Effect of (-)-epigallocatechin-3-gallate on glucose-induced human serum albumin glycation

(-)-Epigallocatechin-3-gallate (EGCg) is a naturally occurring polyphenol found in plant-based foods and beverages such as green tea. Although EGCg can eliminate carbonyl species produced by glucose autoxidation and thus can inhibit protein glycation, it is also reported to be a pro-oxidant that sti...

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Bibliographic Details
Published in:Free radical research 2015-01, Vol.49 (8), p.946-953
Main Authors: Li, M., Hagerman, A. E.
Format: Article
Language:English
Subjects:
AGEs
Antioxidants - chemistry
Antioxidants - pharmacology
carbonyl
Catechin - analogs & derivatives
Catechin - chemistry
Catechin - pharmacology
diabetes
fluorescence
Glucose - pharmacology
Glucose - physiology
Glycosylation
Humans
polyphenol
Serum Albumin - drug effects
Serum Albumin - metabolism
tea
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Summary:(-)-Epigallocatechin-3-gallate (EGCg) is a naturally occurring polyphenol found in plant-based foods and beverages such as green tea. Although EGCg can eliminate carbonyl species produced by glucose autoxidation and thus can inhibit protein glycation, it is also reported to be a pro-oxidant that stimulates protein glycation in vitro. To better understand the balance between antioxidant and pro-oxidant features of EGCg, we evaluated EGCg-mediated bioactivities in a human serum albumin (HSA)/glucose model by varying three different parameters (glucose level, EGCg concentration, and time of exposure to EGCg). Measurements of glycation-induced fluorescence, protein carbonyls, and electrophoretic mobility showed that the level of HSA glycation was positively related to the glucose level over the range 10-100 mM during a 21-day incubation at 37°C and pH: 7.4. Under mild glycemic pressure (10 mM), long exposure to EGCg enhanced HSA glycation, while brief exposure to low concentrations of EGCg did not. Under high glycemic pressure (100 mM glucose), long exposure to EGCg inhibited glycation. For the first time we showed that brief exposure to EGCg reversed glycation-induced fluorescence, indicating a restorative effect. In conclusion, our research identified glucose level, EGCg concentration, and time of exposure as critical factors dictating EGCg bioactivities in HSA glycation. EGCg did not affect HSA glycation under normal physiological conditions but had a potential therapeutic effect on HSA severely damaged by glycation.
ISSN:1071-5762
1029-2470
DOI:10.3109/10715762.2015.1016429