glycation


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Related to glycation: advanced glycation end products

gly·ca·tion

 (glī-kā′shən)
n.
The nonenzymatic covalent bonding of a sugar molecule to another molecule, especially a protein.

glycation

(ɡlaɪˈkeɪʃən)
n
1. the bonding of a sugar molecule to a protein or lipid
2. a compound produced by such bonding
References in periodicals archive ?
de Vries et al., "Accumulation of advanced glycation endproducts in patients with systemic lupus erythematosus," Rheumatology, vol.
To this aim, the crosslinking mechanism in terms of preribose glycation (before freeze drying) and post-ribose glycation (after freeze drying) was investigated.
Glycation is the process by which a monosaccharide, most commonly glucose, attaches nonenzymatically to a protein.
Wrinkles happen because of a process called glycation. This occurs when sugar (glucose) molecules bind to a protein molecule without the help of enzymes.
Background: Glucose-induced protein glycation has been implicated in the progression of diabetic complications and age-related diseases.
This 23-chapter book explores mechanisms linking aging, disease, and biological age estimation, focusing on four of the hallmarks of aging--aspartic acid racemization, advanced glycation endproducts, telomere shortening, and mitochondrial DNA mutations--and their role in aging and diseases and their application in age-at-death estimation in forensic sciences.
Freedom Meditech has developed an FDA-cleared, noninvasive eye scan that utilises lens autoflourescence to detect the presence of advanced glycation products or AGEs in the lens of the eye that has the potential to screen for chronic diseases like diabetes.
This contributes not only to the loss of healthy nutrients, but also to the formation of toxins--including advanced glycation end products (AGEs) [6].
The advanced glycation end product receptor (AGER) has different functions in the toxicity and disposal (detoxification) of advanced glycation end products (AGEs) [9].
Pyridoxamine solves its action by inhibiting the formation of advanced glycation end products (AGEs) from glycated proteins and by trapping pathogenic reactive carbonyl compounds (Amadori product), the intermediates in the formation of AGEs [7].
Researchers focused on substances called advanced glycation end products (AGEs), which are linked with insulin resistance, a risk factor for type 2 diabetes.
Advanced glycation end products constitute a complex group of compounds derived from the nonenzymatic glycation of proteins, lipids, and nucleic acids formed endogenously, but also from exogenous supplies such as tobacco smoking (glycotoxins).