Trypsin-2

Not to be confused with TMPRSS2, Transmembrane protease, serine 2.

PRSS2
Identifiers
Aliases	PRSS2, TRY2, TRY8, TRYP2, protease, serine 2, serine protease 2
External IDs	OMIM: 601564; MGI: 102759; GeneCards: PRSS2
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 3.4.21.4 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 7 (human) Band 7q34 Start 142,760,398 bp End 142,774,564 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6|6 B1 Start 41,498,721 bp End 41,502,013 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas islet of Langerhans duodenum testicle fundus ectocervix right coronary artery body of stomach canal of the cervix right uterine tube Top expressed in pyloric antrum islet of Langerhans pancreatic acinus duodenum sexually immature organism mucous cell of stomach masseter muscle intercostal muscle brown adipose tissue quadriceps femoris muscle More reference expression data BioGPS n/a
Gene ontology Molecular function calcium ion binding peptidase activity protein binding hydrolase activity metal ion binding serine-type endopeptidase activity serine-type peptidase activity metalloendopeptidase activity Cellular component extracellular matrix extracellular region extracellular space azurophil granule lumen Biological process collagen catabolic process digestion positive regulation of cell growth extracellular matrix disassembly proteolysis positive regulation of cell adhesion antimicrobial humoral response neutrophil degranulation Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 5645 22072 Ensembl ENSG00000282049 ENSG00000275896 ENSMUSG00000057163 UniProt P07478 P07146 RefSeq (mRNA) NM_001303414 NM_002770 NM_009430 RefSeq (protein) NP_001290343 NP_002761 NP_033456 Location (UCSC) Chr 7: 142.76 – 142.77 Mb Chr 6: 41.5 – 41.5 Mb PubMed search
Wikidata
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Trypsin-2 (also called serine protease 2) is an enzyme that in humans is encoded by the PRSS2 gene. Trypsin-2 is a digestive enzyme which functions to break down proteins as a protease. Like other trypsins it is secreted in its inactive, trypsinogen form by the acinar cells of the pancreas into the small intestines as part of pancreatic juice. It is distinctive in its potential ability to degrade type II collagen, which may be connected to rheumatoid arthritis.

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. This gene and several other trypsinogen genes are localized to the T cell receptor beta locus on chromosome 7. [provided by RefSeq, Jul 2008].

Further reading

• Williams SJ, Gotley DC, Antalis TM (July 2001). "Human trypsinogen in colorectal cancer". International Journal of Cancer. 93 (1): 67–73. doi:10.1002/ijc.1304. PMID 11391623. S2CID 22649653.
• Mayumi T, Inui K, Maetani I, Yokoe M, Sakamoto T, Yoshida M, et al. (Urinary Trypsinogen-2 Dipstick for Acute Pancreatitis Study Group of Japanese Society of Abdominal Emergency Medicine (UtrAP Study Group)) (August 2012). "Validity of the urinary trypsinogen-2 test in the diagnosis of acute pancreatitis". Pancreas. 41 (6): 869–875. doi:10.1097/MPA.0b013e3182480ab7. PMID 22481290. S2CID 24109182.
• Whitcomb DC (2025). "PRSS1-Related Hereditary Pancreatitis". In Adam MP, Bick S, Mirzaa GM, Wallace SE, Amemiya A (eds.). GeneReviews^®. Seattle (WA): University of Washington, Seattle. PMID 22379635.
• Ahmed M, Forsberg J, Bergsten P (2005). "Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry". Journal of Proteome Research. 4 (3): 931–940. doi:10.1021/pr050024a. PMID 15952740.
• Vilen ST, Suojanen J, Salas F, Risteli J, Ylipalosaari M, Itkonen O, et al. (October 2012). "Trypsin-2 enhances carcinoma invasion by processing tight junctions and activating ProMT1-MMP". Cancer Investigation. 30 (8): 583–592. doi:10.3109/07357907.2012.716467. PMID 22909050. S2CID 29172202.
• Lempinen M, Isoniemi H, Mäkisalo H, Nordin A, Halme L, Arola J, et al. (November 2007). "Enhanced detection of cholangiocarcinoma with serum trypsinogen-2 in patients with severe bile duct strictures". Journal of Hepatology. 47 (5): 677–683. doi:10.1016/j.jhep.2007.05.017. PMID 17640760.
• Galey D, Becker K, Haughey N, Kalehua A, Taub D, Woodward J, et al. (June 2003). "Differential transcriptional regulation by human immunodeficiency virus type 1 and gp120 in human astrocytes". Journal of Neurovirology. 9 (3): 358–371. doi:10.1080/13550280390201119. PMID 12775419. S2CID 22016092.
• Baptista AM, Jonson PH, Hough E, Petersen SB (September 1998). "The origin of trypsin: evidence for multiple gene duplications in trypsins". Journal of Molecular Evolution. 47 (3): 353–362. Bibcode:1998JMolE..47..353B. doi:10.1007/PL00006393. PMID 9732462. S2CID 15271694.
• Gao J, Zhu F, Lv S, Li Z, Ling Z, Gong Y, et al. (June 2010). "Identification of pancreatic juice proteins as biomarkers of pancreatic cancer". Oncology Reports. 23 (6): 1683–1692. doi:10.3892/or_00000812. PMID 20428826.

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