Gene Symbol: Prss2
Description: protease, serine, 2
Alias: Ptryss2, anionic trypsin-2, anionic trypsin II, pancreatic trypsin 2, pancreatic trypsin II, pretrypsinogen II, serine protease 2
Species: rat

Top Publications

  1. MacDonald R, Stary S, Swift G. Two similar but nonallelic rat pancreatic trypsinogens. Nucleotide sequences of the cloned cDNAs. J Biol Chem. 1982;257:9724-32 pubmed
    ..Trypsinogen I mRNA is a major pancreatic mRNA comprising an estimated 2-5% of the total, whereas trypsinogen II mRNA is present at much lower levels. ..
  2. Earnest T, Fauman E, Craik C, Stroud R. 1.59 A structure of trypsin at 120 K: comparison of low temperature and room temperature structures. Proteins. 1991;10:171-87 pubmed
    ..Several features can be localized in the solvent region of the 120 K map that are not seen in the 295 K map. These include several more water molecules as well as an interstitial sulfate ion and two interstitial benzamidine molecules. ..
  3. Dakka N, Puigserver A, Wicker C. Regulation by a protein-free carbohydrate-rich diet of rat pancreatic mRNAs encoding trypsin and elastase isoenzymes. Biochem J. 1990;268:471-4 pubmed
    ..In combination with earlier observations of an overall decrease in cationic trypsin biosynthesis during the same nutritional manipulation, these results suggest that formation of this enzyme is also subject to translational control. ..
  4. Sprang S, Standing T, Fletterick R, Stroud R, Finer Moore J, Xuong N, et al. The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis. Science. 1987;237:905-9 pubmed
    ..The observed decrease in rate results from the loss of nucleophilicity of the active site serine. This decreased nucleophilicity may result from stabilization of a His57 tautomer that is unable to accept the serine hydroxyl proton. ..
  5. Craik C, Choo Q, Swift G, Quinto C, MacDonald R, Rutter W. Structure of two related rat pancreatic trypsin genes. J Biol Chem. 1984;259:14255-64 pubmed
    ..The nucleotide homologies as well as the similarities of intron positions of the two trypsin genes to those of other serine protease genes clearly support an evolutionary relationship between members of this gene family. ..
  6. Hedstrom J, Haglund C, Haapiainen R, Stenman U. Serum trypsinogen-2 and trypsin-2-alpha(1)-antitrypsin complex in malignant and benign digestive-tract diseases. Preferential elevation in patients with cholangiocarcinomas. Int J Cancer. 1996;66:326-31 pubmed
    ..Our results suggest that trypsinogen-2 and trypsin-2-AAT are new potential markers for cholangiocarcinomas. ..
  7. Brinen L, Willett W, Craik C, Fletterick R. X-ray structures of a designed binding site in trypsin show metal-dependent geometry. Biochemistry. 1996;35:5999-6009 pubmed
    ..Of the three metals, the binding of zinc results in the most favorable binding geometry, not dissimilar to those observed in naturally occurring zinc binding proteins. ..
  8. Pasternak A, Ringe D, Hedstrom L. Comparison of anionic and cationic trypsinogens: the anionic activation domain is more flexible in solution and differs in its mode of BPTI binding in the crystal structure. Protein Sci. 1999;8:253-8 pubmed
    ..It is concluded that the activation domain of rat trypsinogen is more flexible than that of bovine trypsinogen, but does not extend further into the protein core. ..
  9. Gillmor S, Takeuchi T, Yang S, Craik C, Fletterick R. Compromise and accommodation in ecotin, a dimeric macromolecular inhibitor of serine proteases. J Mol Biol. 2000;299:993-1003 pubmed
    ..A comparison with two recently described ecotin-like genes from other bacteria suggests that these structural and functional features are conserved in otherwise distant bacterial lineages. ..

More Information


  1. Ye S, Cech A, Belmares R, Bergstrom R, Tong Y, Corey D, et al. The structure of a Michaelis serpin-protease complex. Nat Struct Biol. 2001;8:979-83 pubmed
    ..The serine residue C-terminal to the scissile peptide bond is found in a closer than usual interaction with His 57 at the active site of trypsin. ..
  2. Lucas J, True L, Hawley S, Matsumura M, Morrissey C, Vessella R, et al. The androgen-regulated type II serine protease TMPRSS2 is differentially expressed and mislocalized in prostate adenocarcinoma. J Pathol. 2008;215:118-25 pubmed publisher
    Transmembrane serine protease 2 (TMPRSS2) is an androgen-regulated member of the type two transmembrane protease (TTSP) family...
  3. Lindkvist B, Wierup N, Sundler F, Borgstrom A. Long-term nicotine exposure causes increased concentrations of trypsinogens and amylase in pancreatic extracts in the rat. Pancreas. 2008;37:288-94 pubmed publisher
    ..The combination of increased proenzyme concentrations and unaffected mRNA levels suggests that nicotine impairs secretion rather than production of pancreatic zymogens. ..
  4. Nikolakopoulou A, Dutta R, Chen Z, Miller R, Trapp B. Activated microglia enhance neurogenesis via trypsinogen secretion. Proc Natl Acad Sci U S A. 2013;110:8714-9 pubmed publisher
    ..Mass spectrometry analysis of microglia culture media identified protease serine 2 (PRSS2) as a factor secreted by activated, but not resting, microglia...
  5. Lauhio A, Sorsa T, Srinivas R, Stenman M, Tervahartiala T, Stenman U, et al. Urinary matrix metalloproteinase -8, -9, -14 and their regulators (TRY-1, TRY-2, TATI) in patients with diabetic nephropathy. Ann Med. 2008;40:312-20 pubmed publisher
    ..Our findings suggest that a trypsin-MMP cascade is involved in the pathogenesis of DNP, which may offer new possibilities for diagnosis and treatment of DNP with MMP inhibitors. ..