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AGER (advanced glycosylation end product-specific receptor)

Identity

Other namesMGC22357
RAGE
HGNC (Hugo) AGER
LocusID (NCBI) 177
Location 6p21.32
Location_base_pair Starts at 32148745 and ends at 32152099 bp from pter ( according to hg19-Feb_2009)  [Mapping]
 
  Figure 1. Schematic of human chromosome 6.

DNA/RNA

Note [Annexed document]
  Table 1. Alternative splice variants human RAGE (From Hudson B et al. FASEB J. 2008;22:1572-80).
Description The human AGER (RAGE) gene lies within the major histocompatibility complex class III region on chromosome 6, which contains genes involved in immune responses, such as TNFalpha, lymphotoxin, complement components and homeobox gene HOX12. It comprises 11 exons and 10 introns, and a 5' flanking region that regulates its transcription. The resulting transcribed mRNA of ~1.4 kb with a short 3'UTR is alternatively spliced, and nearly twenty isoforms have been identified in different tissues such as lung, liver, kidney, smooth muscle, endothelial cells and brain. The different RAGE gene splice variants have been named RAGE, RAGE_v1 to RAGE_v19 according to the Human Gene Nomenclature Committee. RAGE is composed of a number of distinct protein domains; an extracellular region (aa 1-342) composed of a signal peptide (aa 1-22), followed by three immunoglobulin-like domains, a V-type domain, (aa 23-116) and two C type domains (C1: aa 124-221 and C2: 227-317), a single transmembrane domain (aa 343-363), and a short cytoplasmic domain (aa 364-404) necessary for signaling. The prevalent isoforms of RAGE are full length RAGE, RAGE_v1 or endogenous secretory (es RAGE) which lacks the cytosolic and transmembrane domains and therefore can be secreted into the extracellular space, and N-terminal truncated RAGE (RAGE_v2) which lacks N-terminal V domain and therefore cannot bind ligands. RAGE_v2 does not form mature protein. Through its ability to scavenge RAGE ligands, soluble RAGE isoforms (sRAGE) are believed to act a decoy receptor by regulating signaling mediated by activation of full length RAGE. Expression of isoforms is tissue specific, suggesting tight tissue-specific regulation of expression. sRAGE can also be formed by ectodomain cleavage by ADAM10/MMP9.
A number of NF-kappaB sites have been identified in the RAGE 5' regulatory region. In addition, transcription is also controlled by other pro-inflammatory transcription factors such as SP-1 and AP-2.
At least 30 polymorphisms are known, most of which are single nucleotide polymorphisms (SNP). A Gly to Ser change at an N-glycosylation sequon at position 82, and two 5' flanking polymorphisms at position -374 and -429 lead to altered function and expression of RAGE.

Protein

Description The V and C1 domains in the extracellular region of RAGE form an integrated structural unit, while C2 is fully independent, attached to VC1 through a flexible linker. RAGE was originally identified as a receptor for advanced glycation end products, but it also interacts with other structurally unrelated ligands including HMGB1, several members of the S100 family, amyloid-beta peptide, transthyretin and beta2 integrin Mac-1. By virtue of its multi-domain structure and ability to recognize different classes of ligands, RAGE behaves as a pattern recognition receptor (PRR) akin to innate immune receptors such as Toll-like receptors (TLRs) in orchestrating immune responses. However, unlike other PRRs that predominantly bind exogenous ligands, RAGE binds endogenous ligands, especially those considered to be damage associated molecular pattern molecules (DAMPs). AGEs, HMGB1, Abeta peptides, S100B, S100A1, S100A2 and S100A5 bind to the V domain, S100A12 binds to V-C1 domains, and S100A6 interacts with V-C2 domain. Studies on S100 protein-RAGE interactions also suggest that multimerization of ligand and receptor occurs and that formation of these higher ordered complexes may be essential for signal transduction. In addition to contribution by protein interaction domains, post-translational modifications such as glycosylation of the receptors, or acetylation or phosphorylation of ligands could also play important roles in defining specificity of interactions, multimerization and downstream signaling. RAGE has two N-glycosylation sites on the V-domain and both sites are occupied by complex and hybrid or high mannose N-glycans. A subpopulation is modified by carboxylated glycans, which promote interaction with HMGB1, S100A8/S100A9 and S100A12. In addition, the quaternary structure of RAGE might also account for the diversity of ligand recognition. Though the cytoplasmic domain lacks endogenous kinase activity or any other known signaling motif, studies indicate that the cytoplasmic domain is essential for intracellular signaling.
 
  Figure 2. Schematic of RAGE protein and its domains. RAGE is a multi-ligand receptor consisting of three Ig-domains (V, C1 and C2), a transmembrane domain and a cytosolic tail required for RAGE-mediated intracellular signaling. The V and C1 domains in the extracellular region of RAGE form an integrated structural unit, while C2 is fully independent, attached to VC1 through a flexible linker. Many ligands bind to the V domain, while some also interact with the V-C1 or V-C2 domains. The V domain has N-glycosylation sites both of which are modified. Ligand binding activates multiple signaling pathways and regulates gene expression through the transcription factors NF-kappaB, CREB and SP1 (From Rauvala H, Rouhiainen A. Biochim Biophys Acta. 2010 Jan-Feb;1799(1-2):164-70. Reproduced with permission from publishers).
Expression RAGE is highly expressed during embryonic development, especially in the brain, but levels decrease in adult tissues. RAGE is found at low levels in neurons, endothelial cells, mononuclear phagocytes, smooth muscle cells, and constitutively expressed at high levels in the lung.
Localisation - Full length: membrane: single pass type I membrane protein.
- Isoforms: secreted.
Function Normal physiological functions of RAGE include embryonal neuronal growth, myogenesis, mobilization of dendritic cells, activation and differentiation of T cells, stem cell migration and osteoclast maturation. HMGB1 interaction of RAGE results in stimulation of myogenesis. RAGE mediates trophic and toxic effects of S100B on embryonal neurons, and promotes neurite outgrowth and neuronal regeneration promoted by HMGB1. RAGE also plays an important role in the regulation of osteoclast maturation and function, and bone remodeling.
Ligand interaction promotes activation of intracellular signaling pathways including the MAPK pathway, RAC-1 and CDC42, NADPH oxidase, PI3 kinase and JAK/STAT pathway, and activation of NF-kappaB. RAGE expression is induced in inflammatory settings, since its transcription is controlled by several transcription factors as mentioned above. Thus a positive feed-forward loop evolves in ligand rich inflammatory settings, perpetuating the pathology. sRAGE is believed to regulate signaling mediated by activation of full length RAGE. Binding of RAGE to HMGB1 induces RAGE shedding by ADAM10 metalloprotease, thus possibly representing another pathway for negatively regulating RAGE mediated cellular activation.

Implicated in

Entity Gastric cancer
Note RAGE is constitutively expressed in human gastric carcinoma cell lines, and poorly differentiated human gastric carcinomas preferentially express RAGE. Strong RAGE expression is seen in cells at the invasive edge of tumors and correlates with invasion and lymph node metastasis. Studies in Chinese population show that Gly82Ser polymorphism on RAGE is associated with increased risk for gastric cancer.
  
Entity Colon cancer
Note RAGE expression is increased in advanced colon tumors. Co-expression of RAGE and its ligands HMGB1 and S100P is strongly associated with invasion and metastasis of human colorectal cancer. RAGE appears to be at the interface of inflammation and colon cancer, since RAGE deficient mice are resistant to the onset of colitis associated colon cancer.
  
Entity Pancreatic cancer
Note Expression of RAGE is strongest in pancreatic cancer cells with high metastatic ability, and RAGE may play an important role in the viability of pancreatic tumor cells against stress-induced apoptosis. RAGE ligand S100P is overexpressed in pancreatic cancer.
  
Entity Prostate cancer
Note RAGE and ligands are highly expressed on prostate cancer cell lines, untreated prostate cancer tissue and hormone-refractory prostate cancer tissue, and RAGE promotes growth and invasion of prostate cancer cells in response to ligand activation.
  
Entity Oral squamous cell cancer
Note RAGE expression closely associates with histologic differentiation, invasiveness, angiogenesis and recurrence of oral squamous cell carcinoma.
  
Entity Common bile duct cancer
Note RAGE is expressed on human biliary cancer cells, and expression correlates with their invasive ability.
  
Entity Glioma
Note HMGB1/RAGE signaling pathways promote the growth and migration of human glioblastoma cells. Inhibition of RAGE-HMGB1 interactions decreases growth and metastases of gliomas in mice.
  
Entity Skin cancer
Note RAGE is expressed in human melanoma cells and promotes ligand-dependent growth and invasion. RAGE null mice are resistant to the onset of inflammation mediated skin tumors in mice.
  
Entity Lung cancer
Note RAGE, as well as its ligands, is highly expressed in normal lung, but unlike other cancers, RAGE is markedly reduced in human lung carcinomas. Down-regulation correlates with advanced tumor stages, suggesting that RAGE may have tumor suppressive functions in lung cancer.
  
Entity Tumor microenvironment
Note Many RAGE ligands are expressed and secreted not only by cancer cells but also by cells within the tumor microenvironment, including myeloid derived cells and vascular cells. These ligands interact with the receptor in both autocrine and paracrine manners, promoting tumor growth, invasion, angiogenesis and metastasis.
  
Entity Inflammation and immune responses
Note RAGE and its ligands are highly enriched in immune and inflammatory foci and their interaction promotes upregulation of inflammatory cytokines, adhesion molecules and matrix metalloproteinases. They are therefore implicated in many inflammatory conditions including colitis and arthritis. RAGE is upregulated in synovial tissue macrophages and its ligands are abundant in inflamed synovial tissue. Activation leads to increased stimulation of chondrocytes and synoviocytes, promoting ongoing inflammation and autoimmunity in arthritis. RAGE mediates HMGB1 activation of dendritic cells in response to DNA containing immune complexes, contributing to autoimmune pathogenesis. Blockade of RAGE interactions suppresses myelin basic protein induced experimental autoimmune encephalomyelitis. Inhibition of RAGE-ligand interactions or RAGE deletion protects mice from septic shock induced by caecal ligation and puncture. RAGE null mice are also resistant to skin and colon inflammation and inflammation-based tumorigenesis.
  
Entity Diabetes
Note RAGE, as a receptor for advanced glycation end products and other pro-inflammatory ligands, contributes to micro and macrovascular changes in diabetes. RAGE over-expression in transgenic mice is associated with increased vascular injury, diabetic nephropathy and neuropathy, while RAGE deletion confers partial protection from these diabetes-associated changes.
  
Entity Atherosclerosis and ischemia
Note Increased RAGE expression is found in endothelial cells in non-diabetic patients with peripheral occlusive vascular disease. sRAGE reduces atherosclerotic lesions and inflammation in normoglycemic Apo E null mice, and reduced neointima expansion in wild type mice following femoral artery injury. Studies on ischemia-reperfusion injury of the heart in wild type and RAGE null mice show that infarct size and severity of tissue damage is dependent on HMGB1-RAGE interactions following necrotic cell death.
  
Entity Neuronal degeneration
Note RAGE is expressed on neurons, microglia and endothelial cells in the brain, and binds the multimeric form of amyloid-beta peptide. Binding leads to activation of NADPH oxidase, generation of reactive oxygen species, activation of NF-kappaB and CREB, and upregulation of cytokines and chemokines, thus promoting neuroinflammation. The associated up-regulation and release of other RAGE ligands such as HMGB1 and S100 proteins further amplifies this cascade, leading to neuronal degeneration. sRAGE has been shown to be beneficial in animal models of Alzheimer's disease. RAGE null mice are also partially protected from diabetes-induced loss of neuronal function.
  

External links

Nomenclature
HGNC (Hugo)AGER   320
Cards
AtlasAGERID594ch6p21
Entrez_Gene (NCBI)AGER  177  advanced glycosylation end product-specific receptor
GeneCards (Weizmann)AGER
Ensembl (Hinxton)ENSG00000204305 [Gene_View]  chr6:32148745-32152099 [Contig_View]  AGER [Vega]
ICGC DataPortalENSG00000204305
cBioPortalAGER
AceView (NCBI)AGER
Genatlas (Paris)AGER
WikiGenes177
SOURCE (Princeton)NM_001136 NM_001206929 NM_001206932 NM_001206934 NM_001206936 NM_001206940 NM_001206954 NM_001206966 NM_172197
Genomic and cartography
GoldenPath (UCSC)AGER  -  6p21.32   chr6:32148745-32152099 -  6p21.3   [Description]    (hg19-Feb_2009)
EnsemblAGER - 6p21.3 [CytoView]
Mapping of homologs : NCBIAGER [Mapview]
OMIM600214   
Gene and transcription
Genbank (Entrez)AB036432 AB061668 AB061669 AF536236 AF536237
RefSeq transcript (Entrez)NM_001136 NM_001206929 NM_001206932 NM_001206934 NM_001206936 NM_001206940 NM_001206954 NM_001206966 NM_172197
RefSeq genomic (Entrez)AC_000138 NC_000006 NC_018917 NG_029868 NT_007592 NT_113891 NT_167244 NT_167246 NT_167247 NT_167248 NT_167249 NW_001838980 NW_004929326
Consensus coding sequences : CCDS (NCBI)AGER
Cluster EST : UnigeneHs.534342 [ NCBI ]
CGAP (NCI)Hs.534342
Alternative Splicing : Fast-db (Paris)GSHG0026492
Alternative Splicing GalleryENSG00000204305
Gene ExpressionAGER [ NCBI-GEO ]     AGER [ SEEK ]   AGER [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ15109 (Uniprot)
NextProtQ15109  [Medical]
With graphics : InterProQ15109
Splice isoforms : SwissVarQ15109 (Swissvar)
Domaine pattern : Prosite (Expaxy)IG_LIKE (PS50835)    IG_MHC (PS00290)   
Domains : Interpro (EBI)CD80_C2-set [organisation]   Ig-like_dom [organisation]   Ig-like_fold [organisation]   Ig/MHC_CS [organisation]   Ig_sub [organisation]   Ig_sub2 [organisation]  
Related proteins : CluSTrQ15109
Domain families : Pfam (Sanger)C2-set_2 (PF08205)   
Domain families : Pfam (NCBI)pfam08205   
Domain families : Smart (EMBL)IG (SM00409)  IGc2 (SM00408)  
DMDM Disease mutations177
Blocks (Seattle)Q15109
PDB (SRS)1PWI    2BJP    2E5E    2ENS    2L7U    2LE9    2LMB    3CJJ    3O3U    4LP4    4LP5    4OF5    4OFV    4OI7    4OI8   
PDB (PDBSum)1PWI    2BJP    2E5E    2ENS    2L7U    2LE9    2LMB    3CJJ    3O3U    4LP4    4LP5    4OF5    4OFV    4OI7    4OI8   
PDB (IMB)1PWI    2BJP    2E5E    2ENS    2L7U    2LE9    2LMB    3CJJ    3O3U    4LP4    4LP5    4OF5    4OFV    4OI7    4OI8   
PDB (RSDB)1PWI    2BJP    2E5E    2ENS    2L7U    2LE9    2LMB    3CJJ    3O3U    4LP4    4LP5    4OF5    4OFV    4OI7    4OI8   
Human Protein AtlasENSG00000204305 [gene] [tissue] [antibody] [cell] [cancer]
Peptide AtlasQ15109
HPRD02568
IPIIPI00014810   IPI00220335   IPI00916198   IPI00941991   IPI00552161   IPI00909948   IPI00910654   IPI00941813   IPI00942476   IPI01020727   IPI01022617   IPI01023062   IPI01023028   IPI01022577   IPI00654726   IPI00654858   IPI00654652   IPI00431197   IPI01013135   IPI00892584   IPI00890699   IPI00893246   IPI00640024   
Protein Interaction databases
DIP (DOE-UCLA)Q15109
IntAct (EBI)Q15109
FunCoupENSG00000204305
BioGRIDAGER
InParanoidQ15109
Interologous Interaction database Q15109
IntegromeDBAGER
STRING (EMBL)AGER
Ontologies - Pathways
Ontology : AmiGOreceptor activity  transmembrane signaling receptor activity  protein binding  extracellular region  plasma membrane  integral component of plasma membrane  inflammatory response  cell surface receptor signaling pathway  response to wounding  neuron projection development  identical protein binding  S100 protein binding  innate immune response  induction of positive chemotaxis  positive regulation of NF-kappaB transcription factor activity  
Ontology : EGO-EBIreceptor activity  transmembrane signaling receptor activity  protein binding  extracellular region  plasma membrane  integral component of plasma membrane  inflammatory response  cell surface receptor signaling pathway  response to wounding  neuron projection development  identical protein binding  S100 protein binding  innate immune response  induction of positive chemotaxis  positive regulation of NF-kappaB transcription factor activity  
Protein Interaction DatabaseAGER
Wikipedia pathwaysAGER
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)AGER
snp3D : Map Gene to Disease177
SNP (GeneSNP Utah)AGER
SNP : HGBaseAGER
Genetic variants : HAPMAPAGER
Exome VariantAGER
1000_GenomesAGER 
ICGC programENSG00000204305 
Somatic Mutations in Cancer : COSMICAGER 
CONAN: Copy Number AnalysisAGER 
Mutations and Diseases : HGMDAGER
Mutations and Diseases : intOGenAGER
Genomic VariantsAGER  AGER [DGVbeta]
dbVarAGER
ClinVarAGER
Pred. of missensesPolyPhen-2  SIFT(SG)  SIFT(JCVI)  Align-GVGD  MutAssessor  Mutanalyser  
Pred. splicesGeneSplicer  Human Splicing Finder  MaxEntScan  
Diseases
OMIM600214   
MedgenAGER
GENETestsAGER
Disease Genetic AssociationAGER
Huge Navigator AGER [HugePedia]  AGER [HugeCancerGEM]
General knowledge
Homologs : HomoloGeneAGER
Homology/Alignments : Family Browser (UCSC)AGER
Phylogenetic Trees/Animal Genes : TreeFamAGER
Chemical/Protein Interactions : CTD177
Chemical/Pharm GKB GenePA24617
Clinical trialAGER
Cancer Resource (Charite)ENSG00000204305
Other databases
Probes
Litterature
PubMed499 Pubmed reference(s) in Entrez
CoreMineAGER
iHOPAGER
OncoSearchAGER

Bibliography

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The extracellular region of the receptor for advanced glycation end products is composed of two independent structural units.
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S100B and S100A6 differentially modulate cell survival by interacting with distinct RAGE (receptor for advanced glycation end products) immunoglobulin domains.
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RAGE signaling sustains inflammation and promotes tumor development.
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Identification, classification, and expression of RAGE gene splice variants.
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RAGE, carboxylated glycans and S100A8/A9 play essential roles in colitis-associated carcinogenesis.
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RAGE: a novel biological and genetic marker for vascular disease.
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Carboxylated N-glycans on RAGE promote S100A12 binding and signaling.
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Contributor(s)

Written06-2010Geetha Srikrishna, Barry Hudson
Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, California 92037, USA (GS); Columbia University Medical Center, 630 West 168th St. New York, NY 10032, USA (BH)

Citation

This paper should be referenced as such :
Srikrishna G, Hudson B
AGER (advanced glycosylation end product-specific receptor);
Atlas Genet Cytogenet Oncol Haematol. June 2010
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/AGERID594ch6p21.html

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