scholarly journals The receptor for advanced glycation endproducts (RAGE) and cardiovascular disease

2009 ◽  
Vol 11 ◽  
Author(s):  
Shi Fang Yan ◽  
Ravichandran Ramasamy ◽  
Ann Marie Schmidt
Keyword(s):  
Advanced Glycation Endproducts ◽  
High Mobility ◽  
Amyloid Peptide ◽  
Immunoglobulin Superfamily ◽  
Advanced Glycation ◽  
Ischaemia Reperfusion Injury ◽  
Glycation Endproducts ◽  
Beneficial Effects ◽  
Ischaemia Reperfusion ◽  
Great Vessels

Recent and compelling investigation has expanded our view of the biological settings in which the products of nonenzymatic glycation and oxidation of proteins and lipids – the advanced glycation endproducts (AGEs) – form and accumulate. Beyond diabetes, natural ageing and renal failure, AGEs form in inflammation, oxidative stress and in ischaemia–reperfusion. The chief signal transduction receptor for AGEs – the receptor for AGEs (RAGE) – is a multiligand-binding member of the immunoglobulin superfamily. In addition to AGEs, RAGE binds certain members of the S100/calgranulin family, high-mobility group box 1 (HMGB1), and β-amyloid peptide and β-sheet fibrils. Recent studies demonstrate beneficial effects of RAGE antagonism and genetic deletion in rodent models of atherosclerosis and ischaemia–reperfusion injury in the heart and great vessels. Experimental evidence is accruing that RAGE ligand generation and release during ischaemia–reperfusion may signal through RAGE, thus suggesting that antagonism of this receptor might provide a novel form of therapeutic intervention in heart disease. However, it is plausible that innate, tissue-regenerative roles for these RAGE ligands may also impact the failing heart – perhaps through RAGE and/or distinct receptors. In this review, we focus on RAGE and the consequences of its activation in the cardiovasculature.

scholarly journals The Development of Prototype Polyclonal Antibody of Receptor Advanced Glycation of Endproducts (RAGE)

2018 ◽  
Vol 2 (1) ◽  
pp. 34-40
Author(s):  
Mgs Irsan Saleh ◽  
Nita Parisa ◽  
Ziske Maritska
Keyword(s):  
Calcium Binding ◽  
Transmembrane Protein ◽  
Advanced Glycation Endproducts ◽  
High Mobility ◽  
Immunoglobulin Superfamily ◽  
Advanced Glycation ◽  
High Mobility Group Protein ◽  
Glycation Endproducts ◽  
S 100 ◽  
And Migration

Abstract Background Receptor for advanced glycation endproducts (RAGE) is a transmembrane protein that belongs to the immunoglobulin superfamily. As its name implicates, it can bind to advanced glycation endproducts, the resulting product of non-enzymatic glycosylation, and it also has the ability to interact with multiple ligands having common motifs as a so-called multi-ligand receptor. The ligands include high-mobility group protein (B)1 (HMGB1), S-100 calcium-binding protein, amyloid-β-protein, Mac-1, and phosphatidylserine. Interaction between RAGE and its ligands activates various cellular processes, including inflammation, proliferation, apoptosis, autophagy, and migration. Methods The proccess of isolation protein of RAGE was initiated with extraction protein and purification of RAGE protein. After that, the immunization of Rats was be done to produce Anti-RAGE. The confirmation of Anti RAGE was be done by SDS PAGE and Immunobloting. Results The production of Anti RAGE was enough pure compared by Anti RAGE commercial. Anti RAGE was protein that have molecular weight around 35 kD. Conclusion The methods that used in this study effective to develop production of anti-RAGE. Keywords : Anti RAGE – Isolation – Production Antibody

scholarly journals The Immune Tolerance Role of the HMGB1-RAGE Axis

Cells ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 564
Author(s):  
Haruki Watanabe ◽  
Myoungsun Son
Keyword(s):  
Immune Responses ◽  
Immune Tolerance ◽  
Lupus Erythematosus ◽  
Advanced Glycation Endproducts ◽  
High Mobility ◽  
Chromatin Binding ◽  
Advanced Glycation ◽  
Glycation Endproducts ◽  
Extracellular Milieu

The disruption of the immune tolerance induces autoimmunity such as systemic lupus erythematosus and vasculitis. A chromatin-binding non-histone protein, high mobility group box 1 (HMGB1), is released from the nucleus to the extracellular milieu in particular environments such as autoimmunity, sepsis and hypoxia. Extracellular HMGB1 engages pattern recognition receptors, including Toll-like receptors (TLRs) and the receptor for advanced glycation endproducts (RAGE). While the HMGB1-RAGE axis drives inflammation in various diseases, recent studies also focus on the anti-inflammatory effects of HMGB1 and RAGE. This review discusses current perspectives on HMGB1 and RAGE’s roles in controlling inflammation and immune tolerance. We also suggest how RAGE heterodimers responding microenvironments functions in immune responses.

scholarly journals The High Mobility Group (Hmg) Boxes of the Nuclear Protein Hmg1 Induce Chemotaxis and Cytoskeleton Reorganization in Rat Smooth Muscle Cells

2001 ◽  
Vol 152 (6) ◽  
pp. 1197-1206 ◽  
Author(s):  
Bernard Degryse ◽  
Tiziana Bonaldi ◽  
Paola Scaffidi ◽  
Susanne Müller ◽  
Massimo Resnati ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Cell Migration ◽  
Smooth Muscle Cells ◽  
Advanced Glycation Endproducts ◽  
High Mobility ◽  
Muscle Cells ◽  
Advanced Glycation ◽  
Glycation Endproducts ◽  
Cytoskeleton Reorganization ◽  
Mitogen Activated Protein

HMG1 (high mobility group 1) is a ubiquitous and abundant chromatin component. However, HMG1 can be secreted by activated macrophages and monocytes, and can act as a mediator of inflammation and endotoxic lethality. Here we document a role of extracellular HMG1 in cell migration. HMG1 (and its individual DNA-binding domains) stimulated migration of rat smooth muscle cells in chemotaxis, chemokinesis, and wound healing assays. HMG1 induced rapid and transient changes of cell shape, and actin cytoskeleton reorganization leading to an elongated polarized morphology typical of motile cells. These effects were inhibited by antibodies directed against the receptor of advanced glycation endproducts, indicating that the receptor of advanced glycation endproducts is the receptor mediating the HMG1-dependent migratory responses. Pertussis toxin and the mitogen-activated protein kinase kinase inhibitor PD98059 also blocked HMG1-induced rat smooth muscle cell migration, suggesting that a Gi/o protein and mitogen-activated protein kinases are required for the HMG1 signaling pathway. We also show that HMG1 can be released by damage or necrosis of a variety of cell types, including endothelial cells. Thus, HMG1 has all the hallmarks of a molecule that can promote atherosclerosis and restenosis after vascular damage.

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