Health Dictionary
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Chymotrypsin-C
Introduction
Chymotrypsin C, also known as caldecrin or elastase 4, is an enzyme that in humans is encoded by the CTRC gene.[1][2]
Function
Function
Chymotrypsin C is a member of the peptidase S1 family. The encoded protein is a serum calcium-decreasing factor that has chymotrypsin-like protease activity.[1]
References
References
- ↑ 1.0 1.1 “Entrez Gene: chymotrypsin C (caldecrin)”.
- ↑ Tomomura A, Akiyama M, Itoh H, Yoshino I, Tomomura M, Nishii Y, Noikura T, Saheki T (May 1996). “Molecular cloning and expression of human caldecrin”. FEBS Lett. 386 (1): 26–8. doi:10.1016/0014-5793(96)00377-8. PMID 8635596.
Further reading
Further reading
- Freeman TC, Davies R, Calam J (1990). “Interactions of pancreatic secretory trypsin inhibitor in small intestinal juice: its hydrolysis and protection by intraluminal factors”. Clin. Chim. Acta. 195 (1–2): 27–39. doi:10.1016/0009-8981(90)90191-T. PMID 2093478.
- Masson E, Chen JM, Scotet V, et al. (2008). “Association of rare chymotrypsinogen C (CTRC) gene variations in patients with idiopathic chronic pancreatitis”. Hum. Genet. 123 (1): 83–91. doi:10.1007/s00439-007-0459-3. PMID 18172691.
- Rosendahl J, Witt H, Szmola R, et al. (2008). “Chymotrypsin C (CTRC) alterations that diminish activity or secretion are associated with chronic pancreatitis”. Nat. Genet. 40 (1): 78–82. doi:10.1038/ng.2007.44. PMC 2650829. PMID 18059268.
- Kitahara K, Kawa S, Katsuyama Y, et al. (2008). “Microsatellite scan identifies new candidate genes for susceptibility to alcoholic chronic pancreatitis in Japanese patients”. Dis. Markers. 25 (3): 175–80. doi:10.1155/2008/426764. PMID 19096130.
- Stavridi ES, O’Malley K, Lukacs CM, et al. (1996). “Structural change in alpha-chymotrypsin induced by complexation with alpha 1-antichymotrypsin as seen by enhanced sensitivity to proteolysis”. Biochemistry. 35 (33): 10608–15. doi:10.1021/bi9605806. PMID 8718849.
- Gregory SG, Barlow KF, McLay KE, et al. (2006). “The DNA sequence and biological annotation of human chromosome 1”. Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
- Chang MC, Chang YT, Wei SC, et al. (2009). “Association of novel chymotrypsin C gene variations and haplotypes in patients with chronic pancreatitis in Chinese in Taiwan”. Pancreatology. 9 (3): 287–92. doi:10.1159/000199437. PMID 19407484.
- Yoshino-Yasuda I, Kobayashi K, Akiyama M, et al. (1998). “Caldecrin is a novel-type serine protease expressed in pancreas, but its homologue, elastase IV, is an artifact during cloning derived from caldecrin gene”. J. Biochem. 123 (3): 546–54. doi:10.1093/oxfordjournals.jbchem.a021971. PMID 9538241.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). “The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Harris WR, Malencik DA, Johnson CM, et al. (1990). “Purification and characterization of catalytic fragments of phosphorylase kinase gamma subunit missing a calmodulin-binding domain”. J. Biol. Chem. 265 (20): 11740–5. PMID 2365696.
- Derikx MH, Szmola R, te Morsche RH, et al. (2009). “Tropical calcific pancreatitis and its association with CTRC and SPINK1 (p.N34S) variants”. Eur J Gastroenterol Hepatol. 21 (8): 889–94. doi:10.1097/MEG.0b013e32832183cf. PMID 19404200.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2002). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Szmola R; Sahin-Tóth M (2007). “Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: Identity with Rinderknecht’s enzyme Y”. Proc. Natl. Acad. Sci. U.S.A. 104 (27): 11227–32. doi:10.1073/pnas.0703714104. PMC 2040881. PMID 17592142.
- Brecher AS, Yang MP (1998). “Acetaldehyde inhibits chymotrypsin and serum anti-chymotrypsin activity”. J. Investig. Med. 46 (4): 146–52. PMID 9635374.