RAGE Mediates a Novel Proinflammatory Axis A Central Cell Surface Receptor for S100/Calgranulin Polypeptides

@article{Hofmann1999RAGEMA,
  title={RAGE Mediates a Novel Proinflammatory Axis A Central Cell Surface Receptor for S100/Calgranulin Polypeptides},
  author={M. Hofmann and S. Drury and C. Fu and W. Qu and A. Taguchi and Yan Lu and C. Avila and N. Kambham and A. Bierhaus and P. Nawroth and M. Neurath and T. Slattery and D. Beach and J. McClary and M. Nagashima and J. Morser and David Stern and A. Schmidt},
  journal={Cell},
  year={1999},
  volume={97},
  pages={889-901}
}
S100/calgranulin polypeptides are present at sites of inflammation, likely released by inflammatory cells targeted to such loci by a range of environmental cues. We report here that receptor for AGE (RAGE) is a central cell surface receptor for EN-RAGE (extracellular newly identified RAGE-binding protein) and related members of the S100/calgranulin superfamily. Interaction of EN-RAGEs with cellular RAGE on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with… Expand
RAGE regulation and signaling in inflammation and beyond
TLDR
The current knowledge about the signaling pathways activated in the different cell types are summarized and a potential activation mechanism of RAGE is discussed, as well as putative options for therapeutic intervention. Expand
RAGE (receptor for advanced glycation end products): a central player in the inflammatory response.
TLDR
RAGE may play a dual role in the inflammatory response: on the other hand, RAGE on ECs may function as an adhesive receptor that directly interacts with leukocyte ss2-integrins, thereby directly being involved in inflammatory cell recruitment. Expand
RAGE: a multi-ligand receptor unveiling novel insights in health and disease.
TLDR
The biology of RAGE and the triggered signaling cascades involved in health and disease will be presented and its potential as an attractive pharmacotherapeutic target will be explored by pointing out the pharmacotherAPEutic agents that have been developed for RAGE blockade. Expand
RAGE: The beneficial and deleterious effects by diverse mechanisms of actions
TLDR
The implication of RAGE in Alzheimer disease, the most common neurodegenerative disease in the elderly population, will be discussed, with a focus on Aβ-RAGE interactions with regard to signaling pathways and their impact on cellular activity. Expand
Receptor for Advanced Glycation Endproducts Mediates Neutrophil Migration across Intestinal Epithelium1
TLDR
It is found that RAGE mediates neutrophil (polymorphonuclear leukocytes (PMN) adhesion to, and subsequent migration across, intestinal epithelial monolayers, and appears to be mediated by the binding of RAGE to the PMN-specific β2 integrin CD11b/CD18. Expand
The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses.
TLDR
These features of RAGE allow the receptor to propagate cellular dysfunction in a number of pathophysiologically relevant situations, most often dictated by the formation and persistence of ligands in the tissues. Expand
Molecular Characteristics of RAGE and Advances in Small-Molecule Inhibitors
TLDR
The targeted inhibition of RAGE or its ligands is considered an important strategy for the treatment of cancer and chronic inflammatory diseases. Expand
HMGB1 and RAGE in inflammation and cancer.
TLDR
The role of the HMGB1-RAGE axis in inflammation and cancer is reviewed, which has been implicated in sterile inflammation as well as in cancer, diabetes, and Alzheimer's disease. Expand
Chronic neuronal perturbation mediated by RAGE, a receptor for β-sheet fibrils and S100/calgranulins
TLDR
This view suggests the relevance of a two-hit model underlying such chronic vascular processes in which an underlying perturbant, such as modified lipoproteins, provides a first hit which then perpetuates an exaggerated host response to subsequent environmental challenges. Expand
Divergent pathways of gene expression are activated by the RAGE ligands S100b and AGE-BSA.
TLDR
The findings using AGEs with strong RAGE-binding properties indicate that A GEs may not uniformly play a role in cellular activation, and this study clarified the role in cell activation through gene expression profiling using both in vitro and in vivo model systems. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 105 REFERENCES
Regulation and proinflammatory properties of the chemotactic protein, CP-10.
  • C. Geczy
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 1996
TLDR
Pure E. coli-derived recombinant CP10 has activity equivalent to the native protein and is chemotactic to human and murine leukocytes, and there is no evidence, by mass spectral analysis, of glycosylation of the native Protein 10 kDa. Expand
Characterization and Functional Analysis of the Promoter of RAGE, the Receptor for Advanced Glycation End Products*
TLDR
Results point to NF-κB-dependent mechanisms regulating cellular expression of RAGE and suggest a means of linking RAGE to the inflammatory response. Expand
RAGE: A Receptor with a Taste for Multiple Ligands and Varied Pathophysiologic States
Publisher Summary This chapter focuses on the functions and properties of immunoglobulin super family molecule receptor for advanced glycation end products (RAGE) that interacts with differentExpand
Activation of the Receptor for Advanced Glycation End Products Triggers a p21 ras -dependent Mitogen-activated Protein Kinase Pathway Regulated by Oxidant Stress*
TLDR
Investigation of the transductional processes by which RAGE ligation transmits signals to the nuclei of cells suggests that RAGE-mediated induction of cellular oxidant stress triggers a cascade of intracellular signals involving p21 ras and MAP kinase, culminating in transcription factor activation. Expand
The receptor for advanced glycation end products (RAGE) is a central mediator of the interaction of AGE-beta2microglobulin with human mononuclear phagocytes via an oxidant-sensitive pathway. Implications for the pathogenesis of dialysis-related amyloidosis.
TLDR
Data indicate that RAGE is a central binding site for AGEs formed in vivo and suggest that AGE-beta2M-MP-RAGE interaction likely contributes to the initiation of an inflammatory response in amyloid deposits of long-term hemodialysis patients, a process which may ultimately lead to bone and joint destruction. Expand
The Receptor for Advanced Glycation End Products (RAGE) Is a Cellular Binding Site for Amphoterin
TLDR
Data indicate that RAGE has physiologically relevant ligands distinct from AGEs which are likely, via their interaction with the receptor, to participate in physiologic processes outside of the context of diabetes and accumulation of AAGEs. Expand
Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins.
TLDR
Data indicate that interaction of AGEs with cellular targets, such as ECs, leads to oxidant stress resulting in changes in gene expression and other cellular properties, potentially contributing to the development of vascular lesions. Expand
B-cell surface antigen B7 provides a costimulatory signal that induces T cells to proliferate and secrete interleukin 2.
  • C. Gimmi, G. Freeman, +4 authors L. Nadler
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1991
TLDR
B7-transfected CHO cells can induce suboptimally activated CD28+ T cells to proliferate and secrete high levels of interleukin 2, and this response is identical whether T cells are submitogenically stimulated with either phorbol myristate acetate or anti-CD3 to activate the T cells. Expand
Interleukin-10-deficient mice develop chronic enterocolitis
TLDR
The results indicate that the bowel inflammation in the mutants originates from uncontrolled immune responses stimulated by enteric antigens and that IL-10 is an essential immunoregulator in the intestinal tract. Expand
Advanced glycation endproducts interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM-1) in cultured human endothelial cells and in mice. A potential mechanism for the accelerated vasculopathy of diabetes.
TLDR
Data are consistent with the hypothesis that AGE-RAGE interaction induces expression of VCAM-1 which can prime diabetic vasculature for enhanced interaction with circulating monocytes. Expand
...
1
2
3
4
5
...