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. 2014 Aug 27;19(9):13212-24.
doi: 10.3390/molecules190913212.

Inhibitory effects of Colocasia esculenta (L.) Schott constituents on aldose reductase

Affiliations

Inhibitory effects of Colocasia esculenta (L.) Schott constituents on aldose reductase

Hong Mei Li et al. Molecules. .

Abstract

The goal of this study was to determine the rat lens aldose reductase-inhibitory effects of 95% ethanol extracts from the leaves of C. esculenta and, its organic solvent soluble fractions, including the dichloromethane (CH2Cl2), ethyl acetate (EtOAc), n-butanol (BuOH) and water (H2O) layers, using dl-glyceraldehyde as a substrate. Ten compounds, namely tryptophan (1), orientin (2), isoorientin (3), vitexin (4), isovitexin (5), luteolin-7-O-glucoside (6), luteolin-7-O-rutinoside (7), rosmarinic acid (8), 1-O-feruloyl-d-glucoside (9) and 1-O-caffeoyl-d-glucoside (10) were isolated from the EtOAc and BuOH fractions of C. esculenta. The structures of compounds 1-10 were elucidated by spectroscopic methods and comparison with previous reports. All the isolates were subjected to an in vitro bioassay to evaluate their inhibitory activity against rat lens aldose reductase. Among tested compounds, compounds 2 and 3 significantly inhibited rat lens aldose reductase, with IC50 values of 1.65 and 1.92 μM, respectively. Notably, the inhibitory activity of orientin was 3.9 times greater than that of the positive control, quercetin (4.12 μM). However, the isolated compounds showed only moderate ABTS+ [2,29-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid)] activity. These results suggest that flavonoid derivatives from Colocasia esculenta (L.) Schott represent potential compounds for the prevention and/or treatment of diabetic complications.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Structures of the constituents isolated from Colocasia esculenta (L.) Schott.
Figure 2
Figure 2
Lineveaver-Burk plots showing the reciprocal of the velocity (1/v) of recombinant rat lens aldose reductase versus the reciprocal of the substrate concentration (1/s) with dl-glyceraldehyde as the substrate at concentrations of 0.1 to 1 mM.

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