Cellular signalling of the receptor for advanced glycation end products (RAGE)

Xie, Jianling; Méndez, José D.; Méndez-Valenzuela, Verna; Aguilar-Hernández, María Montserrat

doi:10.1016/j.cellsig.2013.06.013

Cited by 449 publications

(394 citation statements)

References 181 publications

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“…C3a was also shown to bind to the receptor for advanced glycosylation end-products (RAGE) with a high affinity, but this interaction is more complex than a simple ligand-receptor interaction (29,30). Ruan et al (29) demonstrated that C3a is able to form a complex with CpG oligonucleotides to enhance IFN-a release from mononuclear leukocytes.…”

mentioning

confidence: 99%

Is the Complement Activation Product C3a a Proinflammatory Molecule? Re-evaluating the Evidence and the Myth

Coulthard

Woodruff

2015

The Journal of Immunology

251

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The complement activation product C3a is often described as a proinflammatory mediator, alongside its downstream cousin, C5a. However, emerging studies show that C3a has several anti-inflammatory facets in vivo. For example, in the acute inflammatory response, C3a acts in direct opposition to C5a, through preventing the accumulation of neutrophils in inflamed tissues by independently regulating their mobilization. This acute, protective, and opposing activity of C3a to C5a is also illustrated in models of septicemia. In this article, we reinvestigate the discovery and original classification of C3a as a proinflammatory mediator and highlight the emerging studies demonstrating anti-inflammatory effects for C3a in the immune response. It is our hope that this review illuminates these apparently contradictory roles for C3a and challenges the general dogma surrounding C3a, which, historically, has ubiquitously been described as a proinflammatory mediator. In light of this, we urge investigators to use “inflammatory modulator” as the descriptor for C3a.

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mentioning

confidence: 99%

Is the Complement Activation Product C3a a Proinflammatory Molecule? Re-evaluating the Evidence and the Myth

Coulthard

Woodruff

2015

The Journal of Immunology

251

200

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“…RAGE can form heterodimers with the 2-integrin Mac-1 and with some TLRs and signals via multiple pathways including NFB, MAPKs and JAK/STAT [33].…”

Section: Damp Receptors and Cardiac Remodellingmentioning

confidence: 99%

Inflammatory and fibrotic responses of cardiac fibroblasts to myocardial damage associated molecular patterns (DAMPs)

Turner

2016

Journal of Molecular and Cellular Cardiology

168

124

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Cardiac fibroblasts (CF) are well-established as key regulators of extracellular matrix (ECM) turnover in the context of myocardial remodelling and fibrosis. Recently, this cell type has also been shown to act as a sensor of myocardial damage by detecting and responding to damage-associated molecular patterns (DAMPs) upregulated with cardiac injury. CF express a range of innate immunity pattern recognition receptors (TLRs, NLRs, IL-1R1, RAGE) that are stimulated by a host of different DAMPs that are evident in the injured or remodelling myocardium. These include intracellular molecules released by necrotic cells (heat shock proteins, high mobility group box 1 protein, S100 proteins), proinflammatory cytokines (interleukin-1), specific ECM molecules up-regulated in response to tissue injury (fibronectin-EDA, tenascin-C) or molecules modified by a pathological environment (advanced glycation end product-modified proteins observed with diabetes). DAMP receptor activation on fibroblasts is coupled to altered cellular function including changes in proliferation, migration, myofibroblast transdifferentiation, ECM turnover and production of fibrotic and inflammatory paracrine factors, which directly impact on the heart's ability to respond to injury. This review gives an overview of the important role played by CF in responding to myocardial DAMPs and how the DAMP/CF axis could be exploited experimentally and therapeutically.3

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“…RAGE состоит из трех основных доменов -внеклеточ-ного лигандсвязывающего, одинарной трансмембранной спирали и С-терминального короткого домена, который не обладает ферментативной активностью [2]. Тем не ме-нее С-концевой цитоплазматический домен имеет важное значение для передачи сигналов [3]. Эктодомен RAGE состоит из трех молекул Ig с V-, C1-и C2-доменами, которые отвечают за взаимодействие со специфичными лигандами [4].…”

Section: Rage-белки: общие представления о регуляторной активностиunclassified

Ligands of RAGE-Proteins: Role in Intercellular Communication and Pathogenesis of Inflammation

et al. 2015

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Cellular signalling of the receptor for advanced glycation end products (RAGE)

Cited by 449 publications

References 181 publications

Is the Complement Activation Product C3a a Proinflammatory Molecule? Re-evaluating the Evidence and the Myth

Is the Complement Activation Product C3a a Proinflammatory Molecule? Re-evaluating the Evidence and the Myth

Inflammatory and fibrotic responses of cardiac fibroblasts to myocardial damage associated molecular patterns (DAMPs)

Ligands of RAGE-Proteins: Role in Intercellular Communication and Pathogenesis of Inflammation

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