Anthrax toxin receptor 1 (ANTXR1 or also known asTEM8) is a protein that in humans is encoded by the ANTXR1gene.[5][6][7] Its molecular weight is predicted as about 63kDa.
The protein encoded by this gene is a type I transmembrane protein and is a tumor-specific endothelial marker that has been implicated in colorectal cancer. This protein has been shown to also be a docking protein or receptor for Bacillus anthracis toxin, the causative agent of the disease, anthrax. The binding of the protective antigen (PA) component, of the tripartite anthrax toxin, to this receptor protein mediates delivery of toxin components to the cytosol of cells. Once inside the cell, the other two components of anthrax toxin, edema factor (EF) and lethal factor (LF) disrupt normal cellular processes. Three alternatively spliced variants have been described.[7]
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Bradley KA, Mogridge J, Mourez M, et al. (2001). "Identification of the cellular receptor for anthrax toxin". Nature. 414 (6860): 225–9. doi:10.1038/n35101999. PMID11700562. S2CID4373278.
Jones GG, Reaper PM, Pettitt AR, Sherrington PD (2004). "The ATR-p53 pathway is suppressed in noncycling normal and malignant lymphocytes". Oncogene. 23 (10): 1911–21. doi:10.1038/sj.onc.1207318. PMID14755251. S2CID31825072.
Bonuccelli G, Sotgia F, Frank PG, et al. (2005). "ATR/TEM8 is highly expressed in epithelial cells lining Bacillus anthracis' three sites of entry: implications for the pathogenesis of anthrax infection". Am. J. Physiol., Cell Physiol. 288 (6): C1402–10. doi:10.1152/ajpcell.00582.2004. PMID15689409.
Hotchkiss KA, Basile CM, Spring SC, et al. (2005). "TEM8 expression stimulates endothelial cell adhesion and migration by regulating cell-matrix interactions on collagen". Exp. Cell Res. 305 (1): 133–44. doi:10.1016/j.yexcr.2004.12.025. PMID15777794.
Rmali KA, Puntis MC, Jiang WG (2005). "TEM-8 and tubule formation in endothelial cells, its potential role of its vW/TM domains". Biochem. Biophys. Res. Commun. 334 (1): 231–8. doi:10.1016/j.bbrc.2005.06.085. PMID15993844.