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Gene Review

PRSS2  -  protease, serine, 2 (trypsin 2)

Homo sapiens

Synonyms: Anionic trypsinogen, Serine protease 2, TRY2, TRY8, TRYP2, ...
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Disease relevance of PRSS2


High impact information on PRSS2

  • Because increased proteolytic activity owing to mutated PRSS1 enhances the risk for chronic pancreatitis, mutations in the gene encoding anionic trypsinogen (PRSS2) may also predispose to disease [1].
  • Here we analyzed PRSS2 in individuals with chronic pancreatitis and controls and found, to our surprise, that a variant of codon 191 (G191R) is overrepresented in control subjects: G191R was present in 220/6,459 (3.4%) controls but in only 32/2,466 (1.3%) affected individuals (odds ratio 0.37; P = 1.1 x 10(-8)) [1].
  • Its electrophoretic mobility and isoelectric pH lie between those of the cationic and anionic trypsinogen variants, and we propose the name "mesotrypsinogen" for the new enzyme precursor [6].
  • Four serine protease gene fragments from this parasite were sequenced and one is 67% identical to the rat trypsin II gene [7].
  • Mutations in anionic trypsinogen gene are not associated with tropical calcific pancreatitis [8].

Biological context of PRSS2


Anatomical context of PRSS2


Associations of PRSS2 with chemical compounds

  • After the previous characterization of one trypsin gene (Try1) of the human body louse Pediculus humanus, genes encoding a second trypsin (Try2) and a chymotrypsin (Chy1) have been cloned using degenerate serine proteinase primers and 5'- and 3'-RACE, and sequenced [11].

Regulatory relationships of PRSS2

  • The Try2 gene was always expressed at much lower levels than Try1 or Chy1 [11].

Other interactions of PRSS2


Analytical, diagnostic and therapeutic context of PRSS2


  1. A degradation-sensitive anionic trypsinogen (PRSS2) variant protects against chronic pancreatitis. Witt, H., Sahin-Tóth, M., Landt, O., Chen, J.M., Kähne, T., Drenth, J.P., Kukor, Z., Szepessy, E., Halangk, W., Dahm, S., Rohde, K., Schulz, H.U., Le Maréchal, C., Akar, N., Ammann, R.W., Truninger, K., Bargetzi, M., Bhatia, E., Castellani, C., Cavestro, G.M., Cerny, M., Destro-Bisol, G., Spedini, G., Eiberg, H., Jansen, J.B., Koudova, M., Rausova, E., Macek, M., Malats, N., Real, F.X., Menzel, H.J., Moral, P., Galavotti, R., Pignatti, P.F., Rickards, O., Spicak, J., Zarnescu, N.O., Böck, W., Gress, T.M., Friess, H., Ockenga, J., Schmidt, H., Pfützer, R., Löhr, M., Simon, P., Weiss, F.U., Lerch, M.M., Teich, N., Keim, V., Berg, T., Wiedenmann, B., Luck, W., Groneberg, D.A., Becker, M., Keil, T., Kage, A., Bernardova, J., Braun, M., Güldner, C., Halangk, J., Rosendahl, J., Witt, U., Treiber, M., Nickel, R., Férec, C. Nat. Genet. (2006) [Pubmed]
  2. Interaction between trypsinogen isoforms in genetically determined pancreatitis: mutation E79K in cationic trypsin (PRSS1) causes increased transactivation of anionic trypsinogen (PRSS2). Teich, N., Le Maréchal, C., Kukor, Z., Caca, K., Witzigmann, H., Chen, J.M., Tóth, M., Mössner, J., Keim, V., Férec, C., Sahin-Tóth, M. Hum. Mutat. (2004) [Pubmed]
  3. Human trypsinogen in colorectal cancer. Williams, S.J., Gotley, D.C., Antalis, T.M. Int. J. Cancer (2001) [Pubmed]
  4. Human anionic trypsinogen: properties of autocatalytic activation and degradation and implications in pancreatic diseases. Kukor, Z., Tóth, M., Sahin-Tóth, M. Eur. J. Biochem. (2003) [Pubmed]
  5. Structural and evolutionary consequences of unpaired cysteines in trypsinogen. Kénesi, E., Katona, G., Szilágyi, L. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  6. Mesotrypsin: a new inhibitor-resistant protease from a zymogen in human pancreatic tissue and fluid. Rinderknecht, H., Renner, I.G., Abramson, S.B., Carmack, C. Gastroenterology (1984) [Pubmed]
  7. Serine proteases from nematode and protozoan parasites: isolation of sequence homologs using generic molecular probes. Sakanari, J.A., Staunton, C.E., Eakin, A.E., Craik, C.S., McKerrow, J.H. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  8. Mutations in anionic trypsinogen gene are not associated with tropical calcific pancreatitis. Idris, M.M., Bhaskar, S., Reddy, D.N., Mani, K.R., Rao, G.V., Singh, L., Chandak, G.R. Gut (2005) [Pubmed]
  9. Gene conversion between functional trypsinogen genes PRSS1 and PRSS2 associated with chronic pancreatitis in a six-year-old girl. Teich, N., Nemoda, Z., Köhler, H., Heinritz, W., Mössner, J., Keim, V., Sahin-Tóth, M. Hum. Mutat. (2005) [Pubmed]
  10. Interchromosomal segmental duplications explain the unusual structure of PRSS3, the gene for an inhibitor-resistant trypsinogen. Rowen, L., Williams, E., Glusman, G., Linardopoulou, E., Friedman, C., Ahearn, M.E., Seto, J., Boysen, C., Qin, S., Wang, K., Kaur, A., Bloom, S., Hood, L., Trask, B.J. Mol. Biol. Evol. (2005) [Pubmed]
  11. Serine proteinases of the human body louse (Pediculus humanus): sequence characterization and expression patterns. Waniek, P.J., Hendgen-Cotta, U.B., Stock, P., Mayer, C., Kollien, A.H., Schaub, G.A. Parasitol. Res. (2005) [Pubmed]
  12. Measurements of exocrine proteins in the pig pancreas using microdialysis. Jönsson, P., Borgström, A., Ohlsson, K. Gastroenterol. Jpn. (1992) [Pubmed]
  13. Acute pancreatitis in Soweto, South Africa: relationship between trypsinogen load, trypsinogen activation, and fibrinolysis. Segal, I., Chaloner, C., Douglas, J., John, K.D., Zaidi, A., Cotter, L., Appelros, S., Borgström, A., Braganza, J.M. Am. J. Gastroenterol. (2002) [Pubmed]
  14. Abnormalities of circulating immunoreactive pancreatic anionic trypsinogen in cystic fibrosis: an assay artifact due to cross-reacting serum antibodies. Moore, D.J., Largman, C., Kopelman, H.R., Wong, S., Durie, P.R. Clin. Biochem. (1986) [Pubmed]
  15. Enzyme leakage, trypsinogen activation, and inflammatory response in endoscopic retrograde cholangiopancreatography-induced pancreatitis. Petersson, U., Borgström, A., Ohlsson, K., Fork, F.T., Toth, E. Pancreas (2002) [Pubmed]
  16. Time-resolved immunofluorometric assays for trypsinogen-1 and 2 in serum reveal preferential elevation of trypsinogen-2 in pancreatitis. Itkonen, O., Koivunen, E., Hurme, M., Alfthan, H., Schröder, T., Stenman, U.H. J. Lab. Clin. Med. (1990) [Pubmed]
  17. Idiopathic calcifying pancreatitis in a Japanese pediatric patient. Seino, K., Nishimori, I., Nagai, Y., Inoue, H., Takada, Y., Adachi, S., Todoroki, T., Fukao, K. J. Gastroenterol. (2000) [Pubmed]
  18. Demonstration of human pancreatic anionic trypsinogen in normal serum by radioimmunoassay. Largman, C., Brodrick, J.W., Geokas, M.C., Johnson, J.H. Biochim. Biophys. Acta (1978) [Pubmed]
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