Calpains are ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. The calpain proteins are heterodimers consisting of an invariant small subunit and variable large subunits. The large subunit possesses a cysteine protease domain, and both subunits possess calcium-binding domains. Calpains have been implicated in neurodegenerative processes, as their activation can be triggered by calcium influx and oxidative stress. The protein encoded by this gene is expressed predominantly in stomach and small intestine and may have specialized functions in the digestive tract. This gene is thought to be associated with gastric cancer. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.[3]
References
↑Lee HJ, Sorimachi H, Jeong SY, Ishiura S, Suzuki K (May 1998). "Molecular cloning and characterization of a novel tissue-specific calpain predominantly expressed in the digestive tract". Biol Chem. 379 (2): 175–184. doi:10.1515/bchm.1998.379.2.175. PMID9524069.
↑Yoshikawa Y, Mukai H, Hino F, Asada K, Kato I (Jul 2000). "Isolation of two novel genes, down-regulated in gastric cancer". Jpn J Cancer Res. 91 (5): 459–63. doi:10.1111/j.1349-7006.2000.tb00967.x. PMID10835488.
Suzuki K, Sorimachi H, Yoshizawa T, et al. (1996). "Calpain: novel family members, activation, and physiologic function". Biol. Chem. Hoppe-Seyler. 376 (9): 523–9. PMID8561910.
Davis TL, Walker JR, Finerty PJ, et al. (2007). "The crystal structures of human calpains 1 and 9 imply diverse mechanisms of action and auto-inhibition". J. Mol. Biol. 366 (1): 216–229. doi:10.1016/j.jmb.2006.11.037. PMID17157313.
Lee HJ, Tomioka S, Kinbara K, et al. (1999). "Characterization of a human digestive tract-specific calpain, nCL-4, expressed in the baculovirus system". Arch. Biochem. Biophys. 362 (1): 22–31. doi:10.1006/abbi.1998.1021. PMID9917325.
