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Gene Review

TMPRSS15  -  transmembrane protease, serine 15

Bos taurus

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Disease relevance of PRSS7


High impact information on PRSS7

  • Cloning and functional expression of a cDNA encoding the catalytic subunit of bovine enterokinase [2].
  • Enterokinase (enteropeptidase) is a heterodimeric serine protease that is responsible for the physiological activation of trypsinogen by highly specific cleavage of the trypsinogen activation peptide following the sequence (Asp)4-Lys [2].
  • Incubation of the soybean phospholipid and brush-border membrane vesicles with papain released the exposed molecules of enterokinase [3].
  • Enterokinase is predominantly present as membrane fragments which must be treated with Triton X-100 to release the enzyme [4].
  • The properties of enterokinase in phospholipid vesicles were compared with those of alkaline phosphatase, which was also added to the reconstitution system, and with the enzyme activities present in vesicles prepared from brush-border membranes [3].

Biological context of PRSS7

  • Enterokinase and alkaline phosphatase had their active sites exposed to substrate in the brush-border membrane vesicles [3].
  • Of the zymogens of the serine proteases tested, including several of those involved in blood coagulation, only native and guanidinated trypsinogen are acitvated by enterokinase, whereas acetylated trypsinogen is not [5].
  • Partial heat denaturation of bovine enterokinase causes a differential response toward the activation of trypsinogen and the hydrolysis of benzoyl-L-arginine ethyl ester (BZArgOEt), further suggesting that secondary sites are important in the binding of trypsinogen [5].
  • Hormonal combination of insulin (17 nmol.l(-1)) plus cortisol (138 nmol.l(-1)) or insulin plus recombinant enterokinase linker bST (4.5 nmol.l(-1) increased lipogenesis (P<0.05) [6].

Anatomical context of PRSS7


Associations of PRSS7 with chemical compounds

  • Enterokinase hydrolyzed lysine and arginine substrates and slowly reacted with the trypsin active site titrant 4-methylumbelliferyl-p-guanidinobenzoate [7].
  • We altered the trypsinogen native propeptide sequence by replacing the lysine at position 6 with an aspartic acid, thus destroying the site in the propeptide cleaved by enterokinase and by trypsin [10].
  • The recombinant intact EK catalytic subunit was purified to homogeneity with a specific activity of 720 AUs/mg protein through ammonium sulfate precipitation, DEAE chromatography, and gel filtration [1].
  • After the his-tagged apo-NCS protein had been purified and cleaved with enterokinase, the binding properties of the recombinant protein as to ethidium bromide (EtBr) were studied by monitoring of total fluorescence intensity and fluorescence polarization with a BEACON 2000 system and GraphPad Prism software [11].

Regulatory relationships of PRSS7


Other interactions of PRSS7

  • Upon proteolytic digestion of GIP with the staphylococcal V8 protease and with enterokinase, two fragments are formed in each case, corresponding to GIP1-3, GIP4-42, and GIP1-16, GIP17-42, respectively [12].
  • Milk production, plasma bovine somatotropin (bST) and insulin-like growth factor I (IGF-I) were measured in dairy cows following a single subcutaneous injection of a slowly released preparation of either recombinant enterokinase linker bST (somidobove: 640 mg) or recombinant methionyl bST (sometribove: 500 mg) [13].

Analytical, diagnostic and therapeutic context of PRSS7


  1. Expression, purification, and characterization of a biologically active bovine enterokinase catalytic subunit in Escherichia coli. Yuan, L.D., Hua, Z.C. Protein Expr. Purif. (2002) [Pubmed]
  2. Cloning and functional expression of a cDNA encoding the catalytic subunit of bovine enterokinase. LaVallie, E.R., Rehemtulla, A., Racie, L.A., DiBlasio, E.A., Ferenz, C., Grant, K.L., Light, A., McCoy, J.M. J. Biol. Chem. (1993) [Pubmed]
  3. Incorporation of bovine enterokinase in reconstituted soybean phospholipid vesicles. Fonseca, P., Light, A. J. Biol. Chem. (1983) [Pubmed]
  4. The purification and characterization of bovine enterokinase from membrane fragments in the duodenal mucosal fluid. Fonseca, P., Light, A. J. Biol. Chem. (1983) [Pubmed]
  5. Bovine enterokinase. Purification, specificity, and some molecular properties. Anderson, L.E., Walsh, K.A., Neurath, H. Biochemistry (1977) [Pubmed]
  6. Chronic effects of somatotropin treatment in vivo and in vitro on lipogenic activity of goat adipose tissue in a glucose-free buffer during acute incubation. Skarda, J. Physiological research / Academia Scientiarum Bohemoslovaca. (1999) [Pubmed]
  7. The preparation and properties of bovine enterokinase. Liepnieks, J.J., Light, A. J. Biol. Chem. (1979) [Pubmed]
  8. An analysis of mutagens in the contents of the biliary tract in pancreaticobiliary maljunction. Mizuno, M., Kato, T., Koyama, K. Surgery today. (1996) [Pubmed]
  9. Production of recombinant bovine enterokinase catalytic subunit in Escherichia coli using the novel secretory fusion partner DsbA. Collins-Racie, L.A., McColgan, J.M., Grant, K.L., DiBlasio-Smith, E.A., McCoy, J.M., LaVallie, E.R. Biotechnology (N.Y.) (1995) [Pubmed]
  10. A single mutation in the activation site of bovine trypsinogen enhances its accumulation in the fermentation broth of the yeast Pichia pastoris. Hanquier, J., Sorlet, Y., Desplancq, D., Baroche, L., Ebtinger, M., Lefèvre, J.F., Pattus, F., Hershberger, C.L., Vertès, A.A. Appl. Environ. Microbiol. (2003) [Pubmed]
  11. Design, production, and characterization of recombinant neocarzinostatin apoprotein in Escherichia coli. Nozaki, S., Tomioka, Y., Hishinuma, T., Inoue, M., Nagumo, Y., Tsuruta, L.R., Hayashi, K., Matsumoto, T., Kato, Y., Ishiwata, S., Itoh, K., Suzuki, T., Hirama, M., Mizugaki, M. J. Biochem. (2002) [Pubmed]
  12. A novel form of gastric inhibitory polypeptide (GIP) isolated from bovine intestine using a radioreceptor assay. Fragmentation with staphylococcal protease results in GIP1-3 and GIP4-42, fragmentation with enterokinase in GIP1-16 and GIP17-42. Carlquist, M., Maletti, M., Jörnvall, H., Mutt, V. Eur. J. Biochem. (1984) [Pubmed]
  13. Plasma profiles of somatotropin and IGF-I in diary cows following application of two preparations of recombinant bovine somatotropin in a sustained release vehicle. Slaba, J., Krejcí, P., Skarda, J., Huybrechts, L.M., Decuypere, E., Herrmann, H. Physiological research / Academia Scientiarum Bohemoslovaca. (1994) [Pubmed]
  14. Refolding of the mixed disulfide of bovine trypsinogen and glutathione. Odorzynski, T.W., Light, A. J. Biol. Chem. (1979) [Pubmed]
  15. A direct high-performance liquid chromatography assay of the enzymatic activity of enterokinase (enteropeptidase). Janska, H., Light, A. Anal. Biochem. (1989) [Pubmed]
  16. Expression of a cold-adapted fish trypsin in Pichia pastoris. Macouzet, M., Simpson, B.K., Lee, B.H. FEMS Yeast Res. (2005) [Pubmed]
  17. Prokaryotic expression of Chinese bovine enterokinase catalytic subunit. Huang, H., Zhao, Y., Yi-ru, G. Chin. Med. J. (2004) [Pubmed]
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