Advanced glycation end products AGE

Jang DS, Kim JM, Lee YM, Kim YS, Kim JH, Kim JS. (2006) Puerariafuran, a new inhibitor of advanced glycation end products (AGEs) isolated from the roots of Pueraria lobata. Chem Pharm Bull 54 1315-1317. 

Cantero, A. V., Portero-Otin, M., Ayala, V., Auge, N., Sanson, M., Elbaz, M., Thiers, J. C., Pamplona, R., Salvayre, R., and Negre-Salvayre, A. (2007). Methylglyoxal induces advanced glycation end product (ages) formation and dysfunction of PDGF receptor-beta Implications for diabetic atherosclerosis. FASEB J. 21,3096-3106. 

Yamagishi, S., Nakamura, K., Inoue, H., Kikushi, S., and Takeuchi, M. (2005). Serum and cerebrospinal fluid levels of glyceraldehyde-derived advanced glycation end products (ages) may be a promising biomarker for early detection of Alzheimer s disease. Med. Hypotheses 64,1205-1207. 

Glycation reactions. Glucose or other sugars may react non-enzymatically with proteins to form glycation products. Early glycation products such as fructosamine-protein adducts may later be transformed to the more complex advanced glycation end products (AGE products). 

A. A. Booth, R. G. Khalifa, P. Todd, and B. G. Hudson, In vitro kinetic studies of formation of antigenic advanced glycation end products (AGEs). Novel inhibition of post-Amadori glycation pathways, J. Biol. Chem., 1997, 272, 5430-5437. 

F19. Fu, S., Fu, M. X., Baynes, J. W., Thorpe, S. R., and Dean, R. T., Presence of dopa and amino acid hydroperoxides in proteins modified with advanced glycation end products (AGEs) Amino acid oxidation products as a possible source of oxidative stress induced by AGE proteins. Biochem. J. 330, 233-239 (1998). 

M10. Masaki, H., Okano, Y., and Sakurai, H., Generation of active oxygen species from advanced glycation end-products (AGEs) during ultraviolet light A (UVA) irradiation and a possible mechanism for cell damaging. Biochim. Biophys. Acta 1428,45-56 (1999). 

Figure 1.11 Illustration of advanced glycation end-product (AGE) formation.

Proteins with relatively short half-lives are glycated by rather acute increases in blood glucose, whereas chronic, small elevations of blood glucose lead to irreversible chemical modifications of long-lived proteins. These have been called advanced-glycation end-products (AGEs) (Fig. 8.2). 

The assays most widely employed are the measurement of thiobarbituric acid-reactive species (TBARS) and the formation of conjugated dienes, markers of lipid peroxidation [31-33] the determination of advanced oxidation protein products (AOPP), a marker of protein oxidation, and of advanced glycation end-products (AGE) [34-37] the measurement of erythrocyte antioxidant potential [38]. Of particular importance is the isoprostanes determination, since these compounds are formed by the free radical catalysed peroxidation of arachidonic acid, which is independent of the cyclooxygenase enzyme, giving rise to stable compounds, measurable in urine [39]. As recently assessed in a Workshop on markers of oxidative damage and antioxidant protection [40], currently available methods for the determination of antioxidant and redox status are not yet generally suitable for routine clinical applications, essentially for the lack of standardized tests. 

J. Greten, I. Kreis, K. Wiesel K, E. Stier, A. M. Schmidt, D. M. Stem, E. Ritz, R. Waldherr and P. P. Nawroth, Receptors For Advanced Glycation End-Products(AGE)-Expression by Endothelial Cells in Non-Diabetic Uraemic Patients, Nephrology Dialysis Transplantation 11 (1996) 786-790. 

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