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Prss1  -  protease, serine, 1 (trypsin 1)

Rattus norvegicus

Synonyms: Anionic trypsin I, Anionic trypsin-1, PTRYI, Pretrypsinogen I, RATPTRYI, ...
 
 
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Disease relevance of Prss1

 

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

  • (a) Calcium and pancreatic trypsin inhibitor completely inhibit the binding at concentrations when the degradation is not altered; (b) the sequences of peptides of ACTH which inhibit the binding and degradation of 125-I-ACTH-1-24 are different [18].
  • All three proteases were found to belong to the family of chymotrypic serine proteases as deduced from the absence of the Asp 189 which is characteristic for all serine proteases having cleavage specificities similar to pancreatic trypsin [19].
  • The most effective inhibitors were N-ethylmaleimide, bacitracin, and Kunitz pancreatic trypsin inhibitor [20].
  • Cholesterol sulfate and I3SO3-GalCer, which were commonly contained in the epithelia of mammalian digestive tracts, were found to inhibit the activities of typical digestive enzymes, pancreatic trypsin and chymotrypsin, but steroid sulfates, gangliosides and the other membrane constituents did not show any inhibitory activity [17].
  • By day 21, rats treated with octreotide in the camostate group showed a reduced basal pancreatic trypsin concentration and a decreased basal trypsin content (although the changes were not significant) [21].
 

Regulatory relationships of Prss1

  • Conclusion: Exogenous and endogenous CCK seem not to influence milk intake while decrease pancreatic trypsin/protein ratio [12].
 

Other interactions of Prss1

 

Analytical, diagnostic and therapeutic context of Prss1

  • The stability of the mRNAs encoding pancreatic trypsin isozymes, namely the cationic form and the two anionic forms I and II, as well as that of the secretory trypsin inhibitors I and II, were studied in rats fed on either a high-protein diet, or a protein-free diet compared with a standard diet for a 10-day period [25].

References

  1. Transgenic expression of pancreatic secretory trypsin inhibitor-I ameliorates secretagogue-induced pancreatitis in mice. Nathan, J.D., Romac, J., Peng, R.Y., Peyton, M., Macdonald, R.J., Liddle, R.A. Gastroenterology (2005) [Pubmed]
  2. Cholecystokinin influences pancreatic trophism following total gastrectomy in rats. Büchler, M., Malfertheiner, P., Friess, H., Nustede, R., Feurle, G.E., Beger, H.G. Int. J. Pancreatol. (1989) [Pubmed]
  3. Role of pancreatic trypsin in chronic esophagitis induced by gastroduodenal reflux in rats. Naito, Y., Uchiyama, K., Kuroda, M., Takagi, T., Kokura, S., Yoshida, N., Ichikawa, H., Yoshikawa, T. J. Gastroenterol. (2006) [Pubmed]
  4. Thromboxane A2 receptor antagonist prevents pancreatic microvascular leakage in rats with caerulein-induced acute pancreatitis. Hirano, T., Hirano, K. International journal of surgical investigation. (1999) [Pubmed]
  5. A protective role for protease-activated receptors in the airways. Cocks, T.M., Fong, B., Chow, J.M., Anderson, G.P., Frauman, A.G., Goldie, R.G., Henry, P.J., Carr, M.J., Hamilton, J.R., Moffatt, J.D. Nature (1999) [Pubmed]
  6. Importance of bile in regulation of intraluminal proteolytic enzyme activities in the rat. Green, G.M., Nasset, E.S. Gastroenterology (1980) [Pubmed]
  7. Luminal trypsin may regulate enterocytes through proteinase-activated receptor 2. Kong, W., McConalogue, K., Khitin, L.M., Hollenberg, M.D., Payan, D.G., Böhm, S.K., Bunnett, N.W. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  8. Pancreatic trypsin increases matrix metalloproteinase-9 accumulation and activation during acute intestinal ischemia-reperfusion in the rat. Rosário, H.S., Waldo, S.W., Becker, S.A., Schmid-Schönbein, G.W. Am. J. Pathol. (2004) [Pubmed]
  9. Curcumin ameliorates ethanol and nonethanol experimental pancreatitis. Gukovsky, I., Reyes, C.N., Vaquero, E.C., Gukovskaya, A.S., Pandol, S.J. Am. J. Physiol. Gastrointest. Liver Physiol. (2003) [Pubmed]
  10. Structure of two related rat pancreatic trypsin genes. Craik, C.S., Choo, Q.L., Swift, G.H., Quinto, C., MacDonald, R.J., Rutter, W.J. J. Biol. Chem. (1984) [Pubmed]
  11. Early activation of endoplasmic reticulum stress is associated with arginine-induced acute pancreatitis. Kubisch, C.H., Sans, M.D., Arumugam, T., Ernst, S.A., Williams, J.A., Logsdon, C.D. Am. J. Physiol. Gastrointest. Liver Physiol. (2006) [Pubmed]
  12. Influence of gastrointestinal (GI) hormones on suckling, gastric emptying and pancreatic trypsin content in the developing rat. Kisfalvi, K., Hajnal, F., Varga, G., Papp, M. J. Dev. Physiol. (1993) [Pubmed]
  13. Trypsin IV, a novel agonist of protease-activated receptors 2 and 4. Cottrell, G.S., Amadesi, S., Grady, E.F., Bunnett, N.W. J. Biol. Chem. (2004) [Pubmed]
  14. Synthesis and evaluation of diphenyl phosphonate esters as inhibitors of the trypsin-like granzymes A and K and mast cell tryptase. Jackson, D.S., Fraser, S.A., Ni, L.M., Kam, C.M., Winkler, U., Johnson, D.A., Froelich, C.J., Hudig, D., Powers, J.C. J. Med. Chem. (1998) [Pubmed]
  15. Bile-pancreatic juice-independent increases in pancreatic proteases and intestinal cholecystokinin by dietary protein in rats. Hara, H., Ochi, Y., Kasai, T. Proc. Soc. Exp. Biol. Med. (1998) [Pubmed]
  16. Pancreatic trypsin cleaves intestinal alkaline sphingomyelinase from mucosa and enhances the sphingomyelinase activity. Wu, J., Liu, F., Nilsson, A., Duan, R.D. Am. J. Physiol. Gastrointest. Liver Physiol. (2004) [Pubmed]
  17. Sulfated lipids as inhibitors of pancreatic trypsin and chymotrypsin in epithelium of the mammalian digestive tract. Iwamori, M., Iwamori, Y., Ito, N. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  18. Interactions of adrenocorticotropic hormone with its adrenal receptors. Degradation of ACTH-1-24 and ACTH-11-24. Saez, J.M., Dazord, A., Morera, A.M., Bataille, P. J. Biol. Chem. (1975) [Pubmed]
  19. Cloning and structural analysis of MMCP-1, MMCP-4 and MMCP-5, three mouse mast cell-specific serine proteases. Huang, R.Y., Blom, T., Hellman, L. Eur. J. Immunol. (1991) [Pubmed]
  20. Insulin degradation by hepatocytes in primary culture. Duckworth, W.C., Runyan, K.R., Wright, R.K., Halban, P.A., Solomon, S.S. Endocrinology (1981) [Pubmed]
  21. Age-dependent influence of octreotide on stimulated pancreatic growth in the postnatal period of rats. Kisfalvi, K., Friess, H., Büchler, M.W., Tulassay, Z., Varga, G., Papp, M. European journal of gastroenterology & hepatology. (1996) [Pubmed]
  22. Mapping of caspase-2 in the rat and its exclusion as a candidate gene for lymphopenia. Hornum, L., Rasmussen, S.B., Markholst, H. Mamm. Genome (1999) [Pubmed]
  23. Pancreatic and intestinal enzyme activities in rats in response to balanced and unbalanced plant diets. Kushak, R.I., Drapeau, C., Winter, H.S. Plant foods for human nutrition (Dordrecht, Netherlands) (2002) [Pubmed]
  24. Vigilin and enzyme expression in isolated pancreatic acini after mellitin and gamma-interferon treatment. Hilgendorf, I., Van de Perck, M., Emmrich, J., Krammer, H.J., Kruse, C. Pancreatology (2003) [Pubmed]
  25. Dietary modulation of the mRNA stability of trypsin isozymes and the two forms of secretory trypsin inhibitor in the rat pancreas. Carreira, S., Fueri, C., Chaix, J.C., Puigserver, A. Eur. J. Biochem. (1996) [Pubmed]
 
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