IMR Press / FBE / Volume 12 / Issue 1 / DOI: 10.2741/E864

Frontiers in Bioscience-Elite (FBE) is published by IMR Press from Volume 13 Issue 2 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
G82S RAGE polymorphism is associated with Alzheimer’s disease
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1 Department of Biotechnology, PSG College of Technology, Peelamedu, Coimbatore, Tamil Nadu, 641004, India
Send correspondence to: Palaniswamy Rani, Department of Biotechnology, PSG College of Technology, Peelamedu, Coimbatore, Tamil Nadu, India, Tel: 91 9443161653, Fax:0422-2573833, E-mail: rani.bio@psgtech.ac.in
rani.bio@psgtech.ac.in (Palaniswamy Rani)
Front. Biosci. (Elite Ed) 2020, 12(1), 150–161; https://doi.org/10.2741/E864
Published: 1 March 2020
Abstract

Receptor for advanced glycation end products (RAGE) has been implicated in the pathophysiology of Alzheimer’s disease (AD) due to its ability to interact with amyloid beta and to elicit an inflammatory response. sRAGE, one of the splice variants of RAGE, has been reported to be a decoy receptor for amyloid beta peptides. The present study addresses the occurrence of G82S RAGE polymorphism in AD, and its association with the expression of sRAGE and amyloid beta load (Aβ peptide). The results indicated that the heterozygous genotype (GS) was distributed more than the wild genotype (GG) in patients with AD. Moreover, in patients with AD, there was decreased expression of sRAGE and increased expression of tRAGE and TNF-α. The data show that G82S RAGE polymorphism is highly associated with the development of AD, with decreased expression of sRAGE and increased expression of tRAGE and TNF-α.

Keywords
Amyloid toxicity
oxidative stress
RAGE
sRAGE
polymorphism
AD
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