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 S...
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| Veröffentlicht in: | Trends in immunology 2003-12, Vol.24 (12), p.622-624 |
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| container_title | Trends in immunology |
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| creator | Fuellen, Georg Foell, Dirk Nacken, Wolfgang Sorg, Clemens Kerkhoff, Claus |
| description | 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]. |
| doi_str_mv | 10.1016/j.it.2003.10.004 |
| format | Article |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Sequence Animals Calcium-Binding Proteins - genetics Calcium-Binding Proteins - immunology Genes Genomes Humans Ligands Mice Molecular Sequence Data Receptor for Advanced Glycation End Products Receptors, Immunologic - immunology S100 Proteins S100A12 Protein Sequence Homology, Amino Acid Signal Transduction - immunology |
| title | Absence of S100A12 in mouse: implications for RAGE–S100A12 interaction |
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