advanced glycation end products

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advanced glycation end products



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.
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References in periodicals archive ?
Identification of polymorphisms in the receptor for advanced glycation end products (RAGE) gene: prevalence in type 2 diabetes and ethnic groups.
Age-related changes in cells and tissues due to advanced glycation end products (AGEs).
Advanced glycation end products in the pathogenesis of chronic kidney disease.
(4) Moreover, compared with cooked foods, raw foods contain substantially lower amounts of advanced glycation end products and other potential inflammatory mediators.
Soluble receptor for advanced glycation end products (sRAGE) and endogenous secretory RAGE (esRAGE) in amniotic fluid: Modulation by infection and inflammation.
The association between the -374T/A polymorphism of the receptor for advanced glycation end products gene and blood pressure and arterial stiffness is modified by glucose metabolism status: the Hoorn and CODAM studies.
(5.) 'Advanced Glycation End Products (AGEs): Emerging Mediators of Skin Aging," in Textbook of Aging Skin (Berlin: Springer, 2017, pp.
In an analysis of patients from the VADT-F, he and his associates found that specific advanced glycation end products and oxidation products are associated with the severity of subclinical atherosclerosis over the long term and may play an important role in the "negative metabolic memory" of macrovascular complications in people with long-standing type 2 diabetes mellitus (Diabetes Care.
Advanced glycation end products (AGEs) are a group of heterogeneous compounds formed by endogenous nonenzymatic glycation and oxidation (glycoxidation) of proteins, lipids, and nucleic acids [1-4].
El Bawab, "Bimodal effect of advanced glycation end products on mesangial cell proliferation is mediated by neutral ceramidase regulation and endogenous sphingolipids," The Journal of Biological Chemistry, vol.
Advanced glycation end products (AGEs), a heterogeneous group of toxic molecules formed from proteins and sugar residues by irreversible nonenzymatic reactions in a hyperglycemic milieu, are also important pathogenic factors which stimulate inflammation and enhance atherogenesis in diabetes [4].
Chronic hyperglycemia plays a vital role in the development of long-term diabetic complications by inducing protein glycation and the gradual formation of advanced glycation end products (AGEs) in various body tissues [2, 5, 10].

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