RAGE (receptor)

RAGE (receptor)

Identifiers Symbols AGER; RAGE External IDs OMIM: 600214 MGI: 893592 HomoloGene: 883 GeneCards: AGER Gene

Gene Ontology
Molecular function	• receptor activity • transmembrane signaling receptor activity • protein binding • S100 protein binding
Cellular component	• extracellular region • plasma membrane • integral to plasma membrane
Biological process	• inflammatory response • cell surface receptor signaling pathway • response to wounding • neuron projection development • innate immune response • induction of positive chemotaxis • positive regulation of NF-kappaB transcription factor activity
Sources: Amigo / QuickGO

RNA expression pattern More reference expression data Orthologs Species Human Mouse Entrez 177 11596 Ensembl ENSG00000204305 ENSMUSG00000015452 UniProt Q15109 C5H3H4 RefSeq (mRNA) NM_001136 NM_001271422 RefSeq (protein) NP_001127 NP_001258351 Location (UCSC) Chr 6:
32.15 – 32.15 Mb Chr 17:
34.6 – 34.6 Mb PubMed search

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. It is also called "AGER". Its name comes from its ability to bind advanced glycation endproducts (AGE), which include chiefly glycoproteins the glycans of which have been modified non-enzymatically through the Maillard reaction. In view of its inflammatory function in innate immunity and its ability to detect a class of ligands through a common motif, RAGE is often referred to as a pattern recognition receptor. RAGE also has at least one other agonistic ligand: high mobility group protein B1 (HMGB1). HMGB1 is an intracellular DNA-binding protein important in chromatin remodeling which can be released by necrotic cells passively and by active secretion from macrophages, natural killer (NK) cells and dendritic cells.

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.

Isoforms of the RAGE protein, which lack the transmembrane and the signaling domain (commonly referred to as soluble RAGE or sRAGE) are hypothesized to counteract the detrimental action of the full-length receptor and are hoped to provide a means to develop a cure against RAGE-associated diseases.