Advanced Glycosylation End Product Specific Receptor (AGER)

RAGE; Receptor For Advanced Glycation Endproducts

SPN	W166
HGNC	320
MGI	893592
PubMed	21521347
RGD	69258
UniProt	Q15109
Wiki	RAGE

RAGE, the receptor for advanced glycation endproducts is a 35kD transmembrane receptor of the immunoglobulin super family which was first characterized in 1992 by Neeper et al.. Its name comes from its ability to bind advanced glycation endproducts (AGE), a heterogeneous group of non-enzymatically altered proteins. Besides AGEs, RAGE is also able to bind other ligands and is thus often referred to as a pattern recognition receptor.The interaction between RAGE and its ligands is thought to result in pro-inflammatory gene activation. Due to an enhanced level of RAGE ligands in diabetes or other chronic disorders, this receptor is hypothesised to have a causative effect in a range of inflammatory diseases such as diabetic complications, Alzheimer's disease and even some tumors.

Reference

"Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins."
J. Biol. Chem. 267:14998-15004(1992) [PubMed] [Europe PMC] [Abstract]

"Three genes in the human MHC class III region near the junction with the class II: gene for receptor of advanced glycosylation end products, PBX2 homeobox gene and a notch homolog, human counterpart of mouse mammary tumor gene int-3."
Genomics 23:408-419(1994) [PubMed] [Europe PMC] [Abstract]

"Novel splice variants of the receptor for advanced glycation end-products expressed in human vascular endothelial cells and pericytes, and their putative roles in diabetes-induced vascular injury."
Biochem. J. 370:1097-1109(2003) [PubMed] [Europe PMC] [Abstract]

"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]

"Identification, classification, and expression of RAGE gene splice variants."
FASEB J. 22:1572-1580(2008) [PubMed] [Europe PMC] [Abstract]

"Alternative splicing of the RAGE cytoplasmic domain regulates cell signaling and function."
PLoS ONE 8:E78267-E78267(2013) [PubMed] [Europe PMC] [Abstract]

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and analysis of human chromosome 6."
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Effects of novel polymorphisms in the RAGE gene on transcriptional regulation and their association with diabetic retinopathy."
Diabetes 50:1505-1511(2001) [PubMed] [Europe PMC] [Abstract]

"Both Ca2+ and Zn2+ are essential for S100A12 protein oligomerization and function."
BMC Biochem. 10:11-11(2009) [PubMed] [Europe PMC] [Abstract]

"RAGE-dependent signaling in microglia contributes to neuroinflammation, Abeta accumulation, and impaired learning/memory in a mouse model of Alzheimer's disease."
FASEB J. 24:1043-1055(2010) [PubMed] [Europe PMC] [Abstract]

"S100A14 stimulates cell proliferation and induces cell apoptosis at different concentrations via receptor for advanced glycation end products (RAGE)."
PLoS ONE 6:E19375-E19375(2011) [PubMed] [Europe PMC] [Abstract]

"Disulfide bonds within the C2 domain of RAGE play key roles in its dimerization and biogenesis."
PLoS ONE 7:E50736-E50736(2012) [PubMed] [Europe PMC] [Abstract]

"Solution structure of the third Ig-like domain from human advanced glycosylation end product-specific receptor."
Submitted (APR-2008) to the PDB data bank

"The 1.5 A crystal structure of human receptor for advanced glycation endproducts (RAGE) ectodomains reveals unique features determining ligand binding."
J. Biol. Chem. 285:40762-40770(2010) [PubMed] [Europe PMC] [Abstract]

"Structural basis for ligand recognition and activation of RAGE."
Structure 18:1342-1352(2010) [PubMed] [Europe PMC] [Abstract]

"Advanced glycation end product recognition by the receptor for AGEs."
Structure 19:722-732(2011) [PubMed] [Europe PMC] [Abstract]