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α-glucosidase and glycation inhibitory effects of costus speciosus leaves
BACKGROUND: Hyperglycaemia is a salient feature of poorly controlled diabetes mellitus. Rate of protein glycation is increased with hyperglycaemia leading to long term complications of diabetes. One approach of controlling blood glucose in diabetes targets at reducing the postprandial spikes of bloo...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4700779/ https://www.ncbi.nlm.nih.gov/pubmed/26727889 http://dx.doi.org/10.1186/s12906-015-0982-z |
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author | Perera, Handunge Kumudu Irani Premadasa, Walgama Kankanamlage Vindhya Kalpani Poongunran, Jeyakumaran |
author_facet | Perera, Handunge Kumudu Irani Premadasa, Walgama Kankanamlage Vindhya Kalpani Poongunran, Jeyakumaran |
author_sort | Perera, Handunge Kumudu Irani |
collection | PubMed |
description | BACKGROUND: Hyperglycaemia is a salient feature of poorly controlled diabetes mellitus. Rate of protein glycation is increased with hyperglycaemia leading to long term complications of diabetes. One approach of controlling blood glucose in diabetes targets at reducing the postprandial spikes of blood glucose. The objectives of this study were to assess the in vitro inhibitory effects of Costus speciosus (COS) leaves on α-amylase and α-glucosidase activities, fructosamine formation, protein glycation and glycation-induced protein cross-linking. METHODS: Methanol extracts of COS leaves were used. Inhibitory effects on enzyme activities were measured using porcine pancreatic α-amylase and α-glucosidase from Saccharomyces cerevisiae in the presence of COS extract. Percentage inhibition of the enzymes and the IC(50) values were determined. In vitro protein glycation inhibitory effect of COS leaves on early and late glycation products were measured using bovine serum albumin or chicken egg lysozyme with fructose. Nitroblue tetrazolium was used to assess the relative concentration of fructosamine and polyacrylamide gel electrophoresis was used to assess the degree of glycation and protein cross-linking in the reaction mixtures. RESULTS: α-Glucosidase inhibitory activity was detected in COS leaves with a IC(50) of 67.5 μg/ml which was significantly lower than the IC(50) value of Acarbose (p < 0.01). Amylase inhibitory effects occurred at a comparatively higher concentration of extract with a IC(50) of 5.88 mg/ml which was significantly higher than the IC(50) value of Acarbose (p < 0.01). COS (250 μg/ml) demonstrated inhibitory effects on fructosamine formation and glycation induced protein cross-linking which were in par with 1 mg/ml aminoguanidine were detected. CONCLUSION: Methanol extracts of COS leaves demonstrated in vitro inhibitory activities on α-glucosidase, fructosamine formation, glycation and glycation induced protein cross-linking. These findings provide scientific evidence to support the use of COS leaves for hypoglycemic effects with an added advantage in slowing down protein glycation. |
format | Online Article Text |
id | pubmed-4700779 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-47007792016-01-06 α-glucosidase and glycation inhibitory effects of costus speciosus leaves Perera, Handunge Kumudu Irani Premadasa, Walgama Kankanamlage Vindhya Kalpani Poongunran, Jeyakumaran BMC Complement Altern Med Research Article BACKGROUND: Hyperglycaemia is a salient feature of poorly controlled diabetes mellitus. Rate of protein glycation is increased with hyperglycaemia leading to long term complications of diabetes. One approach of controlling blood glucose in diabetes targets at reducing the postprandial spikes of blood glucose. The objectives of this study were to assess the in vitro inhibitory effects of Costus speciosus (COS) leaves on α-amylase and α-glucosidase activities, fructosamine formation, protein glycation and glycation-induced protein cross-linking. METHODS: Methanol extracts of COS leaves were used. Inhibitory effects on enzyme activities were measured using porcine pancreatic α-amylase and α-glucosidase from Saccharomyces cerevisiae in the presence of COS extract. Percentage inhibition of the enzymes and the IC(50) values were determined. In vitro protein glycation inhibitory effect of COS leaves on early and late glycation products were measured using bovine serum albumin or chicken egg lysozyme with fructose. Nitroblue tetrazolium was used to assess the relative concentration of fructosamine and polyacrylamide gel electrophoresis was used to assess the degree of glycation and protein cross-linking in the reaction mixtures. RESULTS: α-Glucosidase inhibitory activity was detected in COS leaves with a IC(50) of 67.5 μg/ml which was significantly lower than the IC(50) value of Acarbose (p < 0.01). Amylase inhibitory effects occurred at a comparatively higher concentration of extract with a IC(50) of 5.88 mg/ml which was significantly higher than the IC(50) value of Acarbose (p < 0.01). COS (250 μg/ml) demonstrated inhibitory effects on fructosamine formation and glycation induced protein cross-linking which were in par with 1 mg/ml aminoguanidine were detected. CONCLUSION: Methanol extracts of COS leaves demonstrated in vitro inhibitory activities on α-glucosidase, fructosamine formation, glycation and glycation induced protein cross-linking. These findings provide scientific evidence to support the use of COS leaves for hypoglycemic effects with an added advantage in slowing down protein glycation. BioMed Central 2016-01-05 /pmc/articles/PMC4700779/ /pubmed/26727889 http://dx.doi.org/10.1186/s12906-015-0982-z Text en © Perera et al. 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Perera, Handunge Kumudu Irani Premadasa, Walgama Kankanamlage Vindhya Kalpani Poongunran, Jeyakumaran α-glucosidase and glycation inhibitory effects of costus speciosus leaves |
title | α-glucosidase and glycation inhibitory effects of costus speciosus leaves |
title_full | α-glucosidase and glycation inhibitory effects of costus speciosus leaves |
title_fullStr | α-glucosidase and glycation inhibitory effects of costus speciosus leaves |
title_full_unstemmed | α-glucosidase and glycation inhibitory effects of costus speciosus leaves |
title_short | α-glucosidase and glycation inhibitory effects of costus speciosus leaves |
title_sort | α-glucosidase and glycation inhibitory effects of costus speciosus leaves |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4700779/ https://www.ncbi.nlm.nih.gov/pubmed/26727889 http://dx.doi.org/10.1186/s12906-015-0982-z |
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