The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

PRSS1  -  protease, serine, 1 (trypsin 1)

Homo sapiens

 
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of PRSS1

 

Psychiatry related information on PRSS1

  • The strongest relationship found in this study was between the CSQ and PRSS catastrophising scales and depressive symptoms [5].
  • Interestingly, the few (nine) subjects who had both early onset alcoholism and antisocial personality disorder had a higher plasma tryptophan but similar TRYP/LNAA ratio to the others [6].
 

High impact information on PRSS1

 

Chemical compound and disease context of PRSS1

 

Biological context of PRSS1

 

Anatomical context of PRSS1

 

Associations of PRSS1 with chemical compounds

  • RESULTS: A cytosine (C) to thymine (T) mutation at position 2441 (g.2441C>T) of the PRSS1 gene, which results in a substitution of arginine by cysteine at position 116 (R116C) of CT, was identified by direct sequencing in both clinically affected members of the family but was not found in the unaffected member [23].
  • The recombination replaced at least 289 nucleotides with the paralogous sequence from the anionic trypsinogen gene (serine protease 2; PRSS2), and resulted in the PRSS1 mutations c.86A > T and c.161A > G, causing the amino acid substitutions N29I and N54S, respectively [10].
  • Mutational screening identified a single A to T mutation resulting in an asparagine to isoleucine transition mutation at position 21 (N21I) in cationic trypsinogen [24].
  • Third, evolutionary divergence from threonine to asparagine at residue 29 in human cationic trypsinogen provides additional advantage [25].
  • However, trypsin-I presented one lysine at position 11, being the first report of this amino acid in the sequence of a lepidopteran digestive trypsin [26].
 

Regulatory relationships of PRSS1

 

Other interactions of PRSS1

 

Analytical, diagnostic and therapeutic context of PRSS1

  • RESULTS: PRSS1 wild-type (R122) and mutant (H122) allele expression was equivalent in multiple (> 3) samples from the phenotypically affected and non-penetrant subjects with R122H genotypes using allele specific quantitative reverse transcription-polymerase chain reaction (RT-PCR) and intron spanning nested RT-PCR followed by cDNA sequencing [18].
  • A case-control-study of 38 pairs of patients with either PRSS1 or SPINK1 mutations showed that the probability of duct dilatation, diabetes and calcification was slightly higher in patients having a SPINK1 mutation [19].
  • MATERIALS AND METHODS: DNA samples containing either the known c.365G>A or c.365 through 366GC>AT variant in exon 3 of PRSS1 were used as positive controls to establish a denaturing high performance liquid chromatography (DHPLC) assay [34].
  • A simple method for the purification of anionic and cationic trypsinogen and trypsin from human pancreatic juice applying affinity chromatography on aprotinin coupled Sepharose is described together with the N-terminal amino acid sequences for both trypsinogens [35].
  • Using whole mount in situ hybridization, gene expression of Try1, Try2 and Chy1 has been localized not only in the distensible anterior region of the midgut of lice but sometimes also in the area following the distensible region [28].

References

  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. Mutations in serine protease inhibitor Kazal type 1 are strongly associated with chronic pancreatitis. Drenth, J.P., te Morsche, R., Jansen, J.B. Gut (2002) [Pubmed]
  3. Complete cystic fibrosis transmembrane conductance regulator gene sequencing in patients with idiopathic chronic pancreatitis and controls. Weiss, F.U., Simon, P., Bogdanova, N., Mayerle, J., Dworniczak, B., Horst, J., Lerch, M.M. Gut (2005) [Pubmed]
  4. Cationic trypsinogen mutations and pancreatitis. Howes, N., Greenhalf, W., Stocken, D.D., Neoptolemos, J.P. Clin. Lab. Med. (2005) [Pubmed]
  5. A comparison of cognitive measures in low back pain: statistical structure and clinical validity at initial assessment. Main, C.J., Waddell, G. Pain (1991) [Pubmed]
  6. Relationships of plasma tryptophan availability to course of illness and clinical features of alcoholism: a preliminary study. Swann, A.C., Johnson, B.A., Cloninger, C.R., Chen, Y.R. Psychopharmacology (Berl.) (1999) [Pubmed]
  7. Mutations in the gene encoding the serine protease inhibitor, Kazal type 1 are associated with chronic pancreatitis. Witt, H., Luck, W., Hennies, H.C., Classen, M., Kage, A., Lass, U., Landt, O., Becker, M. Nat. Genet. (2000) [Pubmed]
  8. Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene. Whitcomb, D.C., Gorry, M.C., Preston, R.A., Furey, W., Sossenheimer, M.J., Ulrich, C.D., Martin, S.P., Gates, L.K., Amann, S.T., Toskes, P.P., Liddle, R., McGrath, K., Uomo, G., Post, J.C., Ehrlich, G.D. Nat. Genet. (1996) [Pubmed]
  9. Hereditary pancreatitis and the risk of pancreatic cancer. International Hereditary Pancreatitis Study Group. Lowenfels, A.B., Maisonneuve, P., DiMagno, E.P., Elitsur, Y., Gates, L.K., Perrault, J., Whitcomb, D.C. J. Natl. Cancer Inst. (1997) [Pubmed]
  10. 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]
  11. Hereditary pancreatitis caused by a novel PRSS1 mutation (Arg-122 --> Cys) that alters autoactivation and autodegradation of cationic trypsinogen. Simon, P., Weiss, F.U., Sahin-Toth, M., Parry, M., Nayler, O., Lenfers, B., Schnekenburger, J., Mayerle, J., Domschke, W., Lerch, M.M. J. Biol. Chem. (2002) [Pubmed]
  12. Mutations in the cationic trypsinogen gene and evidence for genetic heterogeneity in hereditary pancreatitis. Férec, C., Raguénès, O., Salomon, R., Roche, C., Bernard, J.P., Guillot, M., Quéré, I., Faure, C., Mercier, B., Audrézet, M.P., Guillausseau, P.J., Dupont, C., Munnich, A., Bignon, J.D., Le Bodic, L. J. Med. Genet. (1999) [Pubmed]
  13. Bacterial mutagenic evaluation of Luxabendazole, a new broad spectrum anthelmintic, with the Salmonella typhimurium His- and the Escherichia coli Tryp- reversion tests. Ortiz, A.I., Pollastrini, M.T., Barea, M., Ordóñez, D. Mutagenesis (1996) [Pubmed]
  14. Genetic counseling for hereditary pancreatitis--the role of molecular genetics testing for the cationic trypsinogen gene, cystic fibrosis and serine protease inhibitor Kazal type 1. Ellis, I. Gastroenterol. Clin. North Am. (2004) [Pubmed]
  15. CFTR, PRSS1 and SPINK1 mutations in the development of pancreatitis in Brazilian patients. Bernardino, A.L., Guarita, D.R., Mott, C.B., Pedroso, M.R., Machado, M.C., Laudanna, A.A., Tani, C.M., Almeida, F.L., Zatz, M. JOP (2003) [Pubmed]
  16. 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]
  17. Mutational screening of patients with nonalcoholic chronic pancreatitis: identification of further trypsinogen variants. Teich, N., Bauer, N., Mössner, J., Keim, V. Am. J. Gastroenterol. (2002) [Pubmed]
  18. A 93 year old man with the PRSS1 R122H mutation, low SPINK1 expression, and no pancreatitis: insights into phenotypic non-penetrance. Khalid, A., Finkelstein, S., Thompson, B., Kelly, L., Hanck, C., Godfrey, T.E., Whitcomb, D.C. Gut (2006) [Pubmed]
  19. The course of genetically determined chronic pancreatitis. Keim, V., Witt, H., Bauer, N., Bodeker, H., Rosendahl, J., Teich, N., Mossner, J. JOP (2003) [Pubmed]
  20. 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]
  21. Mutations of the cationic trypsinogen in hereditary pancreatitis. Teich, N., Mössner, J., Keim, V. Hum. Mutat. (1998) [Pubmed]
  22. Human trypsinogen in colorectal cancer. Williams, S.J., Gotley, D.C., Antalis, T.M. Int. J. Cancer (2001) [Pubmed]
  23. A Thai family with hereditary pancreatitis and increased cancer risk due to a mutation in PRSS1 gene. Pho-Iam, T., Thongnoppakhun, W., Yenchitsomanus, P.T., Limwongse, C. World J. Gastroenterol. (2005) [Pubmed]
  24. Mutations in the cationic trypsinogen gene are associated with recurrent acute and chronic pancreatitis. Gorry, M.C., Gabbaizedeh, D., Furey, W., Gates, L.K., Preston, R.A., Aston, C.E., Zhang, Y., Ulrich, C., Ehrlich, G.D., Whitcomb, D.C. Gastroenterology (1997) [Pubmed]
  25. Molecular pathology and evolutionary and physiological implications of pancreatitis-associated cationic trypsinogen mutations. Chen, J.M., Montier, T., Férec, C. Hum. Genet. (2001) [Pubmed]
  26. Isolation and characterization of two digestive trypsin-like proteinases from larvae of the stalk corn borer, Sesamia nonagrioides. Novillo, C., Castañera, P., Ortego, F. Insect Biochem. Mol. Biol. (1999) [Pubmed]
  27. Age-related alterations of immunoreactive pancreatic cationic trypsinogen in sera from cystic fibrosis patients with and without pancreatic insufficiency. Durie, P.R., Forstner, G.G., Gaskin, K.J., Moore, D.J., Cleghorn, G.J., Wong, S.S., Corey, M.L. Pediatr. Res. (1986) [Pubmed]
  28. 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]
  29. Chymotrypsin C (caldecrin) stimulates autoactivation of human cationic trypsinogen. Nemoda, Z., Sahin-Tóth, M. J. Biol. Chem. (2006) [Pubmed]
  30. Cationic trypsinogen and pancreatic secretory trypsin inhibitor gene mutations in neonatal hypertrypsinaemia. Patuzzo, C., Castellani, C., Sagramoso, C., Gomez-Lira, M., Bonamini, D., Belpinati, F., Dechecchi, M.C., Assael, B.M., Pignatti, P.F. Eur. J. Hum. Genet. (2003) [Pubmed]
  31. Comparative mapping of the human homologue of the rat diabetes susceptibility gene lyp to a 1.3-Mb segment on HSA7. Hornum, L., Markholst, H. Genomics (2000) [Pubmed]
  32. Relevance of variants in serum antiproteinases for the course of chronic pancreatitis. Teich, N., Walther, K., Bödeker, H., Mössner, J., Keim, V. Scand. J. Gastroenterol. (2002) [Pubmed]
  33. Identification of a novel pancreatitis-associated missense mutation, R116C, in the human cationic trypsinogen gene (PRSS1). Le Maréchal, C., Bretagne, J.F., Raguénès, O., Quéré, I., Chen, J.M., Ferec, C. Mol. Genet. Metab. (2001) [Pubmed]
  34. Discrimination of three mutational events that result in a disruption of the R122 primary autolysis site of the human cationic trypsinogen (PRSS1) by denaturing high performance liquid chromatography. Le Maréchal, C., Chen, J.M., Quéré, I., Raguénès, O., Férec, C., Auroux, J. BMC Genet. (2001) [Pubmed]
  35. Immunoreactive anionic and cationic trypsin in human serum. Kimland, M., Russick, C., Marks, W.H., Borgström, A. Clin. Chim. Acta (1989) [Pubmed]
 
WikiGenes - Universities