Inhibition of advanced glycation endproduct formation by foodstuffs (original) (raw)
* Corresponding authors
a Department of Food Science and Biotechnology, National Chung-Hsing University, 250 Kuokuang Road, Taichung, Taiwan
E-mail: gcyen@nchu.edu.tw
Fax: +886 4-2285-4378
Tel: +886 4-2287-9755
Abstract
The Maillard reaction, which is generally termed nonenzymatic browning or glycation, has been implicated in accelerated aging and diabetic complications in vivo. Although the molecular basis of glycation-induced pathogenesis is not well understood, the following have been noted: (1) protein glycation leads to the formation and accumulation of toxic advanced glycation endproducts (AGEs); (2) AGEs can permanently alter the structure and function of body proteins; and (3) the interaction between AGE-modified proteins and AGE-specific receptors (RAGEs) on the cell surface induces the overproduction of reactive oxygen species (ROSs) and inflammatory mediators, which leads to cellular disorders in biological systems. To date, studies that have examined the contribution of protein glycation to disease-states have primarily focused on the deleterious effects and related mechanisms of these glycotoxins. However, it remains unknown whether phytochemicals exert protective effects against glycotoxin-induced damage. Thus, the development and investigation of AGE inhibitors, especially the natural anti-AGE agents without adverse effects, may provide a therapeutic approach for delaying and preventing premature aging and diabetic complications. In this review, we provide an outline of anti-glycation properties of foodstuffs and/or their active components, and discuss their mechanisms of action.
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Article information
DOI
https://doi.org/10.1039/C1FO10026B
Article type
Review Article
Submitted
16 Feb 2011
Accepted
19 Mar 2011
First published
08 Apr 2011
Download Citation
Food Funct., 2011,2, 224-234
Permissions
Inhibition of advanced glycation endproduct formation by foodstuffs
C. Wu, S. Huang, J. Lin and G. Yen,Food Funct., 2011, 2, 224DOI: 10.1039/C1FO10026B
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