated catechins CG, GCG, ECG, and EGCG inhibited the enzyme, with IC50 values of 35, 6.3, 27, and 34 μM. From multiple inhibition studies by Dixon plots, GCG appears to bind a new allostelic site, the indole inhibitor site. These gallated catechins also inhibited glucagon-stimulated glucose production dose-dependently, with IC50 values ranging from 33 to 55 μM. Dietary supplementation with these gallated catechins or the greentea extract containing them, which inhibits both α-glucosidases and GP in vitro and in cell culture, would contribute to the protection or improvement of type 2 diabetes.