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Human AGER Protein expressed in HEK-293 Cells - ABIN2180572
Xue, Rai, Singer, Chabierski, Xie, Reverdatto, Burz, Schmidt, Hoffmann, Shekhtman: Advanced glycation end product recognition by the receptor for AGEs. in Structure (London, England : 1993) 2011
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Human AGER Protein expressed in Human Cells - ABIN2004453
Sugaya, Fukagawa, Matsumoto, Mita, Takahashi, Ando, Inoko, Ikemura et al.: 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 ... in Genomics 1995
Show all 5 Pubmed References
Our findings suggested that polymorphisms in the RAGE gene are involved in genetic susceptibility to Alzheimer disease but did not modify the risk of lewy body disease.
Findings suggest soluble Receptor (show IFNAR1 Proteins) for Advanced Glycation End products (sRAGE) protein from sRAGE-mesenchymal stem cells (MSC (show MSC Proteins)) has better protection against neuronal cell death than sRAGE protein or single MSC (show MSC Proteins) treatment by inhibiting the RAGE cell death cascade and RAGE-induce inflammation.
Protection against diabetic nephropathy in RAGE knockout mice is likely to be due in part to the decreased responsiveness to TGF beta (show TGFB1 Proteins) stimulation and an antiapoptotic phenotype in mesangial cells.
the A allele of RAGE -374T/A polymorphism probably increase diabetic retinopathy risk (Meta-Analysis)
Advanced glycation end products decrease collagen I levels in fibroblasts from the vaginal wall of patients with pelvic organ prolapse via the RAGE, MAPK (show MAPK1 Proteins) and NF-kappaB (show NFKB1 Proteins) pathways.
we identified two risk-associated polymorphisms (rs1045411 and rs2070600), and more importantly a joint impact of seven polymorphisms from the HMGB1 (show HMGB1 Proteins)/RAGE axis in susceptibility to hepatocellular carcinoma
the G82S variant of the RAGE gene was significantly associated with an increased risk of all-cause mortality and acute myocardial infarction in the Chinese Han population.
both RAGE and mitochondrial damage primed NLRP3 (show NLRP3 Proteins) and pro-IL-1beta (show IL1B Proteins) activation as upstream signals of NF-kappaB (show NFKB1 Proteins) activity, whereas mitochondrial damage was critical for the assembly of inflammasome components. These results revealed that accumulation of AGEs in NP tissue may initiate inflammation-related degeneration of the intervertebral disc via activation of the NLRP3 (show NLRP3 Proteins) inflammasome.
The main mechanism of Integrin alphaXbeta2 I-domain binding to RAGE is a charge interaction, in which the acidic moieties of Integrin alphaXbeta2 I-domains, including E244, and D249, recognize the basic residues on the RAGE V-domain encompassing K39, K43, K44, R104, and K107.
An overexpression of the receptor for RAGE was found in lesioned samples of patients with acquired reactive perforating collagenosis.
study found that diabetes predisposes to more severe infections because of additional inflammatory output through dual activation of MyD88 (show MYD88 Proteins) by not only TLR4 (show TLR4 Proteins) but also RAGE
RAGE controls myocardial dysfunction and oxidative stress in high-fat fed mice by sustaining mitochondrial dynamics and autophagy-lysosome pathway.
these data provide a previously uncharacterized in vivo mechanism contingent on oligodeoxy-nucleotide -administered dose, where TLR9 (show TLR9 Proteins) governs the primary response and RAGE plays a distinct and cooperative function in providing a pivotal role in balancing the immune response.
data demonstrate that under the diabetic condition, DRG neurons are directly affected by elevated levels of glucose, independent of vascular or glial signals, and dependent on RAGE expression.
findings suggest that HMGB1 (show HMGB1 Proteins) induces the transcytosis of albumin (show ALB Proteins) via RAGE-dependent Src (show SRC Proteins) phosphorylation and Cav-1 (show CAV1 Proteins) phosphorylation. These studies revealed a new mechanism of HMGB1 (show HMGB1 Proteins)-induced endothelial hyperpermeability.
data suggest that S100A8 (show S100A8 Proteins)/A9 acts directly on BV-2 microglial cells via binding to TLR4 (show TLR4 Proteins) and RAGE on the membrane and then stimulates the secretion of proinflammatory cytokines through ERK (show EPHB2 Proteins) and JNK (show MAPK8 Proteins)-mediated NF-kappaB (show NFKB1 Proteins) activity in BV-2 microglial cells.
Activation of RAGE facilitates the development of hypoxia-induced pulmonary hypertension by increasing ECM (show MMRN1 Proteins) deposition in pulmonary arteries.
knockout of RAGE significantly ameliorates mainstream cigarette smoke-induced airway inflammation in mice
Here, the authors show that RAGE deficiency impairs anti-viral immunity during an early-life infection with pneumonia virus of mice (PVM; a murine analogue of RSV). The elevated viral load was associated with the release of high mobility group box-1 (HMGB1 (show HMGB1 Proteins)) which triggered airway smooth muscle remodelling in early-life.
We investigated the role of RAGE in postischaemic leukocyte adhesion after myocardial infarction and its effect on postischaemic myocardial function. RAGE represents an additional pro-inflammatory endothelial mediator of ischaemia-reperfusion injury.
Our results suggested that the increased RAGE expression in inflammatory circumstances and interaction with AGEs are risk factors in decreasing of aggrecan (show ACAN Proteins) content in nucleus pulposus.
The advanced glycosylation end product (AGE) receptor encoded by this gene is a member of the immunoglobulin superfamily of cell surface receptors. It is a multiligand receptor, and besides AGE, interacts with other molecules implicated in homeostasis, development, and inflammation, and certain diseases, such as diabetes and Alzheimer's disease. Many alternatively spliced transcript variants encoding different isoforms, as well as non-protein-coding variants, have been described for this gene (PMID:18089847).
RAGE isoform NtRAGE-delta
, RAGE isoform sRAGE-delta
, advanced glycation end-products receptor
, receptor for advanced glycosylation end products
, advanced glycosylation end product-specific receptor variant 2
, advanced glycosylation end product-specific receptor variant 3
, advanced glycosylation end product-specific receptor variant 4
, advanced glycosylation end product-specific receptor variant 5
, advanced glycosylation end product-specific receptor variant 1
, advanced glycosylation end product-specific receptor variant 6
, advanced glycosylation end product-specific receptor variant 7
, advanced glycosylation end product-specific receptor variant 8
, advanced glycation end product receptor
, advanced glycosylation end product-specific receptor
, MAPK/MAK/MRK overlapping kinase
, renal tumor antigen