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Advanced Glycation End Products—A Special Hazard in Diabetes
Published in Robert Fried, Richard M. Carlton, Type 2 Diabetes, 2018
Robert Fried, Richard M. Carlton
The journal Clinical Chemistry and Laboratory Medicine published a study titled “Glucosepane: a poorly understood advanced glycation end product of growing importance for diabetes and its complications.” The investigators report that AGE formation in diabetes makes them “potential culprits of diabetic complications,” and in particular, retinopathy, nephropathy, and neuropathy.
Advanced Glycation Endproducts for Age-at-Death Estimation
Published in Sara C. Zapico, Mechanisms Linking Aging, Diseases and Biological Age Estimation, 2017
Luis L. Cabo, Christian Thomas, Sara C. Zapico
The Maillard reaction is a complex series of reactions between reducing sugars and amino groups of proteins, which lead to browning, fluorescence and cross-linking of protein (Baynes 2001). AGEs products, formed during the later stages of the Maillard reaction, accumulate in long-lived tissue proteins and may contribute to the development of complications in aging (Thorpe and Baynes 1996). Human aging is associated with a stiffening of tissues that are rich in extracellular matrix and long-lived proteins, such as skeletal muscle, tendons, joints, bone, heart, arteries, lung, skin and lens (Monnier et al. 2005). GO, MGO, and deoxyglucosones belong to a series of dicarbonyl compounds, identified as intermediates in the Maillard reaction. GO and MGO react with lysine and arginine residues in protein yielding compounds such as the N-(carboxy-alkyl)lysines, CML and CEL, and imidazolones and dehydroimidazolones (Ahmed et al. 1997, Ahmed et al. 1986, Henle et al. 1994, Lo et al. 1994). Glucosepane appears to be the most important cross-linking AGE in human tissues, as well as MGO and pentoside. Cross-linking of collagen and other proteins by AGEs affects the mechanical properties of tissues, especially of the vasculature (Monnier et al. 2005).
Identification and characterization of protein cross-links induced by oxidative reactions
Published in Expert Review of Proteomics, 2018
Per Hägglund, Michele Mariotti, Michael J. Davies
A wide variety of cross-links are also generated by reactive aldehydes, or via reactions of glucose, other reducing sugars or cellular metabolites of these. These cross-links are formed via initial adduction of a carbonyl or reducing sugar to a protein side-chain, and in cases where there is a second reactive site, further reaction with another amino acid to give a cross-linked species (e.g. glyoxal-linked dimers, GOLD, and methylglyoxal-linked dimers, MOLD, glucosepane) [13,14]. These reactions are commonly used (e.g. with glutaraldehyde [15]) to “fix” proteins or biological specimens, or adhere specific proteins to targets (e.g. surfaces).