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DOI: 10.1055/s-0033-1351101
Caffeoylated Phenylpropanoid Glycosides from Brandisia hancei Inhibit Advanced Glycation End Product Formation and Aldose Reductase in Vitro and Vessel Dilation in Larval Zebrafish in Vivo
Publication History
received 11 June 2013
revised 21 October 2013
accepted 27 October 2013
Publication Date:
28 November 2013 (online)
Abstract
In our continuing efforts to identify effective naturally sourced agents for diabetic complications, five caffeoylated phenylpropanoid glycosides, acteoside (1), isoacteoside (2), poliumoside (3), brandioside (4), and pheliposide (5) were isolated from the 80 % EtOH extract of Brandisia hancei stems and leaves. These isolates (1–5) were subjected to an in vitro bioassay evaluating their inhibitory activity on advanced glycation end product formation and rat lens aldose reductase activity. All tested compounds exhibited significant inhibition of advanced glycation end product formation with IC50 values of 4.6–25.7 µM, compared with those of aminoguanidine (IC50 = 1056 µM) and quercetin (IC50 = 28.4 µM) as positive controls. In the rat lens aldose reductase assay, acteoside, isoacteoside, and poliumoside exhibited greater inhibitory effects on rat lens aldose reductase with IC50 values of 0.83, 0.83, and 0.85 µM, respectively, than those of the positive controls, 3,3-tetramethyleneglutaric acid (IC50 = 4.03 µM) and quercetin (IC50 = 7.2 µM). In addition, the effect of acteoside on the dilation of hyaloid-retinal vessels induced by high glucose in larval zebrafish was investigated. Acteoside reduced the diameters of high glucose-induced hyaloid-retinal vessels by 69 % at 10 µM and 81 % at 20 µM, compared to the high glucose-treated control group. These results suggest that B. hancei and its active components might be beneficial in the treatment and prevention of diabetic vascular complications.
Key words
Brandisia hancei - Scrophulariaceae - phenylpropanoid glycoside - advanced glycation end-product - rat lens aldose reductase - zebrafish - diabetic vascular complications* These two authors contributed equally to this work.
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