These findings contribute to define the growing group of human polyserine proteases …

• Abstract
• Background
• Results
• Discussion
• Conclusion
• Methods
• Abbreviations
• References
• Figures

1. Liu L, Wilson T, Hastings JW: Molecular evolution of dinoflagellate luciferases, enzymes with three catalytic domains in a single polypeptide.

   Proc Natl Acad Sci U S A 2004, 101:16555-16560.

2. Eberhardt RY, Gilbert HJ, Hazlewood GP: Primary sequence and enzymic properties of two modular endoglucanases, Cel5A and Cel45A, from the anaerobic fungus Piromyces equi.

   Microbiology 2000, 146 ( Pt 8):1999-2008.

3. Cal S, Quesada V, Llamazares M, Diaz-Perales A, Garabaya C, Lopez-Otin C: Human polyserase-2, a novel enzyme with three tandem serine protease domains in a single polypeptide chain.

   J Biol Chem 2005, 280:1953-1961.

4. Li L, Hong R, Hastings JW: Three functional luciferase domains in a single polypeptide chain.

   Proc Natl Acad Sci U S A 1997, 94:8954-8958.

5. Ouwendijk J, Peters WJ, van de Vorstenbosch RA, Ginsel LA, Naim HY, Fransen JA: Routing and processing of lactase-phlorizin hydrolase in transfected Caco-2 cells.

   J Biol Chem 1998, 273:6650-6655.

6. Tsai HJ: Functional organization and evolution of mammalian hexokinases: mutations that caused the loss of catalytic activity in N-terminal halves of type I and type III isozymes.

   Arch Biochem Biophys 1999, 369:149-156.

7. Marrone L, McAllister KA, Clarke AJ: Characterization of function and activity of domains A, B and C of xylanase C from Fibrobacter succinogenes S85.

   Protein Eng 2000, 13:593-601.

8. Howard MB, Ekborg NA, Taylor LE, Weiner RM, Hutcheson SW: Chitinase B of "Microbulbifer degradans" 2-40 contains two catalytic domains with different chitinolytic activities.

   J Bacteriol 2004, 186:1297-1303.

9. Cal S, Quesada V, Garabaya C, Lopez-Otin C: Polyserase-I, a human polyprotease with the ability to generate independent serine protease domains from a single translation product.

   Proc Natl Acad Sci U S A 2003, 100:9185-9190.

10. Wei L, Clauser E, Alhenc-Gelas F, Corvol P: The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors.

    J Biol Chem 1992, 267:13398-13405.

11. Novikova EG, Eng FJ, Yan L, Qian Y, Fricker LD: Characterization of the enzymatic properties of the first and second domains of metallocarboxypeptidase D.

    J Biol Chem 1999, 274:28887-28892.

12. Lopez-Otin C, Overall CM: Protease degradomics: a new challenge for proteomics.

    Nat Rev Mol Cell Biol 2002, 3:509-519.

13. Puente XS, Sanchez LM, Overall CM, Lopez-Otin C: Human and mouse proteases: a comparative genomic approach.

    Nat Rev Genet 2003, 4:544-558.

14. Puente XS, Lopez-Otin C: A genomic analysis of rat proteases and protease inhibitors.

    Genome Res 2004, 14:609-622.

15. Puente XS, Gutierrez-Fernandez A, Ordonez GR, Hillier LW, Lopez-Otin C: Comparative genomic analysis of human and chimpanzee proteases.

    Genomics 2005, 86:638-647.

16. Lindsay LL, Yang JC, Hedrick JL: Ovochymase, a Xenopus laevis egg extracellular protease, is translated as part of an unusual polyprotease.

    Proc Natl Acad Sci U S A 1999, 96:11253-11258.

17. Hiyoshi M, Takamune K, Mita K, Kubo H, Sugimoto Y, Katagiri C: Oviductin, the oviductal protease that mediates gamete interaction by affecting the vitelline coat in Bufo japonicus: its molecular cloning and analyses of expression and posttranslational activation.

    Dev Biol 2002, 243:176-184.

18. Krem MM, Di Cera E: Molecular markers of serine protease evolution.

    Embo J 2001, 20:3036-3045.

19. Ross J, Jiang H, Kanost MR, Wang Y: Serine proteases and their homologs in the Drosophila melanogaster genome: an initial analysis of sequence conservation and phylogenetic relationships.

    Gene 2003, 304:117-131.

20. Yu JX, Chao L, Ward DC, Chao J: Structure and chromosomal localization of the human prostasin (PRSS8) gene.

    Genomics 1996, 32:334-340.

21. Hooper JD, Clements JA, Quigley JP, Antalis TM: Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes.

    J Biol Chem 2001, 276:857-860.

22. Fiorucci L, Ascoli F: Mast cell tryptase, a still enigmatic enzyme.

    Cell Mol Life Sci 2004, 61:1278-1295.

23. Wong GW, Yasuda S, Morokawa N, Li L, Stevens RL: Mouse chromosome 17A3.3 contains 13 genes that encode functional tryptic-like serine proteases with distinct tissue and cell expression patterns.

    J Biol Chem 2004, 279:2438-2452.

24. Netzel-Arnett S, Hooper JD, Szabo R, Madison EL, Quigley JP, Bugge TH, Antalis TM: Membrane anchored serine proteases: a rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer.

    Cancer Metastasis Rev 2003, 22:237-258.

25. Hooper JD, Campagnolo L, Goodarzi G, Truong TN, Stuhlmann H, Quigley JP: Mouse matriptase-2: identification, characterization and comparative mRNA expression analysis with mouse hepsin in adult and embryonic tissues.

    Biochem J 2003, 373:689-702.

26. Velasco G, Cal S, Quesada V, Sánchez LM, López-Otín C: Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins.

    J Biol Chem 2002, 277:37637-37646.

27. Yu JX, Chao L, Chao J: Prostasin is a novel human serine proteinase from seminal fluid. Purification, tissue distribution, and localization in prostate gland.

    J Biol Chem 1994, 269:18843-18848.

28. Caughey GH, Raymond WW, Blount JL, Hau LW, Pallaoro M, Wolters PJ, Verghese GM: Characterization of human gamma-tryptases, novel members of the chromosome 16p mast cell tryptase and prostasin gene families.

    J Immunol 2000, 164:6566-6575.

29. Caughey GH: New developments in the genetics and activation of mast cell proteases.

    Mol Immunol 2002, 38:1353-1357.

30. Wong GW, Yasuda S, Madhusudhan MS, Li L, Yang Y, Krilis SA, Sali A, Stevens RL: Human tryptase epsilon (PRSS22), a new member of the chromosome 16p13.3 family of human serine proteases expressed in airway epithelial cells.

    J Biol Chem 2001, 276:49169-49182.

31. Sommerhoff CP, Bode W, Pereira PJ, Stubbs MT, Sturzebecher J, Piechottka GP, Matschiner G, Bergner A: The structure of the human betaII-tryptase tetramer: fo(u)r better or worse.

    Proc Natl Acad Sci U S A 1999, 96:10984-10991.

32. Bode W, Schwager P: The single calcium-binding site of crystallin bovin beta-trypsin.

    FEBS Lett 1975, 56:139-143.

33. [[http://www.expasy.ch]]

34. Cal S, Freije JM, López JM, Takada Y, López-Otín C: ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the alphavbeta3 integrin through an RGD-independent mechanism.

    Mol Biol Cell 2000, 11:1457-1469.

35. Takeuchi T, Shuman MA, Craik CS: Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue.

    Proc Natl Acad Sci U S A 1999, 96:11054-11061.

36. Huang C, Morales G, Vagi A, Chanasyk K, Ferrazzi M, Burklow C, Qiu WT, Feyfant E, Sali A, Stevens RL: Formation of enzymatically active, homotypic, and heterotypic tetramers of mouse mast cell tryptases. Dependence on a conserved Trp-rich domain on the surface.

    J Biol Chem 2000, 275:351-358.

37. Raymond WW, Tam EK, Blount JL, Caughey GH: Purification and characterization of dog mast cell protease-3, an oligomeric relative of tryptases.

    J Biol Chem 1995, 270:13164-13170.

38. [[http://www.hgmp.mrc.ac.uk]]

39. Sakai K, Ren S, Schwartz LB: A novel heparin-dependent processing pathway for human tryptase. Autocatalysis followed by activation with dipeptidyl peptidase I.

    J Clin Invest 1996, 97:988-995.

40. Wolters PJ, Pham CT, Muilenburg DJ, Ley TJ, Caughey GH: Dipeptidyl peptidase I is essential for activation of mast cell chymases, but not tryptases, in mice.

    J Biol Chem 2001, 276:18551-18556.

41. Tomita H, Nagamitsu S, Wakui K, Fukushima Y, Yamada K, Sadamatsu M, Masui A, Konishi T, Matsuishi T, Aihara M, Shimizu K, Hashimoto K, Mineta M, Matsushima M, Tsujita T, Saito M, Tanaka H, Tsuji S, Takagi T, Nakamura Y, Nanko S, Kato N, Nakane Y, Niikawa N: Paroxysmal kinesigenic choreoathetosis locus maps to chromosome 16p11.2-q12.1.

    Am J Hum Genet 1999, 65:1688-1697.

42. Disse S, Abergel E, Berrebi A, Houot AM, Le Heuzey JY, Diebold B, Guize L, Carpentier A, Corvol P, Jeunemaitre X: Mapping of a first locus for autosomal dominant myxomatous mitral-valve prolapse to chromosome 16p11.2-p12.1.

    Am J Hum Genet 1999, 65:1242-1251.

43. Borgono CA, Diamandis EP: The emerging roles of human tissue kallikreins in cancer.

    Nat Rev Cancer 2004, 4:876-890.

44. Frandsen TL, Holst-Hansen C, Nielsen BS, Christensen IJ, Nyengaard JR, Carmeliet P, Brunner N: Direct evidence of the importance of stromal urokinase plasminogen activator (uPA) in the growth of an experimental human breast cancer using a combined uPA gene-disrupted and immunodeficient xenograft model.

    Cancer Res 2001, 61:532-537.

45. Guex N, Peitsch MC: SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling.

    Electrophoresis 1997, 18:2714-2723.