Absence of S100A12 in mouse: implications for RAGE–S100A12 interaction

RAGE (receptor of advanced glycation endproducts), a member of the IgG superfamily, is present on numerous cell types, including monocytes, fibroblasts, endothelial and smooth muscle cells. Activation of the RAGE pathway is important in wound healing, atherogenesis, tumorgenesis, systemic amyloidosis and Alzheimer's disease [ 1 Stern D. et al. Receptor for advanced glycation endproducts: a multiligand receptor magnifying cell stress in diverse pathologic settings. Adv. Drug Deliv. Rev. 2002; 54: 1615-1625 Crossref PubMed Scopus (250) Google Scholar , 2 Deane R. et al. RAGE mediates amyloid-β peptide transport across the blood–brain barrier and accumulation in brain. Nat. Med. 2003; 9: 907-913 Crossref PubMed Scopus (1208) Google Scholar ]. Ligation of RAGE activates multiple intracellular signalling pathways and several downstream signalling molecules have been identified [ 1 Stern D. et al. Receptor for advanced glycation endproducts: a multiligand receptor magnifying cell stress in diverse pathologic settings. Adv. Drug Deliv. Rev. 2002; 54: 1615-1625 Crossref PubMed Scopus (250) Google Scholar ]. RAGE also binds the non-AGEs (non-advanced glycation endproducts) S100B and S100A12, termed extracellular newly identified RAGE-binding proteins (EN-RAGEs) [ 3 Hofmann M.A. et al. RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides. Cell. 1999; 97: 889-901 Abstract Full Text Full Text PDF PubMed Scopus (1640) Google Scholar ], and the RAGE–S100 interaction represents a novel proinflammatory axis involved in several inflammatory diseases [ 3 Hofmann M.A. et al. RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides. Cell. 1999; 97: 889-901 Abstract Full Text Full Text PDF PubMed Scopus (1640) Google Scholar ].