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Gene Review

TMPRSS15  -  transmembrane protease, serine 15

Homo sapiens

Synonyms: ENTK, Enterokinase, Enteropeptidase, MGC133046, PRSS7, ...
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Disease relevance of PRSS7


High impact information on PRSS7


Chemical compound and disease context of PRSS7

  • Pancreatitis was induced by intraductal injection of sodium-taurocholate (3%, 1 mL/kg BW) and enterokinase (2 U/kg BW) [7].
  • Isolation of high-enterokinase-secreting segments of small bowel from their luminal continuity by fashioning of Thiry--Vella fistulas led to a decay of enterokinase activity to minimal levels within 12--16 h [8].
  • Procedures have been devised for producing in Escherichia coli high yields of purified recombinant human growth hormone (hGH), by utilizing N-terminal pentapeptide sequence of human tumor necrosis factor-alpha, histidine tag and enterokinase cleavage site as a fusion partner [9].

Biological context of PRSS7


Anatomical context of PRSS7

  • Enteropeptidase (enterokinase [E.C.]) is a serine protease of the intestinal brush border in the proximal small intestine [15].
  • Enterokinase is a serine protease of the duodenal brush border membrane that cleaves trypsinogen and produces active trypsin, thereby leading to the activation of many pancreatic digestive enzymes [12].
  • Fourteen patients with diarrhea and grade II mucosal injury revealed a significant (P less than 0.01) reduction of enterokinase, trypsin, and disaccharidase activites as compared to 59 children with normal mucosa [1].
  • In addition, the distributional pattern of EK differs from the disaccharidases, showing the highest activity in duodenum and the lowest in ileum, whereas disaccharidases are highest in jejunum with lower activity in duodenum and ileum [13].
  • The concomitant appearance of enterokinase (EK) and trypsin activities in the human intestinal mucosa is indicative of the importance of EK as an activator of trypsinogen and therefore as the key enzyme in protein digestion [13].

Associations of PRSS7 with chemical compounds


Regulatory relationships of PRSS7

  • The amino acid sequence surrounding the amino terminus of the enterokinase light chain is ITPK-IVGG (human) or VSPK-IVGG (bovine), suggesting that single-chain enterokinase is activated by an unidentified trypsin-like protease that cleaves the indicated Lys-Ile bond [11].
  • The purified mutant hK2 may be activated by either enterokinase or factor Xa to generate an enzyme for use in functional studies with the characteristics of the original wild-type protein [21].
  • In the present study, we produced a secreted form of recombinant MT-SP1/matriptase (ekMT-SP1s) that can be activated by enterokinase in vitro and investigated the inhibitory ability of various protease inhibitors toward the recombinant enzyme [22].

Other interactions of PRSS7

  • When [125I]-PSTI was incubated with pure trypsin, chymotrypsin, elastase or enterokinase greater than 95% of tracer eluted in the position of PSTI-enzyme complex [23].
  • Unfortunately, the conditions necessary for the removal of the peptide by enterokinase resulted in incomplete protease digestion and substantial loss of NAT1 activity [24].
  • In contrast to these growth-promoting effects, administration of ghrelin reduced expression of mRNA for pepsin in the stomach and was without effect on expression of mRNA for enterokinase in the duodenum [25].
  • Full-length human genes for HDAC1 and HDAC3 were cloned into the pcDNA 3.1 vector containing a N-terminal His-tag with an enterokinase cleavage site [26].
  • We expressed human granzyme A in bacteria as a proenzyme capable of in vitro activation by enterokinase [27].

Analytical, diagnostic and therapeutic context of PRSS7


  1. Enterokinase and trypsin activities in pancreatic insufficiency and diseases of the small intestine. Lebenthal, E., Antonowicz, I., Shwachman, H. Gastroenterology (1976) [Pubmed]
  2. Spinesin/TMPRSS5, a novel transmembrane serine protease, cloned from human spinal cord. Yamaguchi, N., Okui, A., Yamada, T., Nakazato, H., Mitsui, S. J. Biol. Chem. (2002) [Pubmed]
  3. 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]
  4. Domains specifying thrombin-receptor interaction. Vu, T.K., Wheaton, V.I., Hung, D.T., Charo, I., Coughlin, S.R. Nature (1991) [Pubmed]
  5. Enterokinase (enteropeptidase): comparative aspects. Light, A., Janska, H. Trends Biochem. Sci. (1989) [Pubmed]
  6. Isolated congenital enterokinase deficiency. Recent findings and review of the literature. Ghishan, F.K., Lee, P.C., Lebenthal, E., Johnson, P., Bradley, C.A., Greene, H.L. Gastroenterology (1983) [Pubmed]
  7. Impact of different modalities of continuous venovenous hemofiltration on sepsis-induced alterations in experimental pancreatitis. Yekebas, E.F., Strate, T., Zolmajd, S., Eisenberger, C.F., Erbersdobler, A., Saalmüller, A., Steffani, K., Busch, C., Elsner, H.A., Engelhardt, M., Gillesen, A., Meins, J., The, M., Knoefel, W.T., Izbicki, J.R. Kidney Int. (2002) [Pubmed]
  8. Regulation of enterokinase synthesis in animal and human small intestine by luminal signals: its implication in upper gastrointestinal surgery. Bett, N.J. The British journal of surgery. (1979) [Pubmed]
  9. High-level production of human growth hormone in Escherichia coli by a simple recombinant process. Shin, N.K., Kim, D.Y., Shin, C.S., Hong, M.S., Lee, J., Shin, H.C. J. Biotechnol. (1998) [Pubmed]
  10. Gene expression analysis of cultured amniotic fluid cell with Down syndrome by DNA microarray. Chung, I.H., Lee, S.H., Lee, K.W., Park, S.H., Cha, K.Y., Kim, N.S., Yoo, H.S., Kim, Y.S., Lee, S. J. Korean Med. Sci. (2005) [Pubmed]
  11. Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains. Kitamoto, Y., Yuan, X., Wu, Q., McCourt, D.W., Sadler, J.E. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  12. cDNA sequence and chromosomal localization of human enterokinase, the proteolytic activator of trypsinogen. Kitamoto, Y., Veile, R.A., Donis-Keller, H., Sadler, J.E. Biochemistry (1995) [Pubmed]
  13. Developmental pattern of small intestinal enterokinase and disaccharidase activities in the human fetus. Antonowicz, I., Lebenthal, E. Gastroenterology (1977) [Pubmed]
  14. Protease specificity determination by using cellular libraries of peptide substrates (CLiPS). Boulware, K.T., Daugherty, P.S. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  15. Mutations in the proenteropeptidase gene are the molecular cause of congenital enteropeptidase deficiency. Holzinger, A., Maier, E.M., Bück, C., Mayerhofer, P.U., Kappler, M., Haworth, J.C., Moroz, S.P., Hadorn, H.B., Sadler, J.E., Roscher, A.A. Am. J. Hum. Genet. (2002) [Pubmed]
  16. Human angiogenin fused to human CD30 ligand (Ang-CD30L) exhibits specific cytotoxicity against CD30-positive lymphoma. Huhn, M., Sasse, S., Tur, M.K., Matthey, B., Schinköthe, T., Rybak, S.M., Barth, S., Engert, A. Cancer Res. (2001) [Pubmed]
  17. The cloned platelet thrombin receptor couples to at least two distinct effectors to stimulate phosphoinositide hydrolysis and inhibit adenylyl cyclase. Hung, D.T., Wong, Y.H., Vu, T.K., Coughlin, S.R. J. Biol. Chem. (1992) [Pubmed]
  18. Extended substrate specificity of rat mast cell protease 5, a rodent alpha-chymase with elastase-like primary specificity. Karlson, U., Pejler, G., Tomasini-Johansson, B., Hellman, L. J. Biol. Chem. (2003) [Pubmed]
  19. Biliary excretion of enterokinase in rats: studies in alcoholic rats with fatty liver. Grant, D.A., Terry, T.R., Hermon-Taylor, J. Gut (1983) [Pubmed]
  20. Mechanism for activation of mouse mast cell tryptase: dependence on heparin and acidic pH for formation of active tetramers of mouse mast cell protease 6. Hallgren, J., Karlson, U., Poorafshar, M., Hellman, L., Pejler, G. Biochemistry (2000) [Pubmed]
  21. Production and activation of recombinant hK2 with propeptide mutations resulting in high expression levels. Lövgren, J., Tian, S., Lundwall, A., Karp, M., Lilja, H. Eur. J. Biochem. (1999) [Pubmed]
  22. Inhibition of membrane-type serine protease 1/matriptase by natural and synthetic protease inhibitors. Yamasaki, Y., Satomi, S., Murai, N., Tsuzuki, S., Fushiki, T. J. Nutr. Sci. Vitaminol. (2003) [Pubmed]
  23. Interactions of pancreatic secretory trypsin inhibitor in small intestinal juice: its hydrolysis and protection by intraluminal factors. Freeman, T.C., Davies, R., Calam, J. Clin. Chim. Acta (1990) [Pubmed]
  24. Arylamine N-acetyltransferases. Expression in Escherichia coli, purification, and substrate specificities of recombinant hamster monomorphic and polymorphic isozymes. Wagner, C.R., Bergstrom, C.P., Koning, K.R., Hanna, P.E. Drug Metab. Dispos. (1996) [Pubmed]
  25. Influence of ghrelin on gastric and duodenal growth and expression of digestive enzymes in young mature rats. Warzecha, Z., Dembi??ski, A., Ceranowicz, P., Dembi??ski, M., Cieszkowski, J., Konturek, S.J., Polus, A., Pawlik, W.W., Kuwahara, A., Kato, I., Konturek, P.C. J. Physiol. Pharmacol. (2006) [Pubmed]
  26. Expression and functional characterization of recombinant human HDAC1 and HDAC3. Li, J., Staver, M.J., Curtin, M.L., Holms, J.H., Frey, R.R., Edalji, R., Smith, R., Michaelides, M.R., Davidsen, S.K., Glaser, K.B. Life Sci. (2004) [Pubmed]
  27. Recombinant human granzyme A binds to two putative HLA-associated proteins and cleaves one of them. Beresford, P.J., Kam, C.M., Powers, J.C., Lieberman, J. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  28. Immunofluorescent localisation of enterokinase in human small intestine. Hermon-Taylor, J., Perrin, J., Grant, D.A., Appleyard, A., Bubel, M., Magee, A.I. Gut (1977) [Pubmed]
  29. The apparent molecular weights of human intestinal aminopeptidase, enterokinase and maltase in native duodenal fluid. Magee, A.I., Grant, D.A., Hermon-Taylor, J. Biochem. J. (1977) [Pubmed]
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