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PMID: 19121341 Published · ppublish English Journal Article Review

Binding of S100 proteins to RAGE: an update.

Biochimica et biophysica acta ·Vol. 1793 ·No. 6 ·2009-06-00 ·Pages 993-1007

Leclerc E, Fritz G, Vetter SW, Heizmann CW

Abstract

The Receptor for Advanced Glycation Endproducts (RAGE) is a multi-ligand receptor of the immunoglobulin family. RAGE interacts with structurally different ligands probably through the oligomerization of the receptor on the cell surface. However, the exact mechanism is unknown. Among RAGE ligands are members of the S100 protein family. S100 proteins are small calcium binding proteins with high structural homology. Several members of the family have been shown to interact with RAGE in vitro or in cell-based assays. Interestingly, many RAGE ligands appear to interact with distinct domains of the extracellular portion of RAGE and to trigger various cellular effects. In this review, we summarize the modes of S100 protein-RAGE interaction with regard to their cellular functions.

MeSH Terms
Animals Humans Ligands Protein Binding Protein Isoforms/chemistry,genetics,metabolism Receptor for Advanced Glycation End Products Receptors, Immunologic/chemistry,genetics,metabolism S100 Proteins/genetics,metabolism
Chemicals
Ligands Protein Isoforms Receptor for Advanced Glycation End Products Receptors, Immunologic S100 Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Leclerc Estelle
Department of Chemistry and Biochemistry, Florida Atlantic University, 777 Glades Road, Boca Raton, Fl 33431, USA.
Fritz Günter
Vetter Stefan W
Heizmann Claus W
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
2009-06-00
Epub
2008-00-11
Pages
993-1007
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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