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ISSN 2063-5346
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RECENT ADVANCES IN RECEPTOR FOR ADVANCED GLYCATION END PRODUCTS (RAGE) IN ORAL CARCINOGENESIS

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G L Gokul, Dr. Palati Sinduja, Dr. R. Priyadharshini
» doi: 10.31838/ecb/2023.12.s2.185

Abstract

The word ‘glycation’ refers to the non enzymatic reaction between the reducing sugar and a protein such as fructose or glucose that leads to the formation of a Receptor for Advanced Glycation End Products (RAGE). AGEs are a cohort of heterogeneous compounds that formed after the non enzymatic glycation of proteins, lipids and nucleic acids. The Receptor for Advanced Glycation End Products (RAGE) is a member of immunoglobulin. It is encoded in the Class iii region of the major histocompatibility complex. The enzyme RAGE which is expressed in the lung that readily measures levels easily at sites of inflammation, on inflammatory and epithelial cells. AGEs have a potent impact in tissues, stimulating processes that are linked to inflammation and its consequences. AGEs cause perturbation during a diverse group of diseases, like diabetes, inflammation, neurodegeneration, and aging. Thus, targeting the pathway may indicate a logical step within the prevention/treatment of these disorders. Ligation of RAGE on the cellular surface triggers a series of cellular signaling events, including the activation and translocation to the nucleus of transcription factor NF-kappaB, and results in the assembly of chemokines, pro-inflammatory cytokines, adhesion molecules and oxidative stress and causing inflammation. newer work has revealed the role of RAGE in inflammatory cell recruitment and extravasation of leukocytes across the endothelial barrier with further inflammatory events. RAGE is a crucial target to treat RAGE activation-associated diseases. The enzyme ‘RAGE’ is expressed by different cell types, which incorporates macrophages, neuronal, endothelial, lymphocytes and smooth muscle cells. In Advanced glycation end products (AGEs), RAGE binds with some of the enzymes like amyloid, amphoterin, S100/calgranulin, transthyretin, and a leukocyte integrin, Mac-1. Engagement of RAGE in intracellular signaling results in the activation of the proinflammatory transcription factor NF-kappaB to sustained cellular dysfunction and tissue destruction.

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