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{{redirect|PRSS1|the outer space satellite|Pakistan Remote Sensing Satellite}}
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{{Infobox_gene}}
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'''Trypsin-1''', also known as '''cationic trypsinogen''', is a [[protein]] that in humans is encoded by the ''PRSS1'' [[gene]].  Trypsin-1 is the main [[isoform]] of [[trypsinogen]] secreted by pancreas, the others are [[PRSS2|trypsin-2]] (anionic trypsinogen), and [[PRSS3|trypsin-3]] (meso-trypsinogen).
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| update_protein_box = yes
== Function ==
| update_summary = yes
 
| update_citations = yes
This gene encodes a trypsinogen, which is a member of the [[trypsin]] family of [[serine protease]]s. 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.<ref>{{cite web | title = Entrez Gene: PRSS1 protease, serine, 1 (trypsin 1)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5644| accessdate = }}</ref>
}}
 
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== Clinical significance ==
{{GNF_Protein_box
 
| image = PBB_Protein_PRSS1_image.jpg
Its malfunction acts in an autosomal dominant manner to cause pancreatitis. Many mutations that can lead to pancreatitis have been found.<ref>{{cite journal |vauthors=Rebours V, Lévy P, Ruszniewski P |title=An overview of hereditary pancreatitiss |journal=Digestive and Liver Disease |volume=44 |issue=1 |pages=8–15 |year=2011 |pmid=21907651 |doi=10.1016/j.dld.2011.08.003}}</ref><ref>{{cite journal  |vauthors=Teich N, Mössner J, Keim V |title=Mutations of the cationic trypsinogen in hereditary pancreatitis |journal=Hum. Mutat. |volume=12 |issue= 1 |pages= 39–43 |year= 1998 |pmid= 9633818 |doi= 10.1002/(SICI)1098-1004(1998)12:1<39::AID-HUMU6>3.0.CO;2-P }}</ref><ref>{{cite journal  |vauthors=Chen JM, Ferec C |title=Molecular basis of hereditary pancreatitis. |journal=Eur. J. Hum. Genet. |volume=8 |issue= 7 |pages= 473–9 |year= 2000 |pmid= 10909845 |doi= 10.1038/sj.ejhg.5200492 }}</ref><ref>{{cite journal  |vauthors=Gorry MC, Gabbaizedeh D, Furey W, etal |title=Mutations in the cationic trypsinogen gene are associated with recurrent acute and chronic pancreatitis |journal=Gastroenterology |volume=113 |issue= 4 |pages= 1063–8 |year= 1997 |pmid= 9322498 |doi=10.1053/gast.1997.v113.pm9322498 }}</ref> An example is a mutation at Arg 117. Arg 117 is a trypsin-sensitive site which can be cleaved by another trypsin and becomes inactivated.  This site may be a fail-safe mechanism by which trypsin, when activated within the pancreas, may become inactivated.  Mutation at this cleavage site would result in a loss of control and permit autodigestion, causing pancreatitis.<ref>{{cite journal |vauthors=Whitcomb DC, Gorry MC, Preston RA, Furey W, Sossenheimer MJ, Ulrich CD, Martin SP, Gates LK, Amann ST, Toskes PP, Liddle R, McGrath K, Uomo G, Post JC, Ehrlich GD |title=Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene|journal=Nature Genetics |volume=14|pages=141–5 |year=1996 |pmid=8841182 |doi=10.1038/ng1096-141 |issue=2}}</ref>
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1trn.
| PDB = {{PDB2|1trn}}
| Name = Protease, serine, 1 (trypsin 1)
| HGNCid = 9475
| Symbol = PRSS1
| AltSymbols =; MGC120175; MGC149362; TRP1; TRY1; TRY4; TRYP1
| OMIM = 276000
| ECnumber =
| Homologene = 68276
  | MGIid = 3687012
| GeneAtlas_image1 = PBB_GE_PRSS1_205869_at_tn.png
| Function = {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0004295 |text = trypsin activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007586 |text = digestion}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5644
    | Hs_Ensembl = ENSG00000173636
    | Hs_RefseqProtein = NP_002760
    | Hs_RefseqmRNA = NM_002769
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 142136904
    | Hs_GenLoc_end = 142140495
    | Hs_Uniprot = P07477
    | Mm_EntrezGene = 386551
    | Mm_Ensembl = ENSMUSG00000059014
    | Mm_RefseqmRNA = NM_001003664
    | Mm_RefseqProtein = NP_001003664
    | Mm_GenLoc_db =
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 41344917
    | Mm_GenLoc_end = 41430791
    | Mm_Uniprot =   
  }}
}}
'''Protease, serine, 1 (trypsin 1)''', also known as '''PRSS1''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = 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.<ref>{{cite web | title = Entrez Gene: PRSS1 protease, serine, 1 (trypsin 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5644| accessdate = }}</ref>
}}
==See also==
==See also==
*[[Trypsin]]
*[[Trypsin]]


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
 
| citations =
*{{cite journal  |vauthors=Chen JM, Ferec C |title=Gene conversion-like missense mutations in the human cationic trypsinogen gene and insights into the molecular evolution of the human trypsinogen family. |journal=Mol. Genet. Metab. |volume=71 |issue= 3 |pages= 463–9 |year= 2000 |pmid= 11073713 |doi= 10.1006/mgme.2000.3086 }}
*{{cite journal  | author=Chen JM, Ferec C |title=Molecular basis of hereditary pancreatitis. |journal=Eur. J. Hum. Genet. |volume=8 |issue= 7 |pages= 473-9 |year= 2000 |pmid= 10909845 |doi= 10.1038/sj.ejhg.5200492 }}
*{{cite journal  |vauthors=Chen JM, Montier T, Férec C |title=Molecular pathology and evolutionary and physiological implications of pancreatitis-associated cationic trypsinogen mutations. |journal=Hum. Genet. |volume=109 |issue= 3 |pages= 245–52 |year= 2001 |pmid= 11702203 |doi= 10.1007/s004390100580 }}
*{{cite journal  | author=Chen JM, Ferec C |title=Gene conversion-like missense mutations in the human cationic trypsinogen gene and insights into the molecular evolution of the human trypsinogen family. |journal=Mol. Genet. Metab. |volume=71 |issue= 3 |pages= 463-9 |year= 2000 |pmid= 11073713 |doi= 10.1006/mgme.2000.3086 }}
*{{cite journal  |vauthors=Howes N, Greenhalf W, Stocken DD, Neoptolemos JP |title=Cationic trypsinogen mutations and pancreatitis. |journal=Clin. Lab. Med. |volume=25 |issue= 1 |pages= 39–59 |year= 2005 |pmid= 15749231 |doi= 10.1016/j.cll.2004.12.004 }}
*{{cite journal  | author=Chen JM, Montier T, Férec C |title=Molecular pathology and evolutionary and physiological implications of pancreatitis-associated cationic trypsinogen mutations. |journal=Hum. Genet. |volume=109 |issue= 3 |pages= 245-52 |year= 2001 |pmid= 11702203 |doi= 10.1007/s004390100580 }}
*{{cite journal  |vauthors=Kandula L, Whitcomb DC, Lowe ME |title=Genetic issues in pediatric pancreatitis. |journal=Current gastroenterology reports |volume=8 |issue= 3 |pages= 248–53 |year= 2006 |pmid= 16764792 |doi=10.1007/s11894-006-0083-8 }}
*{{cite journal  | author=Howes N, Greenhalf W, Stocken DD, Neoptolemos JP |title=Cationic trypsinogen mutations and pancreatitis. |journal=Clin. Lab. Med. |volume=25 |issue= 1 |pages= 39-59 |year= 2005 |pmid= 15749231 |doi= 10.1016/j.cll.2004.12.004 }}
*{{cite journal   |vauthors=Yamamoto KK, Pousette A, Chow P, etal |title=Isolation of a cDNA encoding a human serum marker for acute pancreatitis. Identification of pancreas-specific protein as pancreatic procarboxypeptidase B. |journal=J. Biol. Chem. |volume=267 |issue= 4 |pages= 2575–81 |year= 1992 |pmid= 1370825 |doi=  }}
*{{cite journal  | author=Kandula L, Whitcomb DC, Lowe ME |title=Genetic issues in pediatric pancreatitis. |journal=Current gastroenterology reports |volume=8 |issue= 3 |pages= 248-53 |year= 2006 |pmid= 16764792 |doi=  }}
*{{cite journal   |vauthors=Pollard SR, Meier W, Chow P, etal |title=CD4-binding regions of human immunodeficiency virus envelope glycoprotein gp120 defined by proteolytic digestion |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 24 |pages= 11320–4 |year= 1992 |pmid= 1763044 |doi=10.1073/pnas.88.24.11320  | pmc=53126 }}
*{{cite journal | author=Yamamoto KK, Pousette A, Chow P, ''et al.'' |title=Isolation of a cDNA encoding a human serum marker for acute pancreatitis. Identification of pancreas-specific protein as pancreatic procarboxypeptidase B. |journal=J. Biol. Chem. |volume=267 |issue= 4 |pages= 2575-81 |year= 1992 |pmid= 1370825 |doi=  }}
*{{cite journal  |vauthors=Shieh BH, Travis J |title=The reactive site of human alpha 2-antiplasmin |journal=J. Biol. Chem. |volume=262 |issue= 13 |pages= 6055–9 |year= 1987 |pmid= 2437112 |doi=  }}
*{{cite journal | author=Pollard SR, Meier W, Chow P, ''et al.'' |title=CD4-binding regions of human immunodeficiency virus envelope glycoprotein gp120 defined by proteolytic digestion. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 24 |pages= 11320-4 |year= 1992 |pmid= 1763044 |doi=  }}
*{{cite journal  |vauthors=Kimland M, Russick C, Marks WH, Borgström A |title=Immunoreactive anionic and cationic trypsin in human serum |journal=Clin. Chim. Acta |volume=184 |issue= 1 |pages= 31–46 |year= 1990 |pmid= 2598466 |doi=10.1016/0009-8981(89)90254-4 }}
*{{cite journal  | author=Shieh BH, Travis J |title=The reactive site of human alpha 2-antiplasmin. |journal=J. Biol. Chem. |volume=262 |issue= 13 |pages= 6055-9 |year= 1987 |pmid= 2437112 |doi=  }}
*{{cite journal   |vauthors=Emi M, Nakamura Y, Ogawa M, etal |title=Cloning, characterization and nucleotide sequences of two cDNAs encoding human pancreatic trypsinogens |journal=Gene |volume=41 |issue= 2–3 |pages= 305–10 |year= 1986 |pmid= 3011602 |doi=10.1016/0378-1119(86)90111-3 }}
*{{cite journal  | author=Kimland M, Russick C, Marks WH, Borgström A |title=Immunoreactive anionic and cationic trypsin in human serum. |journal=Clin. Chim. Acta |volume=184 |issue= 1 |pages= 31-46 |year= 1990 |pmid= 2598466 |doi=  }}
*{{cite journal   |vauthors=Honey NK, Sakaguchi AY, Quinto C, etal |title=Chromosomal assignments of human genes for serine proteases trypsin, chymotrypsin B, and elastase |journal=Somat. Cell Mol. Genet. |volume=10 |issue= 4 |pages= 369–76 |year= 1984 |pmid= 6589790 |doi=10.1007/BF01535632 }}
*{{cite journal | author=Emi M, Nakamura Y, Ogawa M, ''et al.'' |title=Cloning, characterization and nucleotide sequences of two cDNAs encoding human pancreatic trypsinogens. |journal=Gene |volume=41 |issue= 2-3 |pages= 305-10 |year= 1986 |pmid= 3011602 |doi=  }}
*{{cite journal  |vauthors=Merrill GA, Butler M, Horowitz PM |title=Limited tryptic digestion near the amino terminus of bovine liver rhodanese produces active electrophoretic variants with altered refolding |journal=J. Biol. Chem. |volume=268 |issue= 21 |pages= 15611–20 |year= 1993 |pmid= 8340386 |doi=  }}
*{{cite journal | author=Honey NK, Sakaguchi AY, Quinto C, ''et al.'' |title=Chromosomal assignments of human genes for serine proteases trypsin, chymotrypsin B, and elastase. |journal=Somat. Cell Mol. Genet. |volume=10 |issue= 4 |pages= 369-76 |year= 1984 |pmid= 6589790 |doi=  }}
*{{cite journal  |vauthors=Rowen L, Koop BF, Hood L |title=The complete 685-kilobase DNA sequence of the human beta T cell receptor locus |journal=Science |volume=272 |issue= 5269 |pages= 1755–62 |year= 1996 |pmid= 8650574 |doi=10.1126/science.272.5269.1755 }}
*{{cite journal  | author=Merrill GA, Butler M, Horowitz PM |title=Limited tryptic digestion near the amino terminus of bovine liver rhodanese produces active electrophoretic variants with altered refolding. |journal=J. Biol. Chem. |volume=268 |issue= 21 |pages= 15611-20 |year= 1993 |pmid= 8340386 |doi=  }}
*{{cite journal   |vauthors=Gaboriaud C, Serre L, Guy-Crotte O, etal |title=Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151 |journal=J. Mol. Biol. |volume=259 |issue= 5 |pages= 995–1010 |year= 1996 |pmid= 8683601 |doi= 10.1006/jmbi.1996.0376 }}
*{{cite journal  | author=Rowen L, Koop BF, Hood L |title=The complete 685-kilobase DNA sequence of the human beta T cell receptor locus. |journal=Science |volume=272 |issue= 5269 |pages= 1755-62 |year= 1996 |pmid= 8650574 |doi=  }}
*{{cite journal  |vauthors=Gu M, Majerus PW |title=The properties of the protein tyrosine phosphatase PTPMEG |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27751–9 |year= 1996 |pmid= 8910369 |doi=10.1074/jbc.271.44.27751}}
*{{cite journal | author=Gaboriaud C, Serre L, Guy-Crotte O, ''et al.'' |title=Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151. |journal=J. Mol. Biol. |volume=259 |issue= 5 |pages= 995-1010 |year= 1996 |pmid= 8683601 |doi= 10.1006/jmbi.1996.0376 }}
*{{cite journal   |vauthors=Christensen S, Valnickova Z, Thogersen IB, etal |title=Assignment of a single disulphide bridge in human alpha2-antiplasmin: implications for the structural and functional properties |journal=Biochem. J. |volume=323 |issue=  Pt 3|pages= 847–52 |year= 1997 |pmid= 9169621 |doi=  | pmc=1218391 }}
*{{cite journal  | author=Whitcomb DC, Gorry MC, Preston RA, ''et al.'' |title=Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene. |journal=Nat. Genet. |volume=14 |issue= 2 |pages= 141-5 |year= 1996 |pmid= 8841182 |doi= 10.1038/ng1096-141 }}
*{{cite journal  |vauthors=Dahlen JR, Foster DC, Kisiel W |title=Expression, purification, and inhibitory properties of human proteinase inhibitor |journal=Biochemistry |volume=36 |issue= 48 |pages= 14874–82 |year= 1998 |pmid= 9402754 |doi= 10.1021/bi970977p }}
*{{cite journal  | author=Gu M, Majerus PW |title=The properties of the protein tyrosine phosphatase PTPMEG. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27751-9 |year= 1996 |pmid= 8910369 |doi= }}
*{{cite journal | author=Christensen S, Valnickova Z, Thogersen IB, ''et al.'' |title=Assignment of a single disulphide bridge in human alpha2-antiplasmin: implications for the structural and functional properties. |journal=Biochem. J. |volume=323 ( Pt 3) |issue=  |pages= 847-52 |year= 1997 |pmid= 9169621 |doi=  }}
*{{cite journal  | author=Gorry MC, Gabbaizedeh D, Furey W, ''et al.'' |title=Mutations in the cationic trypsinogen gene are associated with recurrent acute and chronic pancreatitis. |journal=Gastroenterology |volume=113 |issue= 4 |pages= 1063-8 |year= 1997 |pmid= 9322498 |doi=  }}
*{{cite journal  | author=Dahlen JR, Foster DC, Kisiel W |title=Expression, purification, and inhibitory properties of human proteinase inhibitor. |journal=Biochemistry |volume=36 |issue= 48 |pages= 14874-82 |year= 1998 |pmid= 9402754 |doi= 10.1021/bi970977p }}
*{{cite journal  | author=Teich N, Mössner J, Keim V |title=Mutations of the cationic trypsinogen in hereditary pancreatitis. |journal=Hum. Mutat. |volume=12 |issue= 1 |pages= 39-43 |year= 1998 |pmid= 9633818 |doi= 10.1002/(SICI)1098-1004(1998)12:1<39::AID-HUMU6>3.0.CO;2-P }}
}}
{{refend}}
{{refend}}
==External links==
* [https://www.ncbi.nlm.nih.gov/books/NBK84399/  GeneReviews/NCBI/NIH/UW entry on PRSS1-Related Hereditary Pancreatitis]


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Latest revision as of 07:14, 21 July 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Trypsin-1, also known as cationic trypsinogen, is a protein that in humans is encoded by the PRSS1 gene. Trypsin-1 is the main isoform of trypsinogen secreted by pancreas, the others are trypsin-2 (anionic trypsinogen), and trypsin-3 (meso-trypsinogen).

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. Many mutations that can lead to pancreatitis have been found.[2][3][4][5] An example is a mutation at Arg 117. Arg 117 is a trypsin-sensitive site which can be cleaved by another trypsin and becomes inactivated. This site may be a fail-safe mechanism by which trypsin, when activated within the pancreas, may become inactivated. Mutation at this cleavage site would result in a loss of control and permit autodigestion, causing pancreatitis.[6]

See also

References

  1. ↑ "Entrez Gene: PRSS1 protease, serine, 1 (trypsin 1)".
  2. ↑ Rebours V, Lévy P, Ruszniewski P (2011). "An overview of hereditary pancreatitiss". Digestive and Liver Disease. 44 (1): 8–15. doi:10.1016/j.dld.2011.08.003. PMID 21907651.
  3. ↑ 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.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ Whitcomb DC, Gorry MC, Preston RA, Furey W, Sossenheimer MJ, Ulrich CD, Martin SP, Gates LK, Amann ST, Toskes PP, Liddle R, McGrath K, Uomo G, Post JC, Ehrlich GD (1996). "Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene". Nature Genetics. 14 (2): 141–5. doi:10.1038/ng1096-141. PMID 8841182.

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.



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