advanced glycation end products


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advanced glycation end products

,

AGE

Proteins that have been nonenzymatically modified by the addition of sugar residues to lysine. These altered proteins increase with aging and in patients with hyperglycemia and diabetes mellitus.
References in periodicals archive ?
Role of advanced glycation end product (AGE)-induced receptor (RAGE) expression in diabetic vascular complications.
Sunlight, smoking, air pollution, and advanced glycation end products (AGEs) generate an overload of free radicals that overwhelm the skin's network of protective antioxidants.
Keywords: Advanced glycation end products, glycotoxin, infant formulas
Objective: In the present study, OSSC extracts and major compounds were examined for their effects on binding to the receptors of advanced glycation end products (RAGE) and on transforming growth factor-beta1 (TGF-[beta]1) expression-related signal mechanisms in mouse glomerular mesangial cells (GMCs).
Due to complex metabolic disorder in metabolic syndrome, reactive derivatives are formed via nonenzymatic reaction named Maillard reaction between the free amino groups in lysine and arginine residues in proteins and carbohydrates that undergo a series of complex reactions to an irreversible complex group of compound termed advanced glycation end products (AGEs) [2, 3].
The receptor for advanced glycation end products (RAGE), first identified as a member of the immunoglobulin superfamily, is a pattern-recognition receptor that interacts with multiligands, such as advanced glycation end products (AGEs), high mobility group box 1 (HMGB1), S-100 calcium-binding protein (S100B), and Mac-1 [7].
Data Sources: We retrieved information from the PubMed database up to January, 2014, using various search terms and their combinations including DNA damage, diabetes, cancer, high glucose, hyperglycemia, free fatty acids, palmitic acid, advanced glycation end products, mutation and carcinogenesis.
Published in Chemical Research in Toxicology, the scientific paper, "Bioactive Ginger Constituents Alleviate Protein Glycation by Trapping Methylglyoxal," investigated the ability of gingerols and shogaols to prevent the formation of advanced glycation end products (AGEs) via trapping methylglyoxal (MGO).
It has been reported that advanced glycation end products (A GE'S) are elevated in type 2 DM patients with coronary and carotid angiopathy.
Advanced glycation end products (AGE) are nonenzymatic additions of glucose or other saccharides to proteins, lipids and nucleotides (1,2).
Modern diets largely contain heat-processed products, and as a result also contain high levels of advanced glycation end products (AGEs).
Processed, fried, and sugary foods in the diet contribute to accelerated aging from glycation, the linking of sugars (glucose and fructose) to amino acids (the building blocks of protein) to form advanced glycation end products (AGEs,) according to the AGE Foundation.

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