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

Additional homology searches of all Jackson laboratory murine databases [13], using human S100A12 as the query, were futile. [...]a region homologous to the first exon of S100A12 is also present on the corresponding chromosome 2 of rat, however, exons 2 and 3 are again missing, suggesting that the S100A12 gene might be damaged in all rodents. [...]several proinflammatory properties of this protein might be caused by its binding to RAGE [3]. [...]the RAGE-S100A12 interaction represents an attractive model to explain how RAGE and its proinflammatory ligand contribute to the pathophysiology of several inflammatory diseases [1,3].