Relevant bibliographies by topics / Receptors for advanced glycation end product (RAGE)

Academic literature on the topic 'Receptors for advanced glycation end product (RAGE)'

Author: Grafiati
Published: 4 June 2021
Last updated: 19 February 2022

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Journal articles on the topic "Receptors for advanced glycation end product (RAGE)"

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Mangalmurti, Nilam S., Jessica Friedman, Don L. Siegel, Janet Lee, and Steven M. Albelda. "Erythrocyte Advanced Glycation End-Products as Novel Mediators of Endothelial Dysfunction Following Transfusion." Blood 120, no. 21 (November 16, 2012): SCI—47—SCI—47. http://dx.doi.org/10.1182/blood.v120.21.sci-47.sci-47.

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Abstract Abstract SCI-47 Red cell transfusions are associated with the development of acute lung injury in critically ill patients, yet the mechanisms for this association remain unknown. We have previously shown that stored red blood cells (RBCs) express the advanced glycation end-product Nε-carboxymethyl lysine (Nε-CML) (1). Advanced glycation end-products (AGEs), a heterogeneous group of adducts formed during states of increased oxidative stress or hyperglycemia, are thought to exert their effects by binding to membrane receptors, including RAGE (the receptor for advanced glycation-end products). RAGE is a multiligand pattern-recognition receptor implicated in vascular disease whose function in lung endothelium remains unknown. Our previous data demonstrate that RAGE ligands on stored erythrocytes can induce reactive oxygen species in lung endothelial cells. We therefore hypothesized that RAGE ligands on the surface of stored RBCs exacerbate lung inflammation by interacting with the pulmonary endothelium, thus possibly participating in the pathogenesis of lung injury following transfusion. We first examined lung endothelial cells at baseline using multiple techniques and observed low basal expression of RAGE. Because RAGE ligands can induce the expression of RAGE, and stored red blood cells (RBCs) express the RAGE ligand Nε-carboxymethyl lysine (Nε-CML), we investigated whether RBC transfusion would augment RAGE expression on lung endothelium utilizing a syngeneic model of RBC transfusion. Increased lung endothelial RAGE expression and enhanced lung inflammation and endothelial activation was observed, as evidenced by increases in lung high mobility group box 1 (HMGB1) and vascular cell adhesion molecule (VCAM-1) expression following transfusion. These effects were mediated by RAGE, as endothelial activation was absent in RBC-transfused Rage knockout mice. Therefore, functional consequences of RBC transfusion are augmented RAGE expression, increased RAGE ligation, and endothelial activation, thus linking RAGE activation to lung inflammation following RBC transfusion. Disclosures: No relevant conflicts of interest to declare.
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Wautier, Jean-Luc, and Marie-Paule Wautier. "Cellular and Molecular Aspects of Blood Cell–Endothelium Interactions in Vascular Disorders." International Journal of Molecular Sciences 21, no. 15 (July 27, 2020): 5315. http://dx.doi.org/10.3390/ijms21155315.

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In physiology and pathophysiology the molecules involved in blood cell–blood cell and blood cell–endothelium interactions have been identified. Platelet aggregation and adhesion to the walls belonging to vessels involve glycoproteins (GP), GP llb and GP llla and the GP Ib–IX–V complex. Red blood cells (RBCs) in normal situations have little interaction with the endothelium. Abnormal adhesion of RBCs was first observed in sickle cell anemia involving vascular cell adhesion molecule (VCAM)-1, α4β1, Lu/BCAM, and intercellular adhesion molecule (ICAM)-4. More recently RBC adhesion was found to be increased in retinal-vein occlusion (RVO) and in polycythemia vera (PV). The molecules which participate in this process are phosphatidylserine and annexin V in RVO, and phosphorylated Lu/BCAM and α5 laminin chain in PV. The additional adhesion in diabetes mellitus occurs due to the glycated RBC band 3 and the advanced glycation end-product receptors. The multiligand receptor binds advanced glycation end products (AGEs) or S100 calgranulins, or β-amyloid peptide. This receptor for advanced glycation end products is known as RAGE. The binding to RAGE-activated endothelial cells leads to an inflammatory reaction and a prothrombotic state via NADPH activation and altered gene expression. RAGE blockade is a potential target for drugs preventing the deleterious consequences of RAGE activation.
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Kuzan, Aleksandra, Emilia Królewicz, Karolina Nowakowska, Kamilla Stach, Krzysztof Kaliszewski, Paweł Domosławski, Łukasz Kotyra, Andrzej Gamian, and Irena Kustrzeba-Wójcicka. "Contribution of Glycation and Oxidative Stress to Thyroid Gland Pathology—A Pilot Study." Biomolecules 11, no. 4 (April 10, 2021): 557. http://dx.doi.org/10.3390/biom11040557.

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The patho-mechanism of changes in the thyroid gland, including carcinogenesis, is a complex process, which involves oxidative stress. The goal of our investigation was to verify the extent of stress in the thyroid gland related to glycation. The study samples were comprised of blood sera, thyroid, and adipose tissue sections probed from 37 patients diagnosed with thyroid cancers and goiter. Using immuno-enzymatic and fluorometric assays we analyzed the content of advanced glycation end-products (AGEs), pentosidine, receptors for advanced glycation end-products (RAGE), scavenger receptor class (SR)-A, SR-B, glutathione, malondialdehyde and nitric oxide synthase. In addition to classic AGEs, a recent study detected the melibiose-derived glycation (MAGE) product. We demonstrated the presence of AGEs, MAGE and their receptors of the RAGE and SR-A. In addition, in the control samples of thyroid glands SR-B groups were detected as well as of pathological groups without noticeable tendency to antigen concentration in the area of carcinogenesis. Fluorescent AGEs correlate positively with glutathione, which supports the assumption that glycation stress leads to augmentation of oxidative stress and increase of the intensity of antioxidant mechanisms.
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Buckley, Stephen T., and Carsten Ehrhardt. "The Receptor for Advanced Glycation End Products (RAGE) and the Lung." Journal of Biomedicine and Biotechnology 2010 (2010): 1–11. http://dx.doi.org/10.1155/2010/917108.

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The receptor for advanced glycation end products (RAGE) is a member of the immunoglobulin superfamily of cell surface molecules. As a pattern-recognition receptor capable of binding a diverse range of ligands, it is typically expressed at low levels under normal physiological conditions in the majority of tissues. In contrast, the lung exhibits high basal level expression of RAGE localised primarily in alveolar type I (ATI) cells, suggesting a potentially important role for the receptor in maintaining lung homeostasis. Indeed, disruption of RAGE levels has been implicated in the pathogenesis of a variety of pulmonary disorders including cancer and fibrosis. Furthermore, its soluble isoforms, sRAGE, which act as decoy receptors, have been shown to be a useful marker of ATI cell injury. Whilst RAGE undoubtedly plays an important role in the biology of the lung, it remains unclear as to the exact nature of this contribution under both physiological and pathological conditions.
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Jensen, Louise J. N., Allan Flyvbjerg, and Mette Bjerre. "Soluble Receptor for Advanced Glycation End Product: A Biomarker for Acute Coronary Syndrome." BioMed Research International 2015 (2015): 1–7. http://dx.doi.org/10.1155/2015/815942.

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The receptor of advanced glycation end products (RAGE) and its ligands are linked to the pathogenesis of coronary artery disease (CAD), and circulating soluble receptor of advanced glycation end products (sRAGE), reflecting the RAGE activity, is suggested as a potential biomarker. Elevated sRAGE levels are reported in relation to acute ischemia and this review focuses on the role of sRAGE as a biomarker for the acute coronary syndrome (ACS). The current studies demonstrated that sRAGE levels are elevated in relation to ACS, however during a very narrow time period, indicating that the time of sampling needs attention. Interestingly, activation of RAGE may influence the pathogenesis and reflection in sRAGE levels in acute and stable CAD differently.
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Rouhiainen, Ari, Niko-Petteri Nykänen, Juha Kuja-Panula, Päivi Vanttola, Henri Huttunen, and Heikki Rauvala. "Inhibition of Homophilic Interactions and Ligand Binding of the Receptor for Advanced Glycation End Products by Heparin and Heparin-Related Carbohydrate Structures." Medicines 5, no. 3 (July 30, 2018): 79. http://dx.doi.org/10.3390/medicines5030079.

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Background: Heparin and heparin-related sulphated carbohydrates inhibit ligand binding of the receptor for advanced glycation end products (RAGE). Here, we have studied the ability of heparin to inhibit homophilic interactions of RAGE in living cells and studied how heparin related structures interfere with RAGE–ligand interactions. Methods: Homophilic interactions of RAGE were studied with bead aggregation and living cell protein-fragment complementation assays. Ligand binding was analyzed with microwell binding and chromatographic assays. Cell surface advanced glycation end product binding to RAGE was studied using PC3 cell adhesion assay. Results: Homophilic binding of RAGE was mediated by V1- and modulated by C2-domain in bead aggregation assay. Dimerisation of RAGE on the living cell surface was inhibited by heparin. Sulphated K5 carbohydrate fragments inhibited RAGE binding to amyloid β-peptide and HMGB1. The inhibition was dependent on the level of sulfation and the length of the carbohydrate backbone. α-d-Glucopyranosiduronic acid (glycyrrhizin) inhibited RAGE binding to advanced glycation end products in PC3 cell adhesion and protein binding assays. Further, glycyrrhizin inhibited HMGB1 and HMGB1 A-box binding to heparin. Conclusions: Our results show that K5 polysaccharides and glycyrrhizin are promising candidates for RAGE targeting drug development.
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Sotokawauchi, Ami, Takanori Matsui, Yuichiro Higashimoto, and Sho-ichi Yamagishi. "Fructose causes endothelial cell damage via activation of advanced glycation end products–receptor system." Diabetes and Vascular Disease Research 16, no. 6 (August 2, 2019): 556–61. http://dx.doi.org/10.1177/1479164119866390.

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Objective: Advanced glycation end products and their receptor – RAGE – in the adipose tissues contribute to metabolic derangements in fructose-fed rats. However, it remains unclear whether fructose could cause endothelial cell damage via the activation of AGE-RAGE. Methods: Intracellular advanced glycation end products were evaluated by dot blot analysis. Fructose-derived advanced glycation end products (Fruc-AGEs) were prepared by incubating bovine serum albumin with fructose for 8 weeks. Reactive oxygen species generation was measured using a fluorescent probe. Vascular cell adhesion molecule-1 gene expression was analysed by reverse transcription-polymerase chain reaction. Binding affinities of Fruc-AGEs to DNA-aptamer raised against Fruc-AGEs (Fruc-AGE-aptamer) or RAGE were measured with a quartz crystal microbalance. Results: Fructose increased the advanced glycation end product–specific fluorescence intensity in assay medium, while it stimulated intracellular formation of advanced glycation end products in human umbilical vein endothelial cells. Furthermore, 0.3 mM fructose for 4 days significantly increased reactive oxygen species generation and vascular cell adhesion molecule-1 gene expression in human umbilical vein endothelial cells. Fruc-AGE-aptamer, but not Control-aptamer, bound to Fruc-AGEs with Kd value of 5.60 × 10−6 M and dose-dependently inhibited the binding of Fruc-AGEs to RAGE. Moreover, Fruc-AGE-aptamer prevented the Fruc-AGE- and fructose-induced reactive oxygen species generation and vascular cell adhesion molecule-1 gene expression in human umbilical vein endothelial cells. Conclusion: This study suggests that fructose may elicit endothelial cell damage partly via the activation of AGE-RAGE axis.
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Zhou, Xiaoyan, Jie Weng, Jing Xu, Qiulin Xu, Weiju Wang, Weijin Zhang, Qiaobing Huang, and Xiaohua Guo. "Mdia1 is Crucial for Advanced Glycation End Product-Induced Endothelial Hyperpermeability." Cellular Physiology and Biochemistry 45, no. 4 (2018): 1717–30. http://dx.doi.org/10.1159/000487780.

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Background/Aims: Disruption of endothelial barrier integrity in response to advanced glycation end products (AEGs) stimulation contributes to vasculopathy associated with diabetes mellitus. Mammalian diaphanous-related formin (mDia1) has been reported to bind to the cytoplasmic domain of the receptor for advanced glycation end products (RAGE), which induces a series of cellular processes. This study directly evaluated the participation of mDia1 in AGE-induced hyperpermeability and revealed the precise intracellular signal transductions of this pathological process. Methods: Human umbilical vein endothelial cells (HUVECs) were used in the in vitro studies. Trans-endothelial electric resistance and permeability coefficient for dextran (Pd) were measured to analyze cell permeability. Western blotting, immunofluorescence staining and flow cytometry assay were performed to investigate the underlying mechanism. Dextran flux across the mesentery in mice was monitored to investigate in vivo microvascular permeability. Results: we found that AGEs evoked Nox4 membrane translocation, reactive oxygen species production, phosphorylation of Src and VE-cadherin, dissociation of adherens junctions and eventual endothelial hyperpermeability through RAGE-mDia1 binding. Cells overexpressing mDia1 by recombinant adenovirus infection showed stronger cellular responses induced by AGEs. Down-regulation of mDia1 by infection with an adenovirus encoding siRNA or blockade of RAGE-mDia1 binding by transfection with RAGE mutant plasmids into HUVECs abolished these AGE-induced effects. Furthermore, knockdown of mDia1 using an adenovirus or genetical knockout of RAGE in C57 mice rescued AGE-evoked microvascular hyperpermeability. Conclusion: Our study revealed that mDia1 plays a critical role in AGE-induced microvascular hyperpermeability through binding to RAGE.
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Bohlender, Jürgen M., Sybille Franke, Günter Stein, and Gunter Wolf. "Advanced glycation end products and the kidney." American Journal of Physiology-Renal Physiology 289, no. 4 (October 2005): F645—F659. http://dx.doi.org/10.1152/ajprenal.00398.2004.

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Advanced glycation end products (AGEs) are a heterogeneous group of protein and lipids to which sugar residues are covalently bound. AGE formation is increased in situations with hyperglycemia (e.g., diabetes mellitus) and is also stimulated by oxidative stress, for example in uremia. It appears that activation of the renin-angiotensin system may contribute to AGE formation through various mechanisms. Although AGEs could nonspecifically bind to basement membranes and modify their properties, they also induce specific cellular responses including the release of profibrogenic and proinflammatory cytokines by interacting with the receptor for AGE (RAGE). However, additional receptors could bind AGEs, adding to the complexity of this system. The kidney is both: culprit and target of AGEs. A decrease in renal function increases circulating AGE concentrations by reduced clearance as well as increased formation. On the other hand, AGEs are involved in the structural changes of progressive nephropathies such as glomerulosclerosis, interstitial fibrosis, and tubular atrophy. These effects are most prominent in diabetic nephropathy, but they also contribute to renal pathophysiology in other nondiabetic renal diseases. Interference with AGE formation has therapeutic potential for preventing the progression of chronic renal diseases, as shown from data of animal experiments and, more recently, the first clinical trials.
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Eichhorst, Alexandra, Christoph Daniel, Rita Rzepka, Bettina Sehnert, Falk Nimmerjahn, Reinhard E. Voll, and Nina Chevalier. "Relevance of Receptor for Advanced Glycation end Products (RAGE) in Murine Antibody-Mediated Autoimmune Diseases." International Journal of Molecular Sciences 20, no. 13 (July 1, 2019): 3234. http://dx.doi.org/10.3390/ijms20133234.

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It is incompletely understood how self-antigens become targets of humoral immunity in antibody-mediated autoimmune diseases. In this context, alarmins are discussed as an important level of regulation. Alarmins are recognized by various receptors, such as receptor for advanced glycation end products (RAGE). As RAGE is upregulated under inflammatory conditions, strongly binds nucleic acids and mediates pro-inflammatory responses upon alarmin recognition, our aim was to examine its contribution to immune complex-mediated autoimmune diseases. This question was addressed employing RAGE−/− animals in murine models of pristane-induced lupus, collagen-induced, and serum-transfer arthritis. Autoantibodies were assessed by enzyme-linked immunosorbent assay, renal disease by quantification of proteinuria and histology, arthritis by scoring joint inflammation. The associated immune status was determined by flow cytometry. In both disease entities, we detected tendentiously decreased autoantibody levels in RAGE−/− mice, however no differences in clinical outcome. In accordance with autoantibody levels, a subgroup of the RAGE−/− animals showed a decrease in plasma cells, and germinal center B cells and an increase in follicular B cells. Based on our results, we suggest that RAGE deficiency alone does not significantly affect antibody-mediated autoimmunity. RAGE may rather exert its effects along with other receptors linking environmental factors to auto-reactive immune responses.
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Dissertations / Theses on the topic "Receptors for advanced glycation end product (RAGE)"

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Nelson, Michael Bruce. "The Role of Receptors for Advanced Glycation End-Products (RAGE) and Ceramide in Cardiovascular Disease." BYU ScholarsArchive, 2015. https://scholarsarchive.byu.edu/etd/4423.

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Type 2 diabetes and cigarette smoke exposure are associated with an increased risk of cardiovascular complications. The role of advanced glycation end-products (AGEs) is already well-established in numerous comorbidities including cardiomyopathy. Given the role of AGEs and their receptor, RAGE, in activating inflammatory pathways, we sought to determine whether ceramides could be a mediator of RAGE-induced altered heart mitochondrial function. Using an in vitro model, we treated H9C2 cardiomyocytes with carboxy-methyl lysine-BSA, followed by mitochondrial respiration assessment. We found that mitochondrial respiration was significantly impaired in AGE-treated cells, but not when co-treated with myriocin, an inhibitor of de novo ceramide biosynthesis. Moreover, we exposed WT and RAGE KO mice to side-stream cigarette smoke and found reduced mitochondrial respiration in the left ventricle myocardium from WT mice, but the RAGE KO mice were protected from this effect. Finally, conditional over-expression of RAGE in the lungs of mice also elicited a robust increase in left ventricular ceramides. Altogether, these findings suggest a RAGE-ceramide axis as an important contributor to cardiomyopathy.
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Jyoti, Faidat. "Development of New Antibody Based Theranostic Agents Targeting the Receptor for Advanced Glycation End-Product (Rage)." Diss., North Dakota State University, 2013. https://hdl.handle.net/10365/26866.

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The Receptor for Advanced Glycation End products (RAGE) interacts with several classes of structurally unrelated ligands. The activation of RAGE by its ligands results in the cellular activation of several kinases and transcription factors including mitogen activated protein kinases (MAPKs) and nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) resulting in sustained inflammation, which is involved in pathologies such as diabetes, cancer, Alzheimer's disease, multiple sclerosis and other diseases associated with chronic inflammation. Current mouse models of human disease have shown that RAGE activity can be efficiently suppressed using either soluble RAGE (sRAGE) or anti-RAGE antibodies as inhibitors. Our goal was to generate new monoclonal antibodies against RAGE that can serve as diagnostic as wells as therapeutic tools in RAGE related pathologies. The chapters in this dissertation are a complete documentation of the development of these anti-RAGE antibodies. Additionally, an introductory review of antibodies, which includes structure and function, types of antibodies and production and basic understanding of RAGE and its ligands, has been provided to facilitate the understanding of the chapters. The first chapter details the development and characterization of anti-RAGE antibodies produced from hybridoma. The next chapter explores the effects of the generated antibodies to mammalian cells in in vitro settings and the final chapter applies the generated antibodies in vivo. During the course of this work, the antibodies developed showed binding to RAGE at nano-molar affinities which are comparable to the affinities of current antibodies used for therapeutic purposes, diagnostic and research purposes. We were also able to delineate that the possible mechanism of action of the antibodies is by preventing binding to RAGE. Lastly, we observed that one of the generated antibodies was able to reduce tumor growth in vivo in a melanoma xenograft mouse model.
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Wood, Tyler Thomas. "Targeting of Receptors for Advanced Glycation End-Products (RAGE) Diminishes Acute Secondhand Smoke-Induced Inflammation in Mice." BYU ScholarsArchive, 2014. https://scholarsarchive.byu.edu/etd/4220.

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The receptor for advanced glycation end-products (RAGE) has increasingly been demonstrated to be an important modulator of inflammation in cases of pulmonary disease. Published reports involving tobacco smoke exposure have demonstrated increased expression of RAGE, its participation in pro-inflammatory signaling and its role in irreversible pulmonary remodeling. The current research evaluated for the first time the in vivo effects of short-term tobacco smoke exposure in RAGE null and control mice compared to identical animals exposed to room air only. Quantitative real time PCR, immunoblotting, and immunohistochemistry revealed elevated RAGE expression in controls after four weeks of exposure and an anticipated absence of RAGE expression in RAGE null mice regardless of smoke exposure. Inflammatory cell behaviors were confirmed by measuring active Ras, NF-κB, and cytokine synthesis and secretion. Furthermore, bronchoalveolar lavage fluid (BALF) was procured from RAGE null and control animals after exposure for the assessment of total protein in order to indirectly measure vascular permeability, inflammatory cells and chemoattractant molecules involved in the inflammatory response. As a general theme, inflammation induced by tobacco smoke exposure was influenced by the availability of RAGE. These data reveal captivating information suggesting a role for RAGE signaling in lungs exposed to tobacco smoke. Furthermore, research may demonstrate RAGE signaling as an important therapeutic target capable of ameliorating cell level inflammation in those coping with exposure.
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Alexander, Kristen Lena. "Differential Receptors for Advanced Glycation End-Products (RAGE) Expression in Preeclampsia, Intrauterine Growth Restriction and Gestational Diabetes." BYU ScholarsArchive, 2015. https://scholarsarchive.byu.edu/etd/5463.

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Preeclampsia (PE), intrauterine growth restriction (IUGR) and gestational diabetes (GDM) increase the risk of maternal and fetal morbidity and mortality. The roles of Advanced Glycation End-products (AGEs) are already well documented concerning inflammation, hypoxia and oxidative stress. AGEs bind to its receptor, Receptor for Advanced Glycation End-products (RAGE), and activate an inflammatory pathway. This pathway alters the efficacy of invasive trophoblast cells and in the placenta and can result in placental dysfunction. We hypothesized that the placental dysfunction found in PE, IUGR, and GDM resulted from an over activation of the RAGE-mediated inflammatory pathway. Using human placental samples, we found that RAGE protein expression via western blotting was increased in PE and decreased in IUGR while GDM remained similar to that of control placentas. We then wanted to determine the efficacy of RAGE activation to alter the invasive nature of invasive cytotrophoblasts cells. We found that the addition of AGEs to SW71 cells decreases invasion through the activation of JNK and ERK cellular signaling pathways. Altogether these findings suggest that RAGE activation in trophoblast cells seems result in insufficient placental pathogenesis causing PE, however the IUGR and GDM samples we obtained did not seem to have resulted from RAGE activation. We also found that RAGE activation can alter the ability of invasive trophoblasts to invade, thus limiting the ability of the placental cells to remodel the maternal spiral arteries. We believe that further research into specific triggers of IUGR (smoking-induced) and un-treated diabetes could result in RAGE stimulated placental insufficiency.
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Winden, Duane Ray. "Characterization of Secondhand Smoke (SHS) and Materno-Fetal Interactions in Receptors for Advanced Glycation End-Products (RAGE)-Targeted Mice." BYU ScholarsArchive, 2014. https://scholarsarchive.byu.edu/etd/4072.

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Receptors for advanced glycation end-products (RAGE) are pattern recognition receptors of the immunoglobulin superfamily highly expressed in the lung. Likely functions include the modulation of pulmonary inflammation during disease. However, the contributions of RAGE in the developing lung in cases where secondhand smoke (SHS) exposure occurs are unknown. In order to test the hypothesis that RAGE misexpression adversely affects lung morphogenesis, we exposed gestating dams to a controlled dose of SHS during the last four critical days of in utero lung morphogenesis. We discovered that both maternal and fetal lungs respond to SHS by up-regulating RAGE. Exposed fetuses were markedly smaller compared to controls and lungs were compromised in terms of apoptotic status, collagen abundance necessary in the derivation of respiratory compartments, and the expression of MMP-9, a protease known to target extracellular matrix. Interestingly, RAGE knock out animals similarly exposed to SHS were protected, in part, from the same SHS-mediated pulmonary abnormalities. We next generated a conditional transgenic mouse that provided an opportunity to genetically augment distal lung RAGE expression in the absence of SHS exposure. Our RAGE transgenic mice (RAGE TG) were severely hypoplastic and ultrastructural analysis demonstrated weakened basement membranes in RAGE TG animals compared to controls. Specific observations in RAGE TG mice included diminished type IV collagen required for basement membrane derivation, augmented MMP-9 expression, and inhibition of pulmonary vasculature visualized by Pecam-1 staining, a marker of vascular endothelial cells. The further observation that FoxM1, a critical transcriptional regulator of endothelial cell differentiation, was inhibited in RAGE TG mice suggested a novel potential mechanism of impaired vascularization mediated by RAGE. These data provide evidence that RAGE expression must be tightly regulated during lung organogenesis. Furthermore, additional research into the nuances of RAGE signaling during development may shed needed light on the pathobiochemistry of adult lung diseases that potentially have in utero origins.
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Robinson, Adam Benjamin. "The Pro-Inflammatory Contributions of Receptors for Advanced Glycation End-Products (RAGE) in Alveolar Macrophages Following Cigarette Smoke Exposure." BYU ScholarsArchive, 2012. https://scholarsarchive.byu.edu/etd/3253.

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Receptors for advanced glycation end-products (RAGE) are multi-ligand cell surface receptors of the immunoglobin family expressed by epithelium and macrophages. RAGE expression increases following ligand binding and when diverse cells are exposed to a variety of insults including cigarette smoke extract (CSE). The current research sought to characterize the pro-inflammatory contributions of RAGE expressed by alveolar macrophages (AMs) following CSE exposure. Acute exposure of mice to CSE via nasal instillation revealed diminished bronchoalveolar lavage (BAL) cellularity and fewer AMs in RAGE null mice compared to controls. Primary AMs were obtained from BAL, exposed to CSE in vitro, and RNA, DNA, and protein were analyzed. CSE significantly increased RAGE expression by wild type AMs. Employing ELISAs, wild type AMs exposed to CSE had increased levels of active Ras, a small GTPase that perpetuates pro-inflammatory signaling. Conversely, RAGE null AMs had less Ras activation compared to wild type AMs after exposure to CSE. In RAGE null AMs, assessment of p38 MAPK and NF-κB, important intracellular signaling intermediates induced during an inflammatory response, revealed CSE-induced inflammation occurs at least in part via RAGE signaling. For example, activated p38 was diminished in RAGE null AMs compared to controls and assessment of phosphorylated NF-κB in CSE exposed RAGE null AMs suggest lessened nuclear translocation of NF-κB compared to wild type AMs exposed to CSE. Importantly, quantitative RT-PCR revealed that mRNA expression of pro-inflammatory cytokines including TNF-α and IL-1β were detectably decreased and analysis of secreted proteins by ELISA displayed diminished IL-1β in RAGE null AMs exposed to CSE compared to CSE-exposed wild type AMs. These results reveal that primary AMs orchestrate CSE-induced inflammation, at least in part, via RAGE-mediated mechanisms.
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Chen, Suzi Su-Hsin, and suzi chen@med monash edu au. "Cyclooxygenase Expression in Human Diabetes." RMIT University. Medical Sciences, 2007. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20080206.121439.

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Cyclooxygenase (COX) is the rate limiting enzyme that catalyses the production of prostanoids, which are crucial to vascular homeostasis. Evidence suggests that endothelial dysfunction and inflammation play a role in vascular complications in aging and diabetes. Previous animal studies by our laboratory at RMIT University reported enhanced COX expression with aging in rat aortas, platelets and monocytes. Potentially, alteration in COX expression may result in an imbalanced prostanoid production favoring the synthesis of vasoconstrictors and hence increase the risk of cardiovascular events in the aging population. The regulation of altered COX expression in aging, however, is not clear. It has been suggested that histone hyperacetylation may be an important mechanism that regulates COX levels during the aging process as increased histone acetylation has been shown to occur with aging. Thus, we hypothesized that COX expression is modulated by histone hyperacetylati on. This was investigated by measuring COX expression in histone hyperacetylated cultured endothelial cells. In the case of diabetes, studies have reported that the development of diabetes and its complications is associated with persistent inflammatory activity, evident with increased inflammatory markers in the circulation. COX-mediated pathways may be involved in this inflammatory process in diabetes. Furthermore, the formation of advanced glycation end products (AGEs) is accelerated in diabetes. AGEs can bind to receptors for AGEs (RAGE), which has also been suggested to play a role in inflammation in diabetes. We hypothesized that COX- and RAGE-mediated pathways contribute to increased inflammation in diabetes and potentiate the development of diabetic vascular complications. This was investigated by measuring changes in COX-mediated pathways in both rat and human diabetic models. The current thesis reports: 1) in cultured endothelial cells, histone hyperacetylation was associated with increased COX expression; 2) an overall increase in inflammation was observed in diabetes involving COX- and RAGE-mediated pathways. This was supported by increased platelet COX-1 and monocyte COX-2 levels in Zucker rats, increased monocyte COX-2 in human Type 1 diabetes and elevated plasma TXB2 and PGE2 levels in both human Type 1 and Type 2 diabetic subjects. Up-regulation of RAGE expression was further found in platelets and monocytes in both human diabetes types. When treated with NSAIDs, plasma prostanoid levels, COX and RAGE expression were reduced significantly in both platelets and monocytes in human diabetic subjects. 3) It is unclear how COX and RAGE expression was regulated, but histone modifications may be one of the mechanisms. Data from cultured cells indicated that increased COX expression was associated with increased histone acetylation levels induced by TSA. Concurrent increases in histone acetylation and COX-2 levels were also observed in human Type 1 diabetes, but similar findings were not observed in human Type 2 diabetes. In addition, we failed to find an age-dependent increase in monocyte histone H4 acetylation in human Type 2 diabetes despite an age-dependent increase in monocyte COX-2 expression. Thus, whether histone hyperacetylation modulates COX expression and in what conditions require further investigation.
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Stogsdill, Jeffrey Alan. "Characterization of Altered Epithelial Cell Turnover and Differentiation in Embryonic Murine Lungs That Over-Express Receptors for Advanced Glycation End-Products (RAGE)." BYU ScholarsArchive, 2012. https://scholarsarchive.byu.edu/etd/3217.

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Receptors for advanced glycation end-products (RAGE) are multi-ligand cell surface receptors highly expressed in the lung that modulate pulmonary inflammation during disease. However, the contributions of RAGE signaling are unknown during pulmonary organogenesis. In order to test the hypothesis that RAGE misexpression adversely affects lung morphogenesis, conditional transgenic mice were generated that over-express RAGE in alveolar type II cells of the lung. When RAGE is over-expressed throughout embryogenesis, severe lung hypoplasia ensues, culminating in perinatal lethality. Flow cytometry and immunohistochemistry employing cell-specific markers for various distal cell types demonstrated anomalies in key epithelial cell populations resulting from RAGE up-regulation through embryonic (E) 18.5. Electron microscopy also identified significant morphological disturbances to distal cell types including separation from the basement membrane. Possible mechanisms leading to the disappearance of pulmonary tissue by increased RAGE expression were then evaluated. A time course of lung organogenesis commencing at E12.5 demonstrated that increased RAGE expression primarily alters lung morphogenesis beginning at E16.5. TUNEL immunohistochemistry and immunoblotting for active caspase-3 confirm a shift toward apoptosis in lungs from RAGE over-expressing mice when compared to wild type controls. Assaying for NF-κB also revealed elevated nuclear translocation in lungs from transgenic mice compared to controls. An RT-PCR assessment of genes regulated by NF-κB demonstrated elevated expression of Fas ligand, suggesting increased activity of the Fas-mediated signal transduction pathway in which ligand-receptor interaction triggers cell death. These data provide evidence that RAGE expression must be tightly regulated during organogenesis. Furthermore, additional elucidation of RAGE signaling potentially involved in branching morphogenesis and cell cycle abnormalities may provide insight into the progression of RAGE-mediated lung diseases.
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Sirois, Cherilyn M. "Nucleic Acid Sensing by the Immune System: Roles For the Receptor For Advanced Glycation End Products (RAGE) and Intracellular Receptor Proteins: A Dissertation." eScholarship@UMMS, 2011. https://escholarship.umassmed.edu/gsbs_diss/551.

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As humans, we inhabit an environment shared with many microorganisms, some of which are harmless or beneficial, and others which represent a threat to our health. A complex network of organs, cells and their protein products form our bodies’ immune system, tasked with detecting these potentially harmful agents and eliminating them. This same system also serves to detect changes in the healthy balance of normal functions in the body, and for repairing tissue damage caused by injury. Immune recognition of nucleic acids, DNA and RNA, is one way that the body detects invading pathogens and initiates tissue repair. A number of specialized receptor proteins have evolved to distinguish nucleic acids that represent “threats” from those involved in normal physiology. These proteins include members of the Toll-like receptor family and diverse types of cytosolic proteins, all of which reside within the confines of the cell. Few proteins on the cell surface have been clearly characterized to interact with nucleic acids in the extracellular environment. In this dissertation, I present collaborative work that identifies the receptor for advanced glycation end products (RAGE) as a cell surface receptor for nucleic acids and positions it as an important modulator of immune responses. Molecular dimers of RAGE interact with the sugar-phosphate backbones of nucleic acid ligands, allowing this receptor to recognize a variety of DNA and RNA molecules regardless of their nucleotide sequence. Expression of RAGE on cells promotes uptake of DNA and enhances subsequent responses that are dependent on the nucleic acid sensor Toll-like receptor 9. When mice deficient in RAGE are exposed to DNA in the lung, the predominant site of RAGE expression, they do not mount a typical early inflammatory response, suggesting that RAGE is important in generating immune responses to DNA in mammalian organisms. Further evidence suggests that RAGE interacts preferentially with multimolecular complexes that contain nucleic acids, and that these complexes may induce clustering of receptor dimers into larger multimeric structures. Taken together, the data reported here identify RAGE as an important cell surface receptor protein for nucleic acids, which is capable of modulating the intensity of immune responses to DNA and RNA. Understanding of and intervention in this recognition pathway hold therapeutic promise for diseases characterized by excessive responses to self nucleic acids, such as systemic lupus erythematosus, and for the pathology caused by chronic inflammatory responses to self and foreign nucleic acids.
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Ren, Yimin. "Consequences of the interaction of amyloid beta with amyloid binding alcohol dehydrogenase and the receptor for advanced glycation end products." Thesis, St Andrews, 2008. http://hdl.handle.net/10023/503.

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Books on the topic "Receptors for advanced glycation end product (RAGE)"

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Kamal, Tarek. Significance of Advanced Glycation End-Products (AGE) and the Receptor for AGE (RAGE) in Diabetic Nephropathy. INTECH Open Access Publisher, 2012.

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Book chapters on the topic "Receptors for advanced glycation end product (RAGE)"

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Koyama, Hidenori, and Yoshiki Nishizawa. "Cardiovascular Complications in Renal Failure: Implications of Advanced Glycation End Products and Their Receptor RAGE." In Studies on Renal Disorders, 257–92. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-857-7_13.

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Khan, Rujman, Xin Yee Ooi, Matthew Parvus, Laura Valdez, and Andrew Tsin. "Advanced Glycation End Products: Formation, Role in Diabetic Complications, and Potential in Clinical Applications." In The Eye and Foot in Diabetes. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.89408.

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Hyperglycemic conditions and disruptions to glucose-regulating pathways lead to increased formation of highly reactive aldehydes, methylglyoxal and glyoxal, which react with certain arginine and lysine residues in proteins to form advanced glycation end products (AGEs). These AGEs damage the integrity of the retinal vasculature predominantly through two mechanisms: non-receptor-mediated damage, which pertains to the interaction with extracellular matrix and its functional properties, and receptor-mediated damage through AGE interactions with their receptors (RAGE) on pericytes and Muller cells. Damage occurring between AGE and RAGE potentially generates reactive oxygen species, inflammatory cytokines, and growth factors. Both mechanisms result in increased permeability of endothelial tight junctions, and this increased permeability can lead to leaking and eventually ischemia. Once this ischemia becomes significant, neovascularization can occur, the hallmark of proliferative diabetic retinopathy. Current pharmaceutical studies have shown the potential of AGE inhibitors, such as aminoguanidine, in decreasing AGE production, thus minimizing its effects in hyperglycemic conditions. Other pharmaceutical interventions, such as Tanshinone IIA, aim to protect cells from the impacts of AGEs. Future research will not only continue to understand the properties of AGEs and their effects on diabetes and diabetic complications like diabetic retinopathy but will also explore how they impact other diseases.
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Kamal, Tarek, Yasuhiko Yamamoto, and Hiroshi Yamamoto. "Significance of Advanced Glycation End-Products (AGE) and the Receptor for AGE (RAGE) in Diabetic Nephropathy." In Diabetic Nephropathy. InTech, 2012. http://dx.doi.org/10.5772/34643.

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Fernando, Dinali H., Josephine M. Forbes, Peter W. Angus, and Chandana B. Herath. "The Receptor for Advanced Glycation End Products (RAGE): A Potential Target for Therapeutic Intervention in the Progression of Non-Alcoholic Fatty Liver Disease (NAFLD)." In Prime Archives in Molecular Biology. Vide Leaf, Hyderabad, 2020. http://dx.doi.org/10.37247/pamb.1.2020.25.

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Conference papers on the topic "Receptors for advanced glycation end product (RAGE)"

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Zhang, W., Y. Wu, and S. J. Gunst. "S100A4 Regulates Airway Smooth Muscle (ASM) Inflammation by Acting on Receptors for Advanced Glycation End Products (RAGE)." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a2848.

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Wolf, Lisa, Julia Niederstraßer, Herr Christian, and Bals Robert. "Receptor for advanced glycation end products (RAGE) is involved in cigarette smoke induced inflammation and emphysema." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa5048.

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Thompson, Ben, Alan Stitt, Cecilia O'Kane, and Danny McAuley. "Receptor For Advanced Glycation End Products (RAGE) Ligands Induce Pulmonary Endothelial And Epithelial Cell NF-?B Activation." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5774.

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D'Souza, VK, CR Bassford, D. Park, F. Gao, DR Thickett, and GD Perkins. "The Receptor for Advanced Glycation End Products (RAGE) Is a Marker of Alveolar Epithelial Damage in ARDS." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a3559.

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AI, Cabrera-García, M. Protschka, G. Alber, S. Kather, F. Dengler, U. Müller, JM Steiner, and RM Heilmann. "Dysregulation of gastrointestinal RAGE (receptor for advanced glycation end products) expression in dogs with inflammatory bowel disease." In 29. Jahrestagung der FG „Innere Medizin und klinische Labordiagnostik“ der DVG (InnLab) – Teil 2: Poster. Georg Thieme Verlag KG, 2021. http://dx.doi.org/10.1055/s-0041-1723879.

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Taniguchi, Akihiko, Nobuaki Miyahara, Arihiko Kanehiro, Koichi Waseda, Etsuko Kurimoto, Yasushi Tanimoto, Mikio Kataoka, et al. "Contrasting Roles For The Receptor For Advanced Glycation End-Products (RAGE) In Allergic Airway Inflammation Versus Airway Hyperresponsiveness." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a4288.

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SHARMA, ASHISH K., Damien LaPar, Lucas Fernandez, and Victor Laubach. "Receptor For Advanced Glycation End Products (RAGE) And High Mobility Group Box 1 (HMGB1) Mediate Pulmonary Ischemia-Reperfusion Injury." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5292.

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Bjerregaard, Asger, Celeste Porsbjerg, Lucy Barrett, Ingrid Laing, Siew-Kim Khoo, Markus Fally, Peter Le Souëf, Vibeke Backer, Philip Thompson, and Svetlana Baltic. "Signalling through the receptor for advanced glycation end products (RAGE) is increased in acute asthma and correlates with symptom severity." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa904.

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Retnaningtyas, Ekowati, Budi Susatia, Olly Indrajani, Verina Setyabudhi, and Hendry Santoso. "Hydrogen-rich water supplementation declines advanced glycation-end products (AGE) and receptor for AGE (RAGE) in streptozotocin-induced diabetic rats." In INTERNATIONAL CONFERENCE ON LIFE SCIENCES AND TECHNOLOGY (ICoLiST 2020). AIP Publishing, 2021. http://dx.doi.org/10.1063/5.0052797.

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Reynolds, PR, RE Schmitt, SD Kasteler, and JR Hoidal. "The Receptor for Advanced Glycation End Products (RAGE) Activates Ras and NFκ-β in Pulmonary Epithelial Cells Exposed to Cigarette Smoke." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a4185.

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Reports on the topic "Receptors for advanced glycation end product (RAGE)"

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Ganju, Ramesh K. Receptor for Advanced Glycation End Products (RAGE) as a Novel Target for Inhibiting Breast Cancer Bone Metastasis. Fort Belvoir, VA: Defense Technical Information Center, April 2013. http://dx.doi.org/10.21236/ada592353.

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