2011
DOI: 10.1074/jbc.m111.241281
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The G82S Polymorphism Promotes Glycosylation of the Receptor for Advanced Glycation End Products (RAGE) at Asparagine 81

Abstract: Interaction between the receptor for advanced glycation end products (RAGE) and its ligands amplifies the proinflammatory response. N-Linked glycosylation of RAGE plays an important role in the regulation of ligand binding. The receptor for advanced glycation end products (RAGE) 2 is a multiligand receptor that binds to carboxymethyl lysineand AGE-modified proteins and lipids but also to more autonomous ligands including high mobility group box 1 protein (HMGB1), members of the S100/Calgranulin protein family,… Show more

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Cited by 51 publications
(43 citation statements)
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“…However, our genebased SKAT-O meta-analysis did not reveal any exome-wide significant genes associated with COPD affection status. We were able to recover evidence for the previously described association of COPD with AGER, though this association was driven by a single coding variant (rs2070600) that has been reported to be functional (38,39). Our top gene-based COPD association was the pumilio domain-containing protein KIAA0020 (KIAA0020) (P = 1.2 3 10 24 ).…”
Section: Discussionmentioning
confidence: 50%
“…However, our genebased SKAT-O meta-analysis did not reveal any exome-wide significant genes associated with COPD affection status. We were able to recover evidence for the previously described association of COPD with AGER, though this association was driven by a single coding variant (rs2070600) that has been reported to be functional (38,39). Our top gene-based COPD association was the pumilio domain-containing protein KIAA0020 (KIAA0020) (P = 1.2 3 10 24 ).…”
Section: Discussionmentioning
confidence: 50%
“…Polymorphisms in the RAGE gene may alter AGE processing in tissues or reactions after the binding of AGEs to RAGE. Of specific interest is the RAGE G82S polymorphism; because of its location in the ligand-binding V domain of RAGE in which substitution of Gly (82) with Ser that promotes glycosylation of RAGE at asp81; it is associated with enhanced inflammatory responses, increased ligand binding, downstream signaling as well as RAGE expression (9).…”
mentioning
confidence: 99%
“…antibodies, specific asparagine residues can undergo 638 non-enzymatic deamidation [16,24]. The susceptibility to deami-639 dation markedly increases if a glycine residue is immediately after 640 the asparagine [29].…”
mentioning
confidence: 99%