{"title":"Catechin inhibits glycosidases, ameliorates glucose uptake and Glut-4 expression in 3T3-L1 adipocytes.","authors":"Kavishankar Gawli","doi":"10.1080/14786419.2024.2439007","DOIUrl":null,"url":null,"abstract":"<p><p>The research aimed to determine the inhibitory effects of different fractions of <i>Camellia sinensis</i> on α-glucosidase, α-amylase, glucose uptake, and Glut-4 expression in 3T3-L1 adipocytes and identification of the active principle. The crude aqueous extract was sequentially sub-fractionated using preparative HPLC and subjected to <i>in vitro</i> assays. Fraction 1 (F1) exhibited effective inhibition of both α-glucosidase and α-amylase with an IC<sub>50</sub> value of 90.31 µg/mL and 112.82 µg/mL, respectively. Sub-fraction 5 (F5) effectively inhibited α-glucosidase (IC<sub>50</sub> = 37.86 µg/mL) compared to acarbose (IC<sub>50</sub> = 76.19 µg/mL). The glucose uptake was significantly increased to 1.5 (<i>p</i> < 0.05) and 2.5-fold (<i>p</i> < 0.05) by F5 at 50 and 100 µM concentration, respectively. The synergistic effect of F1 to enhance glucose uptake (1.15 and 1.5-fold stimulation) was significantly higher than the control but less effective than F5. Furthermore, structure elucidation of the principle present in F5 revealed the presence of (2 R,3S)-2-(3,4-dihydroxyphenyl)-3,4-dihydro-2H-chromene-3,5,7-triol.</p>","PeriodicalId":18990,"journal":{"name":"Natural Product Research","volume":" ","pages":"1-7"},"PeriodicalIF":1.9000,"publicationDate":"2024-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Natural Product Research","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1080/14786419.2024.2439007","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
引用次数: 0
Abstract
The research aimed to determine the inhibitory effects of different fractions of Camellia sinensis on α-glucosidase, α-amylase, glucose uptake, and Glut-4 expression in 3T3-L1 adipocytes and identification of the active principle. The crude aqueous extract was sequentially sub-fractionated using preparative HPLC and subjected to in vitro assays. Fraction 1 (F1) exhibited effective inhibition of both α-glucosidase and α-amylase with an IC50 value of 90.31 µg/mL and 112.82 µg/mL, respectively. Sub-fraction 5 (F5) effectively inhibited α-glucosidase (IC50 = 37.86 µg/mL) compared to acarbose (IC50 = 76.19 µg/mL). The glucose uptake was significantly increased to 1.5 (p < 0.05) and 2.5-fold (p < 0.05) by F5 at 50 and 100 µM concentration, respectively. The synergistic effect of F1 to enhance glucose uptake (1.15 and 1.5-fold stimulation) was significantly higher than the control but less effective than F5. Furthermore, structure elucidation of the principle present in F5 revealed the presence of (2 R,3S)-2-(3,4-dihydroxyphenyl)-3,4-dihydro-2H-chromene-3,5,7-triol.
期刊介绍:
The aim of Natural Product Research is to publish important contributions in the field of natural product chemistry. The journal covers all aspects of research in the chemistry and biochemistry of naturally occurring compounds.
The communications include coverage of work on natural substances of land and sea and of plants, microbes and animals. Discussions of structure elucidation, synthesis and experimental biosynthesis of natural products as well as developments of methods in these areas are welcomed in the journal. Finally, research papers in fields on the chemistry-biology boundary, eg. fermentation chemistry, plant tissue culture investigations etc., are accepted into the journal.
Natural Product Research issues will be subtitled either ""Part A - Synthesis and Structure"" or ""Part B - Bioactive Natural Products"". for details on this , see the forthcoming articles section.
All manuscript submissions are subject to initial appraisal by the Editor, and, if found suitable for further consideration, to peer review by independent, anonymous expert referees. All peer review is single blind and submission is online via ScholarOne Manuscripts.