The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Inhibition of advanced glycation endproduct formation by foodstuffs
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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Cites
Molecular aspects of lipoic acid in the prevention of diabetes complications
Packer, L., Kraemer, K., & Rimbach, G. (2001) · Nutrition · doi:10.1016/s0899-9007(01)00658-x · Cited by 556
Ceriello, A., Giugliano, D., Quatraro, A., Donzella, C., Dipalo, G., & Lefebvre, P. J. (1991) · Diabetes Care · doi:10.2337/diacare.14.1.68 · Cited by 271
Qin, B., Panickar, K. S., & Anderson, R. A. (2010) · Journal of Diabetes Science and Technology · doi:10.1177/193229681000400324 · Cited by 220
Inhibition of Protein Glycation by Extracts of Culinary Herbs and Spices
Dearlove, R. P., Greenspan, P., Hartle, D. K., Swanson, R. B., & Hargrove, J. L. (2008) · Journal of Medicinal Food · doi:10.1089/jmf.2007.536 · Cited by 157
Rutter, Sell, Fraser, Obrenovich, Zito, Starke-Reed, & Monnier (2003) · International Journal for Vitamin and Nutrition Research · doi:10.1024/0300-9831.73.6.453 · Cited by 76
Arguing for the motion: yes, RAGE is a receptor for advanced glycation endproducts
Ramasamy, R., Yan, S. F., & Schmidt, A. M. (2007) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700008 · Cited by 58
Cited by
Control of Maillard Reactions in Foods: Strategies and Chemical Mechanisms
Lund, M. N., & Ray, C. A. (2017) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b00882 · Cited by 871
Advanced glycation endproducts in food and their effects on health
Poulsen, M. W., Hedegaard, R. V., Andersen, J. M., de Courten, B., Bügel, S., Nielsen, J., Skibsted, L. H., & Dragsted, L. O. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.06.052 · Cited by 751
Quercetin Inhibits Advanced Glycation End Product Formation by Trapping Methylglyoxal and Glyoxal
Li, X., Zheng, T., Sang, S., & Lv, L. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf504132x · Cited by 288
Nooshkam, M., Varidi, M., & Verma, D. K. (2020) · Food Research International · doi:10.1016/j.foodres.2020.109003 · Cited by 282
The Role of Advanced Glycation End Products in Diabetic Vascular Complications
Rhee, S. Y., & Kim, Y. S. (2018) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2017.0105 · Cited by 274
Metadata
- Authors
- Wu, C.-H., Huang, S.-M., Lin, J.-A., & Yen, G.-C.
- Venue
- Food & Function
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2011
- Volume
- 2
- Issue
- 5
- Pages
- 224
- ISSN
- 2042-6496 (ISSN-L)
- 2042-650X
- OpenAlex
- W2138689678
- Cited by
- 328
- References
- 6
- FWCI
- 10.38
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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