glycation


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Related to glycation: advanced glycation end products

gly·ca·tion

(glī-kā'shŭn),
The nonenzymic reaction that forms a glycate.

glycation

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

glycation

Biochemistry The binding of glucose of proteins, in particular to HbA1c
References in periodicals archive ?
Tanaka et al., "Skin autofluorescence, a marker for advanced glycation end product accumulation, is associated with arterial stiffness in patients with end-stage renal disease," Metabolism, vol.
Therefore, the ribose glycation of collagen can serve as a value tool to study, (i) altered tissue mechanical properties due to glycation, (ii) cell behaviour in response to glycation, (iii) as in-vitro model to study extra cellular matrix changes in age-related bone pathologies.
Interpretation of Hb [A.sub.1c] values is based on the assumption that erythrocytes are freely permeable to glucose and that neither glucose entry, the rate of glycation, nor erythrocyte life span differs significantly among individuals.
Glycation, thiol group oxidation, and aggregation of BSA were then measured using thiobarbituric acid, 2, 4-dinitrophenylhydrazine, and Congo red colorimetric methods, respectively.
Dietary-Advanced Glycation End Products (d-AGEs) and Cognitive Decline
Chuang, "Advanced glycation end product--induced proliferation in NRK-49F cells is dependent on the JAK2/STAT5 pathway and cyclin D1," American Journal of Kidney Diseases, vol.
Hudson, "Amadorins: novel post-Amadori inhibitors of advanced glycation reactions," Biochemical and Biophysical Research Communications, vol.
Keywords: Advanced glycation end products, glycotoxin, infant formulas
(1) An often overlooked factor in skin aging is the cross-linking of collagen caused by glycation. (7)
Hyperglycaemia is a key factor in the pathogenesis of diabetic complications by increasing protein glycation and gradual buildup of advanced glycated end products (AGEs) in body tissues.2 There are receptors for AGEs (RAGEs) found on different cells.
This dimension of A1c-glucose axis becomes even more significant as the people from Asians and specifically from sub-continental region have been suggested to have a more diabetogenic phenotype and varying hemoglobin glycation rates in comparison to their Caucasian counterparts from where most data has evolved7,8.
Advanced glycation end products (AGEs) are formed by non-enzymatic glycation of proteins or lipids by high serum glucose, methylglyoxal, and 3-deoxy glucosone.