Urokinase-type plasminogen activator is a preferred substrate of the human epithelium serine protease tryptase ε/PRSS22

Blood

Volumn 105, Issue 10, 2005, Pages 3893-3901

  Yasuda, Shinsuke ^b   Morokawa, Nasa ^b   Wong, G William ^b   Rossi, Andrea ^b   Madhusudhan, Mallur S ^b   Šali, Andrej ^b   Askew, Yuko S ^b   Adachi, Roberto ^b   Silverman, Gary A ^b   Krilis, Steven A ^b   Stevens, Richard L ^a  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; ARGININE; ASPARTIC ACID; CYSTEINE; ENZYME PRECURSOR; FIBRONECTIN; LAMININ; LYSINE; PLASMA PROTEIN; PLASMINOGEN ACTIVATOR; PROUROKINASE; RECOMBINANT PROTEIN; SECRETORY LEUKOCYTE PROTEINASE INHIBITOR; SINGLE CHAIN TISSUE TYPE PLASMINOGEN ACTIVATOR; TRYPTASE; TRYPTASE EPSILON; UNCLASSIFIED DRUG; UROKINASE; VITRONECTIN;

ANIMAL CELL; ARTICLE; BASEMENT MEMBRANE; CELL MIGRATION; CHROMOSOME 16P; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME SUBSTRATE; EPITHELIUM CELL; EXOCYTOSIS; EXTRACELLULAR MATRIX; FIBRINOLYSIS; HUMAN; HUMAN CELL; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FUNCTION; REGULATORY MECHANISM; SITE DIRECTED MUTAGENESIS;

EID: 20844432525     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2003-10-3501     Document Type: Article

References (48)

1. Wong GW, Yasuda S, Madhusudhan MS, et al. Human tryptase ε (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.
2. Miller JS, Westin EH, Schwartz LB. Cloning and characterization of complementary DNA for human tryptase. J Clin Invest. 1939;84:1188-1195.
3. Miller JS, Moxley G, Schwartz LB. Cloning and characterization of a second complementary DNA for human tryptase. J Clin Invest. 1990;86:864-870.
4. Vanderslice P, Ballinger SM, Tam EK, et al. Human mast cell tryptase: multiple cDNAs and genes reveal a multi-gene serine protease family. Proc Natl Acad Sci U S A. 1990;87:3811-3815.
5. Inoue M, Kanbe N, Kurosawa M, Kido H. Cloning and tissue distribution of a novel serine protease Esp-1 from human eosinophils. Biochem Biophys Res Commun. 1998;252:307-312.
6. Inoue M, Isobe M, Itoyama T, Kido H. Structural analysis of Esp-1 gene. Biochem Biophys Res Commun. 1999;266:564-568.
7. Pallaoro M, Fejzo MS, Shayesteh L, Blount JL, Caughey GH. Characterization of genes encoding known and novel human mast cell tryptases on chromosome 16p13.3. J Biol Chem. 1999;274:3355-3362.
8. Hooper JD, Nicol DL, Dickinson JL, et al. Testisin, a new human serine proteinase expressed by premeiotic testicular germ cells and lost in testicular germ cell tumors. Cancer Res. 1999;59:3199-3205.
9. Wong GW, Tang Y, Feyfant E, et al. Identification of a new member of the tryptase family of mouse and human mast cell proteases that possesses a novel C-terminal hydrophobic extension. J Biol Chem. 1999;274:30734-30793.
10. Caughey GH, Raymond WW, Blount JL, et al. Characterization of human γ tryptases, novel members of the chromosome 16p mast cell tryptase and prostasin gene families. J Immunol. 2000;164:6566-6575.
11. Bhagwandin VJ, Hau LW, Mallen-St Clair J, Wolters PJ, Caughey GH. Structure and activity of human pancreasin, a novel tryptic serine peptidase expressed primarily by the pancreas. J Biol Chem. 2003;278:3363-3371.
12. Chen C, Darrow AL, Qi JS, D'Andrea MR, Andrade-Gordon P. A novel serine protease predominately expressed in macrophages. Biochem J. 2003;374:97-107.
13. Wong GW, Yasuda S, Morokawa N, Li L, Stevens RL. Mouse chromosome 17A3.3 contains thirteen genes that encode functional tryptic-like serine proteases with distinct tissue and cell expression patterns. J Biol Chem. 2004;279:2438-2452.
14. Johnson DA, Barton GJ. Mast cell tryptases: examination of unusual characteristics by multiple sequence alignment and molecular modeling. Protein Sci. 1992;1:370-377.
15. Matsumoto R, Šali A, Ghildyal N, Karplus M, Stevens RL. Packaging of proteases and proteoglycans in the granules of mast cells and other hematopoietic cells: a cluster of histidines on mouse mast cell protease 7 regulates its binding to heparin serglycin proteoglycans. J Biol Chem. 1995;270:19524-19531.
16. Ghildyal N, Friend DS, Stevens RL, et al. Fate of two mast cell tryptases in V3 mastocytosis and normal BALB/c mice undergoing passive systemic anaphylaxis: prolonged retention of exocytosed mMCP-6 in connective tissues, and rapid accumulation of enzymatically active mMCP-7 in the blood. J Exp Med. 1996;184:1061-1073.
17. Pereira PJ, Bergner A, Macedo-Ribeiro S, et al. Human β-tryptase is a ring-like tetramer with active sites facing a central pore. Nature. 1998;392:306-311.
18. Marquardt U, Zettl F, Huber R, Bode W, Sommerhoff C. The crystal structure of human α1-tryptase reveals a blocked substrate-binding region. J Mol Biol. 2002;321:491-502.
19. Huang C, Li L, Krilis SA, et al. Human tryptases α and βII are functionally distinct due, in part, to a single amino acid difference in one of the surface loops that forms the substrate-binding cleft. J Biol Chem. 1999;274:19670-19676.
20. Echtenacher B, Männel DN, Hültner L. Critical protective role of mast cells in a model of acute septic peritonitis. Nature. 1996;381:75-77.
21. Abraham SN, Thankavel K, Malaviya R. Mast cells as modulators of host defense in the lung. Front Biosci. 1997;2:d78-d87.
22. Maurer M, Echtenacher B, Hultner L, et al. The c-kit ligand, stem cell factor, can enhance innate immunity through effects on mast cells. J Exp Med. 1998;188:2343-2348.
23. Huang C, De Sanctis GT, O'Brien PJ, et al. Evaluation of the substrate specificity of human mast cell tryptase βI and demonstration of its importance in bacterial infections of the lung. J Biol Chem. 2001;276:26276-26284.
24. Huang C, Wong GW, Ghildyal N, et al. The tryptase, mouse mast cell protease 7, exhibits anticoagulant activity in vivo and in vitro due to its ability to degrade fibrinogen in the presence of the diverse array of protease inhibitors in plasma. J Biol Chem. 1997;272:31885-31893.
25. Huang C, Friend DS, Qiu WT, et al. Induction of a selective and persistent extravasation of neutrophils into the peritoneal cavity by tryptase mouse mast cell protease 6. J Immunol. 1998;160:1910-1919.
26. Hallgren J, Karlson U, Poorafshar M, Hellman L, Pejler G. 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. Biochemistry. 2000;39:13068-13077.
27. Badge RM, Yardley J, Jeffreys AJ, Armour JA. Crossover breakpoint mapping identifies a subtelomeric hotspot for male meiotic recombination. Hum Mol Genet. 2000;9:1239-1244.
28. Gyetko MR, Sud S, Chen GH, et al. Urokinase-type plasminogen activator is required for the generation of a type 1 immune response to pulmonary Cryptococcus neoformans infection. J Immunol. 2002;168:801-809.
29. Gyetko MR, Aizenberg D, Mayo-Bond L. Urokinase-deficient and urokinase receptor-deficient mice have impaired neutrophil antimicrobial activation in vitro. J Leukoc Biol. 2004;76:648-656.
30. Wong GW, Li L, Madhusudhan MS, et al. Tryptase 4, a new member of the chromosome 17 family of mouse serine proteases. J Biol Chem. 2001;276:20648-20658.
31. Wong GW, Foster PS, Yasuda S, et al. Biochemical and functional characterization of human transmembrane tryptase (TMT)/tryptase γ: TMT is an exocytosed mast cell protease that induces airway hyperresponsiveness in vivo via an IL-13/IL14Rα/STAT6-dependent pathway. J Biol Chem. 2002;277:41906-41915.
32. Jung G, Ueno H, Hayashi R. Carboxypeptidase Y: Structural basis for protein sorting and catalytic triad. J Biochem (Tokyo). 1999;126:1-6.
33. Rudenko G, Bonten E, d'Azzo A, Hol WG. Three-dimensional structure of the human protective protein: structure of the precursor form suggests a complex activation mechanism. Structure. 1995;3:1249-1259.
34. Šali A, Blundell TL. Comparative protein modeling by satisfaction of spatial restraints. J Mol Biol. 1993;234:779-815.
35. Bolognesi M, Gatti G, Menagatti E, et al. Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 Å resolution: structure solution, crystallographic refinement and preliminary structural interpretation. J Mol Biol. 1982;162:839-868.
36. Marquant M, Walter J, Deisenhofer J, Bode W, Huber R. The geometry of the reactive site and of the peptide groups in trypsin, trypsiongen, and its complexes with inhibitors. Acta Crystallogr. 1983;39(sect B):480-490.
37. Rocchia W, Alexov E, Honig B. Extending the applicability of the nonlinear Poisson-Boltzmann equation: multiple dielectric constants and multivalent ions. J Phys Chem B. 2001;105:6507-6514.
38. Rocchia W, Sridharan S, Nicholls A, et al. Rapid grid-based construction of the molecular surface and the use of induced surface charge to calculate reaction field energies: applications to the molecular systems and geometric objects. J Comput Chem. 2002;23:128-137.
39. Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph. 1996;14:51-32.
40. Carmeliet P, Moons L, Herbert JM, et al. Urokinase but not tissue plasminogen activator mediates arterial neointima formation in mice. Circ Res. 1997;81:829-839.
41. Clowes AW, Clowes MM, Au YP, Reidy MA, Belin D. Smooth muscle cells express urokinase during mitogenesis and tissue-type plasminogen activator during migration in injured rat carotid artery. Circ Res. 1990;67:61-67.
42. Yamada K, Takabatake Y, Takabatake T, Takeshima K. The early expression control of Xepsin by nonaxial and planar posteriorizing signals in Xenopus epidermis. Dev Biol. 1999;214:318-330.
43. Bugge TH, Flick MJ, Daugherty CC, Degen JL. Plasminogen deficiency causes severe thrombosis but is compatible with development and reproduction. Genes Dev. 1995;9:794-807.
44. Blasi F, Carmeliet P. uPAR: a versatile signalling orchestrator. Nat Rev Mol Cell Biol. 2002;3:932-943.
45. Kjoller L. The urokinase plasminogen activator receptor in the regulation of the actin cytoskeleton and cell motility. Biol Chem. 2002;383:5-19.
46. Black JL, Johnson PR. Factors controlling smooth muscle proliferation and airway remodelling. Curr Opin Allergy Clin Immunol. 2002;2:47-51.
47. Stepanova V, Mukhina S, Kohler E, et al. Urokinase plasminogen activator induces human smooth muscle cell migration and proliferation via distinct receptor-dependent and proteolysis-dependent mechanisms. Mol Cell Biochem. 1999;195:199-206.
48. Pluskota E, Soloviev DA, Plow EF. Convergence of the adhesive and fibrinolytic systems: recognition of urokinase by integrin αMβ2 as well as by the urokinase receptor regulates cell adhesion and migration. Blood. 2003;101:1582-1590.