Dissertations / Theses on the topic 'Receptor for advanced glycation endproduct'
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Metz, Verena Vanessa [Verfasser]. "Untersuchungen zum Ectodomain shedding des Receptor for advanced glycation endproducts / Verena Vanessa Metz." Mainz : Universitätsbibliothek Mainz, 2012. http://d-nb.info/1024307662/34.
Full textBurke, George A. "The characterisation of the receptor for advanced glycation endproducts (AGEs)in the retinal microvasculature." Thesis, Queen's University Belfast, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.301774.
Full textMOL, MARCO HENDRIKUS ADRIANUS. "Analytical Strategies for the Identification and Characterization of RAGE Binders of Proinflammatory mediators. AGEs and ALES." Doctoral thesis, Università degli Studi di Milano, 2019. http://hdl.handle.net/2434/675044.
Full textUhle, Florian [Verfasser]. "Der Receptor for Advanced Glycation Endproducts (RAGE) und seine Liganden in der systemischen Entzündungsreaktion nach Polytrauma / Florian Uhle." Gießen : Universitätsbibliothek, 2015. http://d-nb.info/1068874724/34.
Full textCecil, Denise L. "The receptor for advanced glycation endproducts and S100A11 modulate pathologic chondrocyte differentiation and dysregulated cartilage matrix catabolism in osteoarthritis." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2008. http://wwwlib.umi.com/cr/ucsd/fullcit?p3315413.
Full textTitle from first page of PDF file (viewed September 3, 2008). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references (p. 104-126).
Jung, Annelie [Verfasser]. "Peroxisome proliferator activated receptor gamma-aktivierende Glitazone vermindern die Ansprechbarkeit humaner Endothelzellen auf proinflammatorische Advanced glycation endproducts-Effekte / Annelie Jung." Ulm : Universität Ulm. Medizinische Fakultät, 2004. http://d-nb.info/1015899420/34.
Full textHoppmann, Susan. "18F-markierte S100-Proteine als potentielle Radioliganden für die funktionelle Charakterisierung des Rezeptors für advanced glycation endproducts (RAGE) in vitro und in vivo." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2009. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-24725.
Full textMembers of the S100 family of EF-hand calcium binding proteins play important regulatory roles not only within cells but also exert effects in a cytokine-like manner on definite target cells once released into extracellular space or circulating blood. Accordingly, increased levels of S100 proteins in the circulating blood have been associated with a number of disease states, e.g., diabetes, cancer, and various inflammatory disorders. As the best known target protein of extracellular S100 proteins, the receptor for advanced glycation endproducts (RAGE) is of significant importance. However, the role of extracellular S100 proteins during etiology, progression, and manifestation of inflammatory disorders still is poorly understood. One reason for this is the shortage of sensitive methods for direct assessment of the metabolic fate of circulating S100 proteins and, on the other hand, measurement of functional expression of extracellular targets of S100 proteins, e.g., RAGE in vivo. In this line, small animal PET provides a valuable tool for noninvasive imaging of physiological processes and interactions like plasma or vascular retention, tissue-specific receptor binding, accumulation or elimination in vivo. To address this question, human S100 proteins were cloned in the bacterial expression vector pGEX-6P-1, expressed in E. coli BL21, and purified by affinity chromatography and anion exchange chromatography. Purified S100A1, S100B and S100A12 proteins were then radiolabeled with the positron emitter fluorine-18 (18F) by N-succinimidyl-4-[18F]fluorobenzoate ([18F]SFB). Radiolabeling of S100 proteins resulted in radiochemical yields of 3-10% (corrected for decay) and effective specific radioactivities of 1 GBq/µmol, respectively. For investigations about RAGE binding soluble RAGE (sRAGE) was expressed and purified using pSecTag2B. A radioligand binding assay confirmed specific binding of 18F-S100A12, 18F-S100A1, and 18F-S100B to immobilized sRAGE, also showing an order of affinity with S100A12 > S100A1 > S100B. These results indicate that radioactive labelling of S100 proteins did not affect their overall affinity to RAGE. Cellular association studies in human THP-1 macrophages and human aortic endothelial cells (HAEC) showed specific binding of all 18F-S100 proteins to the non-internalizing RAGE as confirmed by inhibitory effects exerted either by other RAGE ligands, e.g., glycated LDL, or by soluble RAGE. Of interest, 18F-S100 proteins were also shown to interact with other putative binding sites, e.g. scavenger receptors as well as proteoglycans. In this line, uptake of 18F-S100 proteins in THP-1 and HAEC could be inhibited by various scavenger receptor ligands, in particular by maleylated BSA as well as by lectines (e.g. ConA and SBA). Confocal laser scanning microscopy analysis showed a major part of the fluoresceinated S100A12 bound to the surface of THP-1 macrophages. Beyond this, uptake of S100A12 could be determined indicating an interaction of S100A12 with both non-internalizing, e.g., RAGE, and internalizing receptors, e.g. scavenger receptors. By evaluation of the relative contribution of 18F-S100A12 association to RAGE-overexpressed CHO cells (using pIres2-AcGFP1), 18F-S100A12 showed a significantly higher association to CHO-RAGE cells compared with CHO-mock cells. Based on these findings and due to their crucial role in inflammatory disorders the metabolic fate of S100 proteins was further investigated in dynamic small animal Positron emission tomography (PET) studies as well as in biodistribution studies in Wistar rats in vivo. For interpretation of in vivo investigations in rats, expression of RAGE was analyzed by quantitative real time RT-PCR as well as western blotting in various organs. Lung tissue expressed the highest level of RAGE protein compared to the other tissues. PET studies in rats revealed a comparatively long mean residence time of circulating 18F-S100 proteins. A major contributor to this phenomenon seems to be a sustained temporary interaction with tissues overexpressing RAGE, e.g., the lung. On the other hand, renal clearance of 18F-S100 via glomerular filtration is a major elimination pathway. However, scavenger receptor-mediated pathways in the liver, the spleen and, to a minor extent, in the kidneys, also seem to contribute to the overall clearance. The presence of sRAGE revealed a decreased retention of 18F-S100A12 in the lung, indicating in vivo binding to RAGE. In vivo blocking studies using maleylated BSA demonstrated a strong inhibition of putative binding sites in rat tissues enriched in cells expressing scavenger receptors like liver and spleen. In conclusion, 18F-labeling of S100 proteins and the use of small animal PET provide a valuable tool to discriminate the kinetics and the metabolic fate of S100 proteins in vivo. Furthermore, the results strongly suggest an involvement of other putative receptors beside RAGE in distribution, tissue association and elimination of circulating proinflammatory S100 proteins. Moreover, the approach provides novel probes for imaging of functional expression of RAGE and scavenger receptors in peripheral inflammatory compartments
Muth, Ingrid Elisabeth Verfasser], and Mathias [Akademischer Betreuer] [Bähr. "Die Expression von High Mobility Group Box 1 (HMGB1) und dessen Receptor for Advanced Glycation Endproducts (RAGE) als Pathomechanismus der sporadischen Einschlusskörpermyositis / Ingrid Elisabeth Muth. Gutachter: Mathias Bähr. Betreuer: Mathias Bähr." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2009. http://d-nb.info/1043027270/34.
Full textIvanova, Nina Mihaylova. "Activation of receptors for advanced glycation endproducts (RAGEs) in human monocytes." [S.l. : s.n.], 2005. http://nbn-resolving.de/urn:nbn:de:bsz:289-vts-55812.
Full textWolf, Susann. "Die Bedeutung von S100A4 und dessen Interaktion mit RAGE bei der Metastasierung des malignen Melanoms." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2014. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-136753.
Full textMahrouf-Yorgov, Meriem. "Contribution à l'étude des propriétés vasculoprotectrices de la metformine : effets sur la voie de transduction de la protéine kinase C et sur le dysfonctionnement endothélial vasculaire du diabète." Paris 5, 2007. http://www.theses.fr/2007PA05P623.
Full textType 2 diabetes is an important public health problem due to vascular complications caused by chronic hyperglycemia. Hyperglycemia has been shown to induce intracellular formation of reactive oxygen species and causes oxidative stress leading to vascular dysfunction. Metformin (met) is a widely used drug for the management of type 2 diabetes. Several studies showed that met improves vascular function of diabetic patients but its exact mechanism of action remains unclear. We investigate in this study the effect of met on the protein kinase C (PKC) and polyADP-ribose polymerase (PARP) pathways involved in diabetic vascular complications. We also explored whether met could modulate the redox-sensible expression of advanced glycation end products receptor (RAGE) and lectin-like oxidized receptor 1 (LOX-1). Taken together our results suggests that met acts at the membrane level and we proposed a unifying mechanism by which metformin improves diabetic vascular endothelial functions
Deo, P. "Effect of Food-Derived Advanced Glycation Endproducts on Receptors and Markers of Oxidative Stress in Human Cell Lines." Thesis, Queen's University Belfast, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.501257.
Full textIndurthi, Venkata. "Interactions of the Receptor for Advanced Glycation End Products (Rage) with Advanced Glycation End Products (AGEs) and S100B." Diss., North Dakota State University, 2016. http://hdl.handle.net/10365/25817.
Full textFarmer, David George Stephen. "The receptor for advanced glycation end-products in pulmonary hypertension." Thesis, University of Glasgow, 2012. http://theses.gla.ac.uk/3730/.
Full textMeghnani, Varsha. "Receptor for Advanced Glycation End Products (RAGE) in Melanoma Progression." Diss., North Dakota State University, 2014. http://hdl.handle.net/10365/24782.
Full textRuhs, Stefanie [Verfasser], Sven-Erik Akademischer Betreuer] Behrens, Andreas [Akademischer Betreuer] Simm, and Monika [Akademischer Betreuer] [Pischetsrieder. "Der Einfluss von "Advanced Glycation Endproduct" - reichen Nahrungsmittelextrakten auf die Funktion kardialer Fibroblasten / Stefanie Ruhs. Betreuer: Sven-Erik Behrens ; Andreas Simm ; Monika Pischetsrieder." Halle, Saale : Universitäts- und Landesbibliothek Sachsen-Anhalt, 2009. http://d-nb.info/1025484436/34.
Full textWhite, Amy Katherine. "Modulators of receptor for advanced glycation end products signalling in the human endometrium." Thesis, Swansea University, 2011. https://cronfa.swan.ac.uk/Record/cronfa42362.
Full textKadasah, Sultan Ftayes Saeed. "The Biology of the Receptor for Advanced Glycation End Products (RAGE) in Cancer." Diss., North Dakota State University, 2020. https://hdl.handle.net/10365/31754.
Full textCobre grant "P20GM109024"
Tsuji, Hiroko. "Ribozyme targeting of receptor for advanced glycation end products in mouse mesangial cells." Kyoto University, 1998. http://hdl.handle.net/2433/182259.
Full textEythrib, Farid Jalil. "The Search for the Receptor for Advanced Glycation End-Products in Avian Vasculature." Thesis, The University of Arizona, 2013. http://hdl.handle.net/10150/297557.
Full textThompson, Ben Arthur. "The role of the receptor for advanced glycation end products in acute lung injury." Thesis, Queen's University Belfast, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.580123.
Full textTeissier, Thibault. "Implication of the receptor for advanced glycation end-products (RAGE) during inflammation and ageing." Thesis, Lille 2, 2019. http://www.theses.fr/2019LIL2S017.
Full textAgeing is defined by the accumulation of events leading to a reduction in the efficacy of organ functions and an increased probability of death with time. This process affects all the animal kingdom and while the pace of ageing varies significantly among species, greatly affecting longevity, the mechanisms of ageing itself are widely conserved. In humans, as life expectancy at birth has been steadily increasing for over a century, the amount of people with age-related diseases and dependency has greatly increased and is becoming a major concern.Glycation is a non-enzymatic process leading to the irreversible interaction of carbonyl compounds, such as sugars, with nucleophiles, including lysine or arginine, forming advanced glycation end-products (AGEs). This process is thought to be involved in ageing as AGEs accumulate in the body with age. However, the role in ageing of consuming AGEs produced during cooking processes is much less understood. Digestion vastly modifies their structure and they can only have indirect an impact. Our group has shown that the long-term consumption of a diet enriched with carboxymethyllysine (CML), one of the most abundant AGEs, induced an accelerated vascular ageing in middle-aged mice. However, this effect was entirely dependent on the expression of the receptor for AGEs, RAGE.RAGE is a multiligand receptor and its activation is primarily characterised by a self-sustaining pro-inflammatory response which has been implicated in both age-related and age-independent disorders including complications of diabetes, cardiovascular diseases, Alzheimer’s disease or cancers. Given the relationship between AGEs and RAGE and their respective role in ageing or age-related disorders, it was hypothesized that RAGE has an important role in both physiological and AGE-accelerated ageing. In addition, our group has demonstrated that dietary CML mostly accumulates in mice kidneys, which age slower than vessels. Therefore, a key aim of this thesis was to investigate whether dietary CML also induces accelerated kidney ageing in older mice and whether the deletion of RAGE prevents this effect and has an impact on normal ageing.Two-month-old wild-type (WT) and RAGE-/- mice were fed a control or a CML-enriched diet (200μg CML/gfood) for 18 months. CML distribution was assessed by immunohistochemistry (IHC) and HPLC-MS/MS. Kidney ageing was assessed by measuring markers of its function, lesions and amyloidosis, as well as of inflammation, oxidation and ageing. In addition, motor function in old (~22 month-old) mice was also assessed using locomotion tests.Firstly, it was demonstrated that although CML accumulated in the kidneys of mice fed the CML-enriched diet, this diet had little effect upon the studied parameters while mice deprived of RAGE were largely protected against age-related renal lesions, renal senile amyloidosis and exhibited decreased inflammation and improved pro-longevity pathways. Thereafter, it was shown that some of old RAGE-/- mice motor functions might be better preserved than in old WT animals, suggesting a reduced sarcopenia in RAGE-/- mice.The significant impact of RAGE on ageing and on low-grade and chronic inflammation, associated with its intrinsic characteristic, strongly suggest that RAGE is a pattern recognition receptor and is a proof of principle that inflammaging is an important motor of ageing which may be modulated through genetic or possibly pharmacologic interventions
Tadayon, Roya [Verfasser], and Oliver [Akademischer Betreuer] Einsle. "Resolving the ligand-binding to pattern recognition receptor for advanced glycation end products (RAGE)." Freiburg : Universität, 2016. http://d-nb.info/115012427X/34.
Full textSwami, Priyanka. "Understanding the Role of the Receptor for Advanced Glycation End-Products (Rage) in Pancreatic Cancer." Diss., North Dakota State University, 2019. https://hdl.handle.net/10365/29865.
Full textNorth Dakota State University. College of Health Professions
NIH Grant # P20 GM109024 from the National Institute of General Medicine
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.
Full textDolling, Sarah Jane. "Characterisation of the Transcriptional regulation of the genetic variants of the receptor for advanced glycation end-products." Thesis, University of Leeds, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.418729.
Full textLo, Alexandra Siu Lok, and n/a. "Paradigms of inflammation : interactions between calcium-binding proteins and the receptor for advanced glycation end products (RAGE)." University of Otago. Department of Physiology, 2005. http://adt.otago.ac.nz./public/adt-NZDU20061016.163427.
Full textHewera, Lisa Franziska [Verfasser], and Andreas [Akademischer Betreuer] Link. "Die Bedeutung des "Receptor of Advanced Glycation End Products" im kardiogenen Schock / Lisa Franziska Hewera. Betreuer: Andreas Link." Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2016. http://d-nb.info/1081935030/34.
Full textSirois, 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.
Full textCreagh-Brown, Benedict Charles. "The receptor for advanced glycation end-products (RAGE) and its ligands in systemic inflammation following surgery necessitating cardiopulmonary bypass." Thesis, Imperial College London, 2011. http://hdl.handle.net/10044/1/7057.
Full textBertheloot, Damien [Verfasser]. "Role of the Receptor for Advanced Glycation End-products (RAGE) in the Immune Sensing of Nucleic Acids / Damien Bertheloot." Bonn : Universitäts- und Landesbibliothek Bonn, 2016. http://d-nb.info/113977512X/34.
Full textChavez, Matias Elizabeth Murayama. "Expression of Osteoarthritis Biomarkers in Temporomandibular Joints of Mice with and Without Receptor for Advanced Glycation End Products (RAGE)." BYU ScholarsArchive, 2014. https://scholarsarchive.byu.edu/etd/5242.
Full textBetz, Christine [Verfasser], and Oliver [Akademischer Betreuer] Einsle. "Structural characterization of the metal-binding ligands S100A8/S100A9 and S100B of the receptor for advanced glycation end products = Strukturelle Charakterisierung der metallbindenden Liganden S100A8/S100A9 und S100B des Rezeptors für Advanced Glycation End Products." Freiburg : Universität, 2013. http://d-nb.info/1115813455/34.
Full textRen, 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.
Full textOstendorp, Thorsten. "Structure and function of the metal-binding protein S100B and its interaction with the receptor for advanced glycation end products." [S.l. : s.n.], 2006. http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-23752.
Full textZENI, FILIPPO. "Circulating levels of soluble Receptor for Advanced Glycation End-products (sRAGE) decrease with aging and may predict age-related cardiac remodeling." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2017. http://hdl.handle.net/10281/170797.
Full textBackground: Aging is an unavoidable risk factor in later life that can influence the onset and progression of many diseases. In fact, the high incidence of cardiovascular diseases in the elderly is mainly attributable to cardiac remodelling associated to physiological intrinsic aging. RAGE is a multi-ligand receptor involved in many age-related disorders. Its soluble isoform (sRAGE) acts as a decoy receptor being able to block the activation of the membrane-bound receptor, and its circulation levels have been found altered in several chronic and acute pathologies. The role of RAGE isoforms in aging and, in particular, cardiac senescence has never been investigated. Moreover, the finding of reliable biomarkers able to assess individual health status of subjects has important applications in prevention, diagnosis, and disease management. In this context, the aim of this study was to ascertain whether sRAGE is a biomarker of aging and age-related cardiac remodelling, and evaluate the contribution of RAGE isoforms to cardiac aging. Results: Serum of male and female from 20 to 92 years old healthy subjects was collected and sRAGE levels were evaluated by ELISA. We found a significant decrease of circulating sRAGE in males while only a trend in females. Accordingly, we observed a strong correlation of sRAGE with chronological age in male but not in female subjects. Male and female mice at different age (2.5-12-22-months, Young, Middle Age (MA) and Old, respectively) undergone 2D-echocardiography to determine the left ventricle (LV) dimensions and function during aging. Serum sRAGE similarly declines from the Young to the MA group in both sexes, and inversely correlate with LV dimensions and function, preferentially in males. No detectable amount of RAGE protein was found in LV at all ages. Rage-/- mice displayed a significant increase of LV volumes and diameters in diastole and systole, and a concomitant decrease in ejection fraction (EF) and fractional shortening (FS), compared to age-matched wt animals during aging with the strongest differences present between the MA groups. Moreover, MA Rage-/- mice exhibited higher deposition of collagen and expression of heart failure marker genes (BNP and Ankrd1) in respect to the wt counterpart. Conversely, no differences in cardiomyocytes size were observed at any age between the two genotypes. Finally, microarray functional annotation analysis based on the interaction between age-genotype revealed that the chronic lack of RAGE affected the expression of genes associated to contractile fibre function, antigen presenting process and adaptive immunity, insulin pathway, cell death and apoptosis. We also found a correlation between LV volumes and diameters in diastole and systole and differentially expressed genes involved in several processes like muscle contraction, fibrosis, wound healing and regulation of apoptosis. Conclusions: Our results indicate that sRAGE is a serum biomarker of healthy aging and age-related cardiac remodeling, preferentially in males. The absence of RAGE in mice exacerbates adverse cardiac remodeling with age. We propose that, among RAGE isoforms, sRAGE may play a pivotal role in cardiac senescence.
Anggayasti, Wresti Listu. "The self-association of High Mobility Group Box 1 (HMGB1): Implications for interaction with Receptor for Advanced Glycation End-products (RAGE) and DNA." Thesis, Curtin University, 2015. http://hdl.handle.net/20.500.11937/2004.
Full textLöbner, Jürgen. "N-Terminale Glykierung von Proteinen in Lebensmitteln und unter physiologischen Bedingungen." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2018. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-233695.
Full textDasari, Shilpa. "Proinflammatory signalling by receptor for advanced glycation end products (RAGE), an important mediator of retinal pigment epithelium (RPE) dysfunction and age related macular degeneration (AMD)." Thesis, Queen's University Belfast, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.602476.
Full textHernandez-Ontiveros, Diana G. "Neuroinflammatory Alterations via CD-36 in Traumatic Brain Injury." Scholar Commons, 2015. http://scholarcommons.usf.edu/etd/5699.
Full textLorenzi, Rodrigo. "Value of RAGE as a circulating biomarker : from sRAGE to anti-sRAGE autoantibodies." Phd thesis, Université du Droit et de la Santé - Lille II, 2013. http://tel.archives-ouvertes.fr/tel-01059800.
Full textPinto, Raphael de Souza. "Inibição do estresse oxidativo em macrófagos previne a redução no conteúdo do receptor ABCA-1 induzida por albumina modificada por glicação avançada." Universidade de São Paulo, 2011. http://www.teses.usp.br/teses/disponiveis/5/5135/tde-22082011-134651/.
Full textAdvanced glycation end products (AGE) impair reverse cholesterol transport, by decreasing the HDL-mediated cholesterol efflux from macrophages. We evaluated the role of advanced glycated albumin (AGE-albumin) on the generation of reactive oxygen species (ROS) by mitochondria and NADPH oxidase, and its implication on the HDL receptor (ABCA-1) level in macrophages. AGE-albumin was prepared by incubation with glyoxal (GO), methylglyoxal (MGO) or glycolaldehyde (GAD) and control albumin (C-albumin) with phosphate buffered saline alone. C and AGE-albumin were incubated along time with J774 macrophages in order to determine ROS production and ABCA-1 protein level by flow citometry. Macrophages treated with GO, MGO and GAD-albumin presented, respectively, 24%, 25% and 24% increased ROS production compared to cells treated with C-albumin. The increase in ROS production was prevented by cell treatment with a NADPH oxidase inhibitor or mitochondrial uncoupler, demonstrating a role of NADPH oxidase and mitochondria in AGE-albumin-induced ROS generation. Compared to cells treated with C-albumin, basal mitochondrial respiration, determined by oxygraphy, was 35% and 46% reduced in cells exposed, respectively, to GO and GAD-albumin and was not restored after cell treatment with mitochondrial uncoupling. Intracellular carbonyl content increased 41% in macrophages treated with GAD-albumin as compared to C-albumin. In macrophages treated with GAD-albumin, the reduction in ABCA-1 content observed after 8 hours of treatment was accompained by the increase of ROS production. Aminoguanidine that prevented ROS generation was able to restore ABCA-1 levels. On the other hand, benfotiamine failed to restore ABCA-1 protein levels which was ascribed to a lesser reduction in ROS generation by this compund. These results point to a role of AGE-albumin on the reduction of cellular cholesterol efflux, notably by diminishing ABCA-1 protein level in macrophages which is associated with intracellular oxidative stress. Inhibition of oxidative stress induced by AGE-albumin prevents disturbances in reverse cholesterol transport by curbing the reduction of ABCA-1 elicited by advanced glycation in macrophages and therefore may contribute to the prevention of atherosclerosis in diabetes mellitus
Krause, René. "Untersuchungen zur Bildung von Furosin und N-terminalen 2(1H)-Pyrazinonen." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2005. http://nbn-resolving.de/urn:nbn:de:swb:14-1111838972095-91003.
Full textKrause, René. "Untersuchungen zur Bildung von Furosin und N-terminalen 2(1H)-Pyrazinonen." Doctoral thesis, Technische Universität Dresden, 2004. https://tud.qucosa.de/id/qucosa%3A24472.
Full textUllah, MD Ashik. "Novel mechanisms of airway inflammation in mouse models of allergen and virus-induced asthma." Thesis, The University of Sydney, 2014. http://hdl.handle.net/2123/12830.
Full textBerrocal, Almanza Luis Carlos [Verfasser]. "The impact of the serum levels of soluble receptor for advanced glycation end products (sRAGE) and its ligand S100A12 for the course and extent of lung involvement in smear positive pulmonary tuberculosis in a cohort study in Hyderabad - India. / Luis Carlos Berrocal Almanza." Berlin : Freie Universität Berlin, 2015. http://d-nb.info/1070570729/34.
Full textJabaudon, Gandet Matthieu. "Approche translationnelle de la voie RAGE au cours du syndrôme de détresse respiratoire aiguë : implications diagnostiques, physiopathologiques et thérapeutiques." Thesis, Clermont-Ferrand 1, 2016. http://www.theses.fr/2016CLF1MM09.
Full textThe acute respiratory distress syndrome (ARDS) is associated with diffuse alveolarinjury leading to increased permeability pulmonary edema and hypoxemic respiratory failure. Despite recent improvements in intensive care, ARDS is still frequent and associated with high mortality and morbidity. Two major features of ARDS may contribute to mortality and response to treatment: impaired alveolar fluid clearance (AFC), i.e. altered capacity of the alveolar epithelium to remove edema fluid from distal lung airspaces, and phenotypes of severe inflammation. Pharmacological approaches of ARDS treatment are limited and further mechanistic explorations are needed to develop innovative diagnostic and therapeutic approaches. The receptor for advanced glycation endproducts (RAGE) is a multiligand pattern recognition receptor that is abundantly expressed by lung alveolar epithelial cells andmodulates several cellular signaling pathways. There is growing evidence supporting sRAGE (the main soluble isoform of RAGE) as a marker of epithelial cell injury, and RAGE may be pivotal in ARDS pathophysiology through the initiation and perpetuation of inflammatory responses. Our objectives were to characterize the roles of RAGE in ARDS through a translational approach combining preclinical and clinical studies. First, observational and interventional clinical studies were conducted to test sRAGE as a biomarker during ARDS.Then, cultures of epithelial cells, macrophages and a mouse model of acidinduced lung injury were used to describe the effects of RAGE pathway on AFC and inflammation, with special emphasis on a macrophage activation through NodLikeReceptor family, Pyrindomain containing 3 (NLRP3) inflammasome. Acidinjured mice were treated with an antiRAGE monoclonal antibody or recombinant sRAGE to test the impact of RAGE inhibition on criteria of experimental ARDS. Results from clinical studies support a role of sRAGE as a biomarker of ARDS, withdiagnostic, prognostic and predictive values. In addition, plasma sRAGE is correlated with a lung imaging phenotype of nonfocal ARDS and could inform on therapeutic response. Herein, we also describe in vivo and in vitro effects of RAGE activation on transepithelial fluid transport and expression levels of epithelial channels (aquaporin 5, αNa,KATPaseandαENaC) and on macrophage activation through NLRP3 inflammasome. Finally, RAGE inhibition improves AFC and decreases lung injury in vivo. Taken together, our findings support a role of RAGE pathway in the regulation of lung injury, AFC and macrophage activation during ARDS, albeit precise regulatory mechanisms remain uncertain. sRAGE has most features of a validated biomarker that could be used in clinical medicine, but whether it may help to identify subgroups (or phenotypes) of patients that would benefit from tailored therapy remains underinvestigated. Modulation ofRAGE pathway may be a promising therapeutic target, and though validation studies are warranted, such findings may ultimately open novel diagnostic and therapeutic perspectivesin patients with ARDS
Muth, Ingrid Elisabeth. "Die Expression von High Mobility Group Box 1 (HMGB1) und dessen Receptor for Advanced Glycation Endproducts (RAGE) als Pathomechanismus der sporadischen Einschlusskörpermyositis." Doctoral thesis, 2009. http://hdl.handle.net/11858/00-1735-0000-0006-AF6D-C.
Full textKoch, Michael [Verfasser]. "Structural insights into signal transducing proteins : regulation of the EF-hand protein S100A2 and activation of the receptor for advanced glycation endproducts / vorgelegt von Michael Koch." 2007. http://d-nb.info/986768782/34.
Full textΔεττοράκη, Αθηνά. "Η συσχέτιση των τελικών προϊόντων προχωρημένης γλυκοζυλίωσης (AGEs), του υποδοχέα τους (RAGE) και του διαλυτού τμήματός του (sRAGE) σε παιδιά, εφήβους και νεαρούς ενήλικες με σακχαρώδη διαβήτη τύπου 1 (ΣΔ1)." Thesis, 2011. http://hdl.handle.net/10889/5275.
Full textThe binding of Advanced Glycation Endproducts (AGEs) to their receptor (RAGE) plays a major role in the development of diabetic vascular complications. This work is based on the relation between circulating soluble RAGE (sRAGE) levels in children, adolescents and young adults with IDDM and RAGE protein expression in association with N-(carboxymethyl)lysine (CML), a major antigenic AGEs component. Circulating sRAGE and CML levels were determined by ELISA and RAGE protein expression was evaluated in peripheral blood mononuclear cells by western immunoblotting in 74 children, adolescents and young adults with IDDM (134 years old) and 43 age, sex and Tanner stage-matched controls. Serum sRAGE levels were significantly higher in IDDM than in controls, inversely correlated to diabetes duration and directly correlated to LDL levels. Furthermore, circulating CML levels were not significantly different between IDDM and controls. Also, the protein expression of the RAGE isoforms 55 kd (full-length), 64 kd and 100 kd, measured by western immunoblotting, was significantly lower in IDDM than in controls, whereas RAGE 37 kd levels were not significantly different between IDDM and controls. Finally, when there was a risk factor, such as increased age, poor lipid profile, increased BMI or waist circumference or increased systolic or diastolic pressure, then it seemed that isoforms RAGE 55, 64 and 100 kd were increased. Isoform RAGE 64 kd could be RAGE-v5, a splice variant which resulted in a change of amino acid sequence in the extracellular ligand-binding domain of RAGE. Isoform RAGE 37 kd seemed to be Δ8-RAGE, a soluble splice variant with probably protective function, which had been found increased in patients with increased HDL. Finally, isoform RAGE 100 kd seemed to be some other splice variant in peripheral mononuclear cells. In conclusion, increased serum levels of sRAGE seen in IDDM children may be a temporary protective measure against cell damage and may be sufficient to efficiently eliminate excessive circulating CML. Moreover, the lower protein expression of the full-length RAGE in IDDM may also reflect the increased sRAGE expression in patients due to RAGE cleavage by metalloproteases. Consequently, in IDDM children, adolescents and young adults there may be a subclinical perturbation of the sRAGE-RAGE-CML axis, which could lead to future clinical vascular damage if additional risk factors are added over time.