Rapid formation of -(carboxymethyl)lysine (CML) from ribose depends on glyoxal production by oxidation.

-(Carboxymethyl)lysine (CML) is a major advanced glycation end-product (AGE) involved in protein dysfunction and inflammation . Its accumulation increases with age and is enhanced with the pathogenesis of diabetic complications. Therefore, the pathways involved in CML formation should be elucidated to understand the pathological conditions involved in CML.

Mitochondrial stress and glycoxidation increase with decreased kidney function.

Mitochondrial stress increases the production of fumarate, an intermediate of the Krebs cycle. Fumarate non-enzymatically reacts with the thiol group of cysteine, leading to the production of -(2-succinyl)cysteine. Here, we quantified the concentration of fumarate, the free form of -(2-succinyl)cysteine, and advanced glycation end-products, including -(carboxymethyl)lysine and -(5-hydro-5-methyl-4-imidazolone-2-yl)-ornithine, in the serum of chronic kidney disease patients, using liquid chromatography-tandem mass spectrometry and an enzymatic assay.

Changes in S-(2-succinyl)cysteine and advanced glycation end-products levels in mouse tissues associated with aging.

Cysteine is non-enzymatically modified by fumarate, which is an intermediate of the tricarboxylic acid cycle, leading to the formation of S-(2-succinyl)cysteine (2SC). Post-translational modification of physiological proteins by fumarate causes enzyme dysfunction. The aim of the study was to evaluate the changes in 2SC accumulation in physiological tissues associated with aging.

Roxb. and lutein ameliorate cataract in type 1 diabetic rats.

Roxb. is an annual aquatic grass of the citrus family. Although its hot water extract displays antioxidative activity , little is known about its biological effectiveness.

Glucoselysine is derived from fructose and accumulates in the eye lens of diabetic rats.

Prolonged hyperglycemia generates advanced glycation end-products (AGEs), which are believed to be involved in the pathogenesis of diabetic complications. In the present study, we developed a polyclonal antibody against fructose-modified proteins (Fru-P antibody) and identified its epitope as glucoselysine (GL) by NMR and LC-electrospray ionization (ESI)- quadrupole TOF (QTOF) analyses and evaluated its potential role in diabetes sequelae. Although the molecular weight of GL was identical to that of fructoselysine (FL), GL was distinguishable from FL because GL was resistant to acid hydrolysis, which converted all of the FLs to furosine.