Trypsin 1
Trypsin-1 is a protein that in humans is encoded by the PRSS1 gene.
Function
This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases. This enzyme is secreted by the pancreas and cleaved to its active form in the small intestine. It is active on peptide linkages involving the carboxyl group of lysine or arginine. Mutations in this gene are associated with hereditary pancreatitis. This gene and several other trypsinogen genes are localized to the T cell receptor beta locus on chromosome 7.[1]
Clinical significance
Its malfunction acts in an autosomal dominant manner to cause pancreatitis.
See also
References
Further reading
- Chen JM, Ferec C (2000). "Molecular basis of hereditary pancreatitis.". Eur. J. Hum. Genet. 8 (7): 473–9. doi:10.1038/sj.ejhg.5200492. PMID 10909845.
- Chen JM, Ferec C (2000). "Gene conversion-like missense mutations in the human cationic trypsinogen gene and insights into the molecular evolution of the human trypsinogen family.". Mol. Genet. Metab. 71 (3): 463–9. doi:10.1006/mgme.2000.3086. PMID 11073713.
- Chen JM, Montier T, Férec C (2001). "Molecular pathology and evolutionary and physiological implications of pancreatitis-associated cationic trypsinogen mutations.". Hum. Genet. 109 (3): 245–52. doi:10.1007/s004390100580. PMID 11702203.
- Howes N, Greenhalf W, Stocken DD, Neoptolemos JP (2005). "Cationic trypsinogen mutations and pancreatitis.". Clin. Lab. Med. 25 (1): 39–59. doi:10.1016/j.cll.2004.12.004. PMID 15749231.
- Kandula L, Whitcomb DC, Lowe ME (2006). "Genetic issues in pediatric pancreatitis.". Current gastroenterology reports 8 (3): 248–53. doi:10.1007/s11894-006-0083-8. PMID 16764792.
- Yamamoto KK, Pousette A, Chow P, et al. (1992). "Isolation of a cDNA encoding a human serum marker for acute pancreatitis. Identification of pancreas-specific protein as pancreatic procarboxypeptidase B.". J. Biol. Chem. 267 (4): 2575–81. PMID 1370825.
- Pollard SR, Meier W, Chow P, et al. (1992). "CD4-binding regions of human immunodeficiency virus envelope glycoprotein gp120 defined by proteolytic digestion". Proc. Natl. Acad. Sci. U.S.A. 88 (24): 11320–4. doi:10.1073/pnas.88.24.11320. PMC 53126. PMID 1763044. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=53126.
- Shieh BH, Travis J (1987). "The reactive site of human alpha 2-antiplasmin". J. Biol. Chem. 262 (13): 6055–9. PMID 2437112.
- Kimland M, Russick C, Marks WH, Borgström A (1990). "Immunoreactive anionic and cationic trypsin in human serum". Clin. Chim. Acta 184 (1): 31–46. doi:10.1016/0009-8981(89)90254-4. PMID 2598466.
- Emi M, Nakamura Y, Ogawa M, et al. (1986). "Cloning, characterization and nucleotide sequences of two cDNAs encoding human pancreatic trypsinogens". Gene 41 (2–3): 305–10. doi:10.1016/0378-1119(86)90111-3. PMID 3011602.
- Honey NK, Sakaguchi AY, Quinto C, et al. (1984). "Chromosomal assignments of human genes for serine proteases trypsin, chymotrypsin B, and elastase". Somat. Cell Mol. Genet. 10 (4): 369–76. doi:10.1007/BF01535632. PMID 6589790.
- Merrill GA, Butler M, Horowitz PM (1993). "Limited tryptic digestion near the amino terminus of bovine liver rhodanese produces active electrophoretic variants with altered refolding". J. Biol. Chem. 268 (21): 15611–20. PMID 8340386.
- Rowen L, Koop BF, Hood L (1996). "The complete 685-kilobase DNA sequence of the human beta T cell receptor locus". Science 272 (5269): 1755–62. doi:10.1126/science.272.5269.1755. PMID 8650574.
- Gaboriaud C, Serre L, Guy-Crotte O, et al. (1996). "Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151". J. Mol. Biol. 259 (5): 995–1010. doi:10.1006/jmbi.1996.0376. PMID 8683601.
- Whitcomb DC, Gorry MC, Preston RA, et al. (1996). "Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene". Nat. Genet. 14 (2): 141–5. doi:10.1038/ng1096-141. PMID 8841182.
- Gu M, Majerus PW (1996). "The properties of the protein tyrosine phosphatase PTPMEG". J. Biol. Chem. 271 (44): 27751–9. doi:10.1074/jbc.271.44.27751. PMID 8910369.
- Christensen S, Valnickova Z, Thogersen IB, et al. (1997). "Assignment of a single disulphide bridge in human alpha2-antiplasmin: implications for the structural and functional properties". Biochem. J. 323 ( Pt 3) (Pt 3): 847–52. PMC 1218391. PMID 9169621. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1218391.
- Gorry MC, Gabbaizedeh D, Furey W, et al. (1997). "Mutations in the cationic trypsinogen gene are associated with recurrent acute and chronic pancreatitis". Gastroenterology 113 (4): 1063–8. doi:10.1053/gast.1997.v113.pm9322498. PMID 9322498.
- Dahlen JR, Foster DC, Kisiel W (1998). "Expression, purification, and inhibitory properties of human proteinase inhibitor". Biochemistry 36 (48): 14874–82. doi:10.1021/bi970977p. PMID 9402754.
- Teich N, Mössner J, Keim V (1998). "Mutations of the cationic trypsinogen in hereditary pancreatitis". Hum. Mutat. 12 (1): 39–43. doi:10.1002/(SICI)1098-1004(1998)12:1<39::AID-HUMU6>3.0.CO;2-P. PMID 9633818.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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1trn: CRYSTAL STRUCTURE OF HUMAN TRYPSIN 1: UNEXPECTED PHOSPHORYLATION OF TYROSINE 151
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factors: Thrombin · Factor VIIa · Factor IXa · Factor Xa · Factor XIa · Factor XIIa · Kallikrein ( PSA, KLK1, KLK2, KLK3, KLK4, KLK5, KLK6, KLK7, KLK8, KLK9, KLK10, KLK11, KLK12, KLK13, KLK14, KLK15)
fibrinolysis: Plasmin · Plasminogen activator ( Tissue plasminogen activator · Urinary plasminogen activator)
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B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
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