Volume 28, Issue 5 (Monthly_Aug 2017)
Studies in Medical Sciences 2017, 28(5): 363-372 |
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Meamar Z, Masoudiyan N, Bahmani F. EVALUATION OF THE EFFECTS OF ASCORBIC ACID ON GLYCATION REACTION OF ALBUMIN ON IN VITRO CONDITION. Studies in Medical Sciences 2017; 28 (5) :363-372
URL: http://umj.umsu.ac.ir/article-1-3944-en.html
URL: http://umj.umsu.ac.ir/article-1-3944-en.html
Kashan University of Medical Sciences , bahmani@Kaums.ac.ir
Abstract: (4918 Views)
Background & Aims: Advanced glycation end products (AGEs) formation is increased in diabetes mellitus, leading to microvascular and macrovascular complications. Recently, much attention has been focused on natural and synthetic inhibitors to delay the onset or progression of diabetes and its comorbidities. In this study, an in vitro glycation model containing albumin as a model protein together with glucose as glycating agent was used to study antiglycation activity of AA.
Materials & Methods: Bovine serum albumin was incubated with 0.5 M of glucose with or without AA in 37°C for 4 weeks. The formation of fluorescent AGEs was determined to indicate protein glycation, whereas the level of protein carbonyl content and thiol group were examined for protein oxidation. Glycation is known to induce aggregation and fibrillation of proteins. To determine the inhibitory effect of AA on aggregation and fibrillation of albumin, amyloid specific dyes such as Thioflavin T was used.
Results: The results found that AA significantly inhibited the formation of fluorescent AGEs (P < 0.05) and significantly prevented protein oxidation manifested by reducing protein carbonyl and the depletion of protein thiol groups (P < 0.05). Moreover, our results indicated the inhibitory potential of AA toward amyloid like aggregation of albumin and protective effect of AA on albumin native conformation.
Conclusion: Thus, these findings indicated that AA has high potential for decreasing protein glycation and oxidation that may delay or prevent AGEs-related diabetic complications.
Materials & Methods: Bovine serum albumin was incubated with 0.5 M of glucose with or without AA in 37°C for 4 weeks. The formation of fluorescent AGEs was determined to indicate protein glycation, whereas the level of protein carbonyl content and thiol group were examined for protein oxidation. Glycation is known to induce aggregation and fibrillation of proteins. To determine the inhibitory effect of AA on aggregation and fibrillation of albumin, amyloid specific dyes such as Thioflavin T was used.
Results: The results found that AA significantly inhibited the formation of fluorescent AGEs (P < 0.05) and significantly prevented protein oxidation manifested by reducing protein carbonyl and the depletion of protein thiol groups (P < 0.05). Moreover, our results indicated the inhibitory potential of AA toward amyloid like aggregation of albumin and protective effect of AA on albumin native conformation.
Conclusion: Thus, these findings indicated that AA has high potential for decreasing protein glycation and oxidation that may delay or prevent AGEs-related diabetic complications.
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