The role of RAGE in host pathology and crosstalk between RAGE and TLR4 in innate immune signal transduction pathways.
DAMPs
HMGB1
inflammation
toll-like receptors
Journal
FASEB journal : official publication of the Federation of American Societies for Experimental Biology
ISSN: 1530-6860
Titre abrégé: FASEB J
Pays: United States
ID NLM: 8804484
Informations de publication
Date de publication:
12 2020
12 2020
Historique:
received:
11
09
2020
revised:
07
10
2020
accepted:
13
10
2020
pubmed:
2
11
2020
medline:
28
4
2021
entrez:
1
11
2020
Statut:
ppublish
Résumé
Although the innate immune receptor protein, Receptor for Advanced Glycation End products (RAGE), has been extensively studied, there has been renewed interest in RAGE for its potential role in sepsis, along with a host of other inflammatory diseases of chronic, noninfectious origin. In contrast to other innate immune receptors, for example, Toll-like receptors (TLRs), that recognize ligands derived from pathogenic organisms that are collectively known as "pathogen-associated molecular patterns" (PAMPs) or host-derived "damage-associated molecular patterns" (DAMPs), RAGE has been shown to recognize a broad collection of DAMPs exclusively. Historically, these DAMPs have been shown to be pro-inflammatory in nature. Early studies indicated that the adaptor molecule, MyD88, might be important for this change. More recent studies have explored further the mechanisms underlying this inflammatory change. Overall, the newer results have shown that there is extensive crosstalk between RAGE and TLRs. The three canonical RAGE ligands, Advanced Glycation End products (AGEs), HMGB1, and S100 proteins, have all been shown to activate both TLRs and RAGE to varying degrees in order to induce inflammation in in vitro models. As with any field that delves deeply into innate signaling, obstacles of reagent purity may be a cause of some of the discrepancies in the literature, and we have found that commercial antibodies that have been widely used exhibit a high degree of nonspecificity. Nonetheless, the weight of published evidence has led us to speculate that RAGE may be physically interacting with TLRs on the cell surface to elicit inflammation via MyD88-dependent signaling.
Identifiants
pubmed: 33131091
doi: 10.1096/fj.202002136R
pmc: PMC8121140
mid: NIHMS1699886
doi:
Substances chimiques
Receptor for Advanced Glycation End Products
0
Toll-Like Receptor 4
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
15659-15674Subventions
Organisme : NIAID NIH HHS
ID : R01 AI123371
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI125215
Pays : United States
Organisme : NIH HHS
ID : S10 OD025101
Pays : United States
Informations de copyright
© 2020 Federation of American Societies for Experimental Biology.
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