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Journal articles on the topic 'Receptor for advanced glycation endproduct'

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Published: 9 March 2023
Last updated: 10 March 2023

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1

Yamagishi, Sho-ichi. "Role of Advanced Glycation Endproduct (AGE)-Receptor for Advanced Glycation Endproduct (RAGE) Axis in Cardiovascular Disease and Its Therapeutic Intervention." Circulation Journal 83, no. 9 (August 23, 2019): 1822–28. http://dx.doi.org/10.1253/circj.cj-19-0618.

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2

Gaens, Katrien HJ, Coen DA Stehouwer, and Casper G. Schalkwijk. "Advanced glycation endproducts and its receptor for advanced glycation endproducts in obesity." Current Opinion in Lipidology 24, no. 1 (February 2013): 4–11. http://dx.doi.org/10.1097/mol.0b013e32835aea13.

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3

McFarlane, S. "Characterisation of the advanced glycation endproduct receptor complex in the retinal pigment epithelium." British Journal of Ophthalmology 89, no. 1 (January 1, 2005): 107–12. http://dx.doi.org/10.1136/bjo.2004.045914.

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4

Walker, Douglas, Lih Fen Lue, Gaurav Paul, Amar Patel, and Marwan N. Sabbagh. "Receptor for advanced glycation endproduct modulators: a new therapeutic target in Alzheimer’s disease." Expert Opinion on Investigational Drugs 24, no. 3 (January 14, 2015): 393–99. http://dx.doi.org/10.1517/13543784.2015.1001490.

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5

Haslbeck, Karl-Matthias, Angelika Bierhaus, Schliecher Erwin, Annette Kirchner, Peter Nawroth, Ursula Schlötzer, Bernhard Neundörfer, and Dieter Heuss. "Receptor for advanced glycation endproduct (RAGE)-mediated nuclear factor-κB activation in vasculitic neuropathy." Muscle & Nerve 29, no. 6 (April 12, 2004): 853–60. http://dx.doi.org/10.1002/mus.20039.

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6

Leclerc, Estelle, Emmanuel Sturchler, and Stefan W. Vetter. "The S100B/RAGE Axis in Alzheimer's Disease." Cardiovascular Psychiatry and Neurology 2010 (June 21, 2010): 1–11. http://dx.doi.org/10.1155/2010/539581.

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Increasing evidence suggests that the small EF-hand calcium-binding protein S100B plays an important role in Alzheimer's disease. Among other evidences are the increased levels of both S100B and its receptor, the Receptor for Advanced Glycation Endproducts (RAGEs) in the AD diseased brain. The regulation of RAGE signaling by S100B is complex and probably involves other ligands including the amyloid beta peptide (A), the Advanced Glycation Endproducts (AGEs), or transtheyretin. In this paper we discuss the current literature regarding the role of S100B/RAGE activation in Alzheimer's disease.
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7

Frank, Franziska, Veronika Bezold, Kaya Bork, Philip Rosenstock, Jonas Scheffler, and Rüdiger Horstkorte. "Advanced glycation endproducts and polysialylation affect the turnover of the neural cell adhesion molecule (NCAM) and the receptor for advanced glycation endproducts (RAGE)." Biological Chemistry 400, no. 2 (January 28, 2019): 219–26. http://dx.doi.org/10.1515/hsz-2018-0291.

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Abstract The balance between protein synthesis and degradation regulates the amount of expressed proteins. This protein turnover is usually quantified as the protein half-life time. Several studies suggest that protein degradation decreases with age and leads to increased deposits of damaged and non-functional proteins. Glycation is an age-dependent, non-enzymatic process leading to posttranslational modifications, so-called advanced glycation endproducts (AGE), which usually damage proteins and lead to protein aggregation. AGE are formed by the Maillard reaction, where carbonyls of carbohydrates or metabolites react with amino groups of proteins. In this study, we quantified the half-life time of two important receptors of the immunoglobulin superfamily, the neural cell adhesion molecule (NCAM) and the receptor for advanced glycation end products (RAGE) before and after glycation. We found, that in two rat PC12 cell lines glycation leads to increased turnover, meaning that glycated, AGE-modified proteins are degraded faster than non-glycated proteins. NCAM is the most prominent carrier of a unique enzymatic posttranslational modification, the polysialylation. Using two PC12 cell lines (a non-polysialylated and a polysialylated one), we could additionally demonstrate, that polysialylation of NCAM has an impact on its turnover and that it significantly increases its half-life time.
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8

Fukami, Kei, Kensei Taguchi, Sho-ichi Yamagishi, and Seiya Okuda. "Receptor for advanced glycation endproducts and progressive kidney disease." Current Opinion in Nephrology and Hypertension 24, no. 1 (January 2015): 54–60. http://dx.doi.org/10.1097/mnh.0000000000000091.

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9

Got'e, S. V. "TYPE 1 DIABETES MELLITUS, DIABETIC NEPHROPATHY: TRANSPLANTOLOGY POTENTIAL." Annals of the Russian academy of medical sciences 67, no. 1 (January 22, 2012): 54–60. http://dx.doi.org/10.15690/vramn.v67i1.111.

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The review covers the role of transplantology in treatment of patients with type 1 diabetes and the state of its development in the world and in Russia. The results of major multicenter studies, devoted to the influence of simultaneous kidney and pancreas transplantation and kidney transplantation alone on life expectancy and quality of life of diabetic patients are summarized here. Experience in pancreas-kidney transplantation, gained in Academician V.I. Shumakov Federal Research Center of Transplantology and Artificial Organs, is described, including surgical technical and postoperative treatment. Also we perform the results of research work, devoted to the influence of pancreas transplantation on different homeostasis parameters, such as: oxidative stress parameters, homocysteine, receptor for advanced glycation endproduct (RAGE), and markers of endocrine function of pancreas transplant.
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10

Yue, S., H. M. Zhou, J. J. Zhu, J. H. Rao, R. W. Busuttil, J. W. Kupiec-Weglinski, L. Lu, and Y. Zhai. "Hyperglycemia and Liver Ischemia Reperfusion Injury: A Role for the Advanced Glycation Endproduct and Its Receptor Pathway." American Journal of Transplantation 15, no. 11 (June 25, 2015): 2877–87. http://dx.doi.org/10.1111/ajt.13360.

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11

Zhao, Dongdong, Yong Wang, and Yawei Xu. "Decreased serum endogenous secretory receptor for advanced glycation endproducts and increased cleaved receptor for advanced glycation endproducts levels in patients with atrial fibrillation." International Journal of Cardiology 158, no. 3 (July 2012): 471–72. http://dx.doi.org/10.1016/j.ijcard.2012.05.042.

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12

Srikanth, Velandai, Annette Maczurek, Thanh Phan, Megan Steele, Bernadette Westcott, Damian Juskiw, and Gerald Münch. "Advanced glycation endproducts and their receptor RAGE in Alzheimer's disease." Neurobiology of Aging 32, no. 5 (May 2011): 763–77. http://dx.doi.org/10.1016/j.neurobiolaging.2009.04.016.

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13

Ohgami, Nobutaka, Ryoji Nagai, Mamoru Ikemoto, Hiroyuki Arai, Akira Miyazaki, Hideki Hakamata, Seikoh Horiuchi, and Hitoshi Nakayama. "CD36, serves as a receptor for advanced glycation endproducts (AGE)." Journal of Diabetes and its Complications 16, no. 1 (January 2002): 56–59. http://dx.doi.org/10.1016/s1056-8727(01)00208-2.

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14

Juranek, Judyta K., Alexey Aleshin, Eileen M. Rattigan, Lynne Johnson, Wu Qu, Fei Song, Radha Ananthakrishnan, et al. "Morphological Changes and Immunohistochemical Expression of RAGE and its Ligands in the Sciatic Nerve of Hyperglycemic Pig (Sus Scrofa)." Biochemistry Insights 3 (January 2010): BCI.S5340. http://dx.doi.org/10.4137/bci.s5340.

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The aim of our project was to study the effect of streptozotocin (STZ)–-induced hyperglycemia on sciatic nerve morphology, blood plasma markers and immunohistochemical expression of RAGE (the Receptor for Advanced Glycation End-products), and its ligands–-S100B and Carboxymethyl Lysine (CML)-advanced glycation endproduct (AGE) in the laboratory pig. Six months after STZ–-injections, blood plasma measurements, morphometric analysis of sciatic nerve fiber density, immunofluorescent distribution of potential molecular neuropathy contributors, ELISA measurement of plasma AGE level and HPLC analysis of sciatic nerve levels of one of the pre-AGE and the glycolysis intermediate products–-methylglyoxal (MG) were performed. The results of our study revealed that STZ–-injected animals displayed elevated levels of plasma glucose, gamma glutamyl transferase (GGT) and triglycerides. The sciatic nerve of STZ-injected pigs revealed significantly lower numbers of small-diameter myelinated fibers, higher immunoreactivity for RAGE and S100B and increased levels of MG as compared to control animals. Our results correspond to clinical findings in human patients with hyperglycemia/diabetes-evoked peripheral neuropathy and suggest that the domestic pig may be a suitable large animal model for the study of mechanisms underlying hyperglycemia-induced neurological complications in the peripheral nerve and may serve as a relevant model for the pre-clinical assessment of candidate drugs in neuropathy.
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15

Ma, Heng, Shi-Yan Li, Peisheng Xu, Sara A. Babcock, E. Kurt Dolence, Michael Brownlee, Ji Li, and Jun Ren. "Advanced glycation endproduct (AGE) accumulation and AGE receptor (RAGE) up-regulation contribute to the onset of diabetic cardiomyopathy." Journal of Cellular and Molecular Medicine 13, no. 8b (October 13, 2008): 1751–64. http://dx.doi.org/10.1111/j.1582-4934.2008.00547.x.

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16

van der Lugt, Timme, Antje R. Weseler, Misha F. Vrolijk, Antoon Opperhuizen, and Aalt Bast. "Dietary Advanced Glycation Endproducts Decrease Glucocorticoid Sensitivity In Vitro." Nutrients 12, no. 2 (February 10, 2020): 441. http://dx.doi.org/10.3390/nu12020441.

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Glucocorticoids are very effective anti-inflammatory drugs and widely used for inflammatory bowel disease (IBD) patients. However, approximately 20% of IBD patients do not respond to glucocorticoids and the reason for this is largely unknown. Dietary advanced glycation endproducts (AGEs) are formed via the Maillard reaction during the thermal processing of food products and can induce a pro-inflammatory reaction in human cells. To investigate whether this pro-inflammatory response could be mitigated by glucocorticoids, human macrophage-like cells were exposed to both LPS and AGEs to induce interleukin-8 (IL8) secretion. This pro-inflammatory response was then modulated by adding pharmacological compounds interfering in different steps of the anti-inflammatory mechanism of glucocorticoids: rapamycin, quercetin, and theophylline. Additionally, intracellular reactive oxygen species (ROS) were measured and the glucocorticoid receptor phosphorylation state was assessed. The results show that AGEs induced glucocorticoid resistance, which could be mitigated by quercetin and rapamycin. No change in the phosphorylation state of the glucocorticoid receptor was observed. Additionally, intracellular ROS formation was induced by AGEs, which was mitigated by quercetin. This suggests that AGE-induced ROS is an underlying mechanism to AGE-induced glucocorticoid resistance. This study shows for the first time the phenomenon of dietary AGE-induced glucocorticoid resistance due to the formation of ROS. Our findings indicate that food products with a high inflammatory potential can induce glucocorticoid resistance; these results may be of great importance to IBD patients suffering from glucocorticoid resistance.
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17

Snelson, Matthew, Elisa Lucut, and Melinda T. Coughlan. "The Role of AGE-RAGE Signalling as a Modulator of Gut Permeability in Diabetes." International Journal of Molecular Sciences 23, no. 3 (February 3, 2022): 1766. http://dx.doi.org/10.3390/ijms23031766.

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There is increasing evidence for the role of intestinal permeability as a contributing factor in the pathogenesis of diabetes; however, the molecular mechanisms are poorly understood. Advanced glycation endproducts, of both exogenous and endogenous origin, have been shown to play a role in diabetes pathophysiology, in part by their ligation to the receptor for advanced glycation endproducts (RAGE), leading to a proinflammatory signalling cascade. RAGE signalling has been demonstrated to play a role in the development of intestinal inflammation and permeability in Crohn’s disease and ulcerative colitis. In this review, we explore the role of AGE-RAGE signalling and intestinal permeability and explore whether activation of RAGE on the intestinal epithelium may be a downstream event contributing to the pathogenesis of diabetes complications.
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18

Simon, Frieder, Kaya Bork, Vinayaga S. Gnanapragassam, Tim Baldensperger, Marcus A. Glomb, Simone Di Sanzo, Alessandro Ori, and Rüdiger Horstkorte. "Increased Expression of Immature Mannose-Containing Glycoproteins and Sialic Acid in Aged Mouse Brains." International Journal of Molecular Sciences 20, no. 24 (December 4, 2019): 6118. http://dx.doi.org/10.3390/ijms20246118.

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Aging represents the accumulation of changes in an individual over time, encompassing physical, psychological, and social changes. Posttranslational modifications of proteins such as glycosylation, including sialylation or glycation, are proposed to be involved in this process, since they modulate a variety of molecular and cellular functions. In this study, we analyzed selected posttranslational modifications and the respective proteins on which they occur in young and old mouse brains. The expression of neural cell adhesion molecule (NCAM), receptor for advanced glycation endproducts (RAGE), as well as the carbohydrate-epitopes paucimannose and high-mannose, polysialic acid, and O-GlcNAc were examined. We demonstrated that mannose-containing glycans increased on glycoproteins in aged mouse brains and identified synapsin-1 as one major carrier of paucimannose in aged brains. In addition, we found an accumulation of so-called advanced glycation endproducts, which are generated by non-enzymatic reactions and interfere with protein function. Furthermore, we analyzed the expression of sialic acid and found also an increase during aging.
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19

Pertyńska-Marczewska, Magdalena, Ewa Głowacka, Małgorzata Sobczak, Katarzyna Cypryk, and Jan Wilczyński. "ORIGINAL ARTICLE: Glycation Endproducts, Soluble Receptor for Advanced Glycation Endproducts and Cytokines in Diabetic and Non-diabetic Pregnancies." American Journal of Reproductive Immunology 61, no. 2 (January 11, 2009): 175–82. http://dx.doi.org/10.1111/j.1600-0897.2008.00679.x.

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20

Abo-Elezz, AhmedA, SamirM Hasan, ShimaaA Mashaly, MohamedA Saad, and MaalyM Mabrouk. "Receptor for advanced glycation endproducts in pediatric sepsis: a pilot study." Tanta Medical Journal 44, no. 4 (2016): 135. http://dx.doi.org/10.4103/1110-1415.201722.

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21

Zen, Ke, Celia X. J. Chen, Yi-Tien Chen, Rosemarie Wilton, and Yuan Liu. "Receptor for Advanced Glycation Endproducts Mediates Neutrophil Migration across Intestinal Epithelium." Journal of Immunology 178, no. 4 (February 2, 2007): 2483–90. http://dx.doi.org/10.4049/jimmunol.178.4.2483.

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22

Lue, L., S. Yan, D. Stern, and D. Walker. "Preventing Activation of Receptor for Advanced Glycation Endproducts in Alzheimers Disease." Current Drug Target -CNS & Neurological Disorders 4, no. 3 (June 1, 2005): 249–66. http://dx.doi.org/10.2174/1568007054038210.

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23

Reed, James C., Paula Preston-Hurlburt, William Philbrick, Gabriel Betancur, Maria Korah, Carrie Lucas, and Kevan C. Herold. "The receptor for advanced glycation endproducts (RAGE) modulates T cell signaling." PLOS ONE 15, no. 9 (September 28, 2020): e0236921. http://dx.doi.org/10.1371/journal.pone.0236921.

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24

van Zoelen, Marieke AD, Ahmed Achouiti, and Tom van der Poll. "The role of receptor for advanced glycation endproducts (RAGE) in infection." Critical Care 15, no. 2 (2011): 208. http://dx.doi.org/10.1186/cc9990.

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25

Teismann, Peter, Kinnari Sathe, Angelika Bierhaus, Lin Leng, Heather L. Martin, Richard Bucala, Bernd Weigle, Peter P. Nawroth, and Jörg B. Schulz. "Receptor for advanced glycation endproducts (RAGE) deficiency protects against MPTP toxicity." Neurobiology of Aging 33, no. 10 (October 2012): 2478–90. http://dx.doi.org/10.1016/j.neurobiolaging.2011.12.006.

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26

STERN, D., S. YAN, S. YAN, and A. SCHMIDT. "Receptor for advanced glycation endproducts (RAGE) and the complications of diabetes." Ageing Research Reviews 1, no. 1 (February 2002): 1–15. http://dx.doi.org/10.1016/s0047-6374(01)00366-9.

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27

Fasshauer, Mathias, Jeannette Seeger, Theresa Waldeyer, Susanne Schrey, Thomas Ebert, Ulrike Lossner, Matthias Bluher, Michael Stumvoll, Renaldo Faber, and Holger Stepan. "Endogenous soluble receptor for advanced glycation endproducts is increased in preeclampsia." Journal of Hypertension 26, no. 9 (September 2008): 1824–28. http://dx.doi.org/10.1097/hjh.0b013e3283060c5c.

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28

Huang, Emina H. "Receptor for Advanced Glycation Endproducts and Murine ColitisLimited Project Grant #066." Seminars in Colon and Rectal Surgery 17, no. 4 (December 2006): 160–64. http://dx.doi.org/10.1053/j.scrs.2006.10.001.

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29

Saleh, Mgs Irsan, Nita Parisa, and Ziske Maritska. "The Development of Prototype Polyclonal Antibody of Receptor Advanced Glycation of Endproducts (RAGE)." Bioscientia Medicina : Journal of Biomedicine and Translational Research 2, no. 1 (January 13, 2018): 34–40. http://dx.doi.org/10.32539/bsm.v2i1.16.

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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
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30

Lu, C., J. C. He, W. Cai, H. Liu, L. Zhu, and H. Vlassara. "Advanced glycation endproduct (AGE) receptor 1 is a negative regulator of the inflammatory response to AGE in mesangial cells." Proceedings of the National Academy of Sciences 101, no. 32 (August 2, 2004): 11767–72. http://dx.doi.org/10.1073/pnas.0401588101.

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31

Akasaka, Naruse, Sado, Uchiyama, Makino, Yamauchi, Ota, et al. "Involvement of Receptor for Advanced Glycation Endproducts in Hypertensive Disorders of Pregnancy." International Journal of Molecular Sciences 20, no. 21 (November 1, 2019): 5462. http://dx.doi.org/10.3390/ijms20215462.

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Preeclampsia/hypertensive disorders of pregnancy (PE/HDP) is a serious and potentially life-threatening disease. Recently, PE/HDP has been considered to cause adipose tissue inflammation, but the detailed mechanism remains unknown. We exposed human primary cultured adipocytes with serum from PE/HDP and healthy controls for 24 h, and analyzed mRNA expression of several adipokines, cytokines, and ligands of the receptor for advanced glycation endproducts (RAGE). We found that the mRNA levels of interleukin-6 (IL-6), C-C motif chemokine ligand 2 (CCL2), high mobility group box 1 (HMGB1), and RAGE were significantly increased by the addition of PE/HDP serum. Among RAGE ligands, advanced glycation endproducts (AGE) and HMGB1 increased mRNA levels of IL-6 and CCL2 in SW872 human adipocytes and mouse 3T3-L1 cells. The introduction of small interfering RNA for RAGE (siRAGE) into SW872 cells abolished the AGE- and HMGB1-induced up-regulation of IL-6 and CCL2. In addition, lipopolysaccharide (LPS), a ligand of RAGE, increased the expression of IL-6 and CCL2 and siRAGE attenuated the LPS-induced expression of IL-6 and CCL2. These results strongly suggest that the elevated AGE, HMGB1, and LPS in pregnant women up-regulate the expression of IL-6 and CCL2 via the RAGE system, leading to systemic inflammation such as PE/HDP.
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Zhu, Hong, Jin Yu, Zhen Liu, and Mark S. Kindy. "P1-421: The role of advanced glycation endproduct (AGE) receptors in the pathogenesis of Alzheimer's disease." Alzheimer's & Dementia 4 (July 2008): T343. http://dx.doi.org/10.1016/j.jalz.2008.05.1003.

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33

Degryse, Bernard, Tiziana Bonaldi, Paola Scaffidi, Susanne Müller, Massimo Resnati, Francesca Sanvito, Gianluigi Arrigoni, and Marco E. Bianchi. "The High Mobility Group (Hmg) Boxes of the Nuclear Protein Hmg1 Induce Chemotaxis and Cytoskeleton Reorganization in Rat Smooth Muscle Cells." Journal of Cell Biology 152, no. 6 (March 19, 2001): 1197–206. http://dx.doi.org/10.1083/jcb.152.6.1197.

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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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Bongarzone, Salvatore, Vilius Savickas, Federico Luzi, and Antony D. Gee. "Targeting the Receptor for Advanced Glycation Endproducts (RAGE): A Medicinal Chemistry Perspective." Journal of Medicinal Chemistry 60, no. 17 (May 19, 2017): 7213–32. http://dx.doi.org/10.1021/acs.jmedchem.7b00058.

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35

Navarra, T., P. De Simone, S. Del Turco, A. Gastaldelli, F. Filipponi, and G. Basta. "215 THE RECEPTOR FOR ADVANCED GLYCATION ENDPRODUCTS (RAGE) AXIS IN LIVER TRANSPLANTATION." Journal of Hepatology 56 (April 2012): S91. http://dx.doi.org/10.1016/s0168-8278(12)60228-1.

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Drake, Lindsey R., Allen F. Brooks, Jenelle Stauff, Phillip S. Sherman, Janna Arteaga, Robert A. Koeppe, Aimee Reed, Timothy J. Montavon, Marc B. Skaddan, and Peter J. H. Scott. "Strategies for PET imaging of the receptor for advanced glycation endproducts (RAGE)." Journal of Pharmaceutical Analysis 10, no. 5 (October 2020): 452–65. http://dx.doi.org/10.1016/j.jpha.2020.07.009.

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Chen, Jianfei, Minbao Song, Shiyong Yu, Pan Gao, Yang Yu, Hong Wang, and Lan Huang. "Advanced glycation endproducts alter functions and promote apoptosis in endothelial progenitor cells through receptor for advanced glycation endproducts mediate overpression of cell oxidant stress." Molecular and Cellular Biochemistry 335, no. 1-2 (September 15, 2009): 137–46. http://dx.doi.org/10.1007/s11010-009-0250-y.

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McCarthy, A. D., S. B. Etcheverry, and A. M. Cortizo. "Advanced glycation endproduct-specific receptors in rat and mouse osteoblast-like cells: regulation with stages of differentiation." Acta Diabetologica 36, no. 1-2 (July 1, 1999): 45–52. http://dx.doi.org/10.1007/s005920050144.

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Yamada, Yuko, Kazuko Ishibashi, Kazuki Ishibashi, Imran A. Bhutto, Jane Tian, Gerard A. Lutty, and James T. Handa. "The expression of advanced glycation endproduct receptors in rpe cells associated with basal deposits in human maculas." Experimental Eye Research 82, no. 5 (May 2006): 840–48. http://dx.doi.org/10.1016/j.exer.2005.10.005.

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Stern, David, Shi Du Yan, Shi Fang Yan, and Ann Marie Schmidt. "Receptor for advanced glycation endproducts: a multiligand receptor magnifying cell stress in diverse pathologic settings." Advanced Drug Delivery Reviews 54, no. 12 (December 2002): 1615–25. http://dx.doi.org/10.1016/s0169-409x(02)00160-6.

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Babkina, I. V., I. S. Chernomaz, E. S. Gershtein, I. N. Kuznetsov, N. A. Ognerubov, I. V. Bulycheva, Y. N. Solovyev, and N. E. Kushlinskii. "Content of receptor for advanced glycation endproduct (RAGE) and matrix metalloproteinase of 2 type in blood serum of bone tumor patients." Tambov University Reports. Series: Natural and Technical Sciences 22, no. 2 (2017): 283–88. http://dx.doi.org/10.20310/1810-0198-2017-22-2-283-288.

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42

Barbezier, Nicolas, Frédéric J. Tessier, and Abalo Chango. "Receptor of advanced glycation endproducts RAGE/AGER: an integrative view for clinical applications." Annales de biologie clinique 72, no. 6 (November 2014): 669–80. http://dx.doi.org/10.1684/abc.2014.1010.

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Yonekura, Hideto, Yasuhiko Yamamoto, Shigeru Sakurai, Takuo Watanabe, and Hiroshi Yamamoto. "Roles of the Receptor for Advanced Glycation Endproducts in Diabetes-Induced Vascular Injury." Journal of Pharmacological Sciences 97, no. 3 (2005): 305–11. http://dx.doi.org/10.1254/jphs.cpj04005x.

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Park, Lisa, Kathleen G. Raman, Kenneth J. Lee, Yan Lu, Luis J. Ferran, Wing Sun Chow, David Stern, and Ann Marie Schmidt. "Suppression of accelerated diabetic atherosclerosis by the soluble receptor for advanced glycation endproducts." Nature Medicine 4, no. 9 (September 1998): 1025–31. http://dx.doi.org/10.1038/2012.

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Hudson, Barry I., Evis Harja, Bernhard Moser, and Ann Marie Schmidt. "Soluble Levels of Receptor for Advanced Glycation Endproducts (sRAGE) and Coronary Artery Disease." Arteriosclerosis, Thrombosis, and Vascular Biology 25, no. 5 (May 2005): 879–82. http://dx.doi.org/10.1161/01.atv.0000164804.05324.8b.

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Basta, Giuseppina. "Receptor for advanced glycation endproducts and atherosclerosis: From basic mechanisms to clinical implications." Atherosclerosis 196, no. 1 (January 2008): 9–21. http://dx.doi.org/10.1016/j.atherosclerosis.2007.07.025.

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Meijer, Berrie, Teagan Hoskin, Anna Ashcroft, Laura Burgess, Jacqueline I. Keenan, James Falvey, Richard B. Gearry, and Andrew S. Day. "Total soluble and endogenous secretory receptor for advanced glycation endproducts (RAGE) in IBD." Journal of Crohn's and Colitis 8, no. 6 (June 2014): 513–20. http://dx.doi.org/10.1016/j.crohns.2013.11.004.

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Zhu, Yunxia, Tingting Shu, Yan Lin, Hongdong Wang, Junwei Yang, Yuguang Shi, and Xiao Han. "Inhibition of the receptor for advanced glycation endproducts (RAGE) protects pancreatic β-cells." Biochemical and Biophysical Research Communications 404, no. 1 (January 2011): 159–65. http://dx.doi.org/10.1016/j.bbrc.2010.11.085.

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Ramasamy, Ravichandran, Shi Fang Yan, and Ann Marie Schmidt. "Arguing for the motion: Yes, RAGE is a receptor for advanced glycation endproducts." Molecular Nutrition & Food Research 51, no. 9 (September 2007): 1111–15. http://dx.doi.org/10.1002/mnfr.200700008.

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Watanabe, Haruki, and Myoungsun Son. "The Immune Tolerance Role of the HMGB1-RAGE Axis." Cells 10, no. 3 (March 5, 2021): 564. http://dx.doi.org/10.3390/cells10030564.

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Abstract:
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.
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