Trichuris suis: A secretory chymotrypsin/elastase inhibitor with potential as an immunomodulator

Experimental Parasitology

Volumn 95, Issue 1, 2000, Pages 36-44

  Rhoads, M L ^a   Fetterer, R H ^a   Hill, D E ^a   Urban Jr , J F ^a  

^a AGRICULTURAL RESEARCH SERVICE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN G; CHYMASE; CHYMOTRYPSIN INHIBITOR; ELASTASE INHIBITOR; IMMUNOMODULATING AGENT; LEUKOCYTE ELASTASE; THROMBIN INHIBITOR;

AMINO ACID SEQUENCE; ARTICLE; DOWN REGULATION; DRUG PURIFICATION; HOST RESISTANCE; IMMUNE RESPONSE; IMMUNOMODULATION; NONHUMAN; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; TRICHURIS;

ANISAKIS SIMPLEX; ANURA; APIS MELLIFERA; ASCARIS SUUM; BOMBINA BOMBINA; NEMATODA; RANA TEMPORARIA; SUS SCROFA; TRICHURIS SUIS;

EID: 0034088301     PISSN: 00144894     EISSN: None     Source Type: Journal    
DOI: 10.1006/expr.2000.4502     Document Type: Article

References (41)

1. Bania J., Stachowiak D., Polanowski A. Primary structure and properties of the cathepsin G/chymotrypsin inhibitor from the larval hemolymph of Apis mellifera. European Journal of Biochemistry. 262:1999;680-687.
2. Bieth J. Some kinetic consequences of the tight binding of protein-proteinase-inhibitors to proteolytic enzymes and their application to the determination of dissociation constants. Bayer Symposium V: Proteinase Inhibitors. 1974;Springer-Verlag, Berlin/New York. p. 463-469.
3. Blaxter M. L., Ingram L., Tweedie S. Sequence, expression and evolution of the globins of the parasitic nematode Nippostrongy lus brasiliensis. Molecular and Biochemical Parasitology. 68:1994;1-14.
4. 1-Proteinase inhibitor, antichymotrypsin, and a recombinant hybrid mutant of antichmotrypsin (LEX032) modulate neutrophil adhesion interactions. Journal of Leukocyte Biology. 63:1998;75-82.
5. 2 formation by activated human polymorphonuclear leukocytes. Carcinogenesis. 8:1987;1207-1212.
6. Grasberger B. L., Clore G. M., Gronenborn A. M. High-resolution structure of Ascaris trypsin inhibitor in solution: Direct evidence for a pH-induced conformational transition in the reactive site. Structure. 2:1994;669-678.
7. Hawley J. H., Martzen M. R., Peanasky R. J. Proteinase inhibitors in Ascarida. Parasitology Today. 10:1994;308-313.
8. He S., Walls A. F. Human mast cell chymase induces the accumulation of neutrophils, eosinophils and other inflammatory cells in vivo. British Journal of Pharmacology. 125:1998;1491-1500.
9. Hill D. E., Gamble H. R., Rhoads M. L., Fetterer R. H., Urban J. F. Jr. Trichuris suis: A zinc metalloprotease from culture fluids of adult parasites. Experimental Parasitology. 77:1993;170-178.
10. Hill D. E., Sakanari J. A. Trichuris suis: Thiol protease activity from adult worms. Experimental Parasitology. 85:1997;55-62.
11. Hook J., Weinbaum G., Oppenheim D., Bai C., Deren J. J., Rubin H., Sands H. Novel modified recombinant human alpha-1 antichymotrypsin (LEX032) inhibits inflammation as determined by neutrophil recruitment in vivo. FASEB Journal. 9:1995;A965.
12. Huang K., Strynadka N. C. J., Bernard V. D., Peanasky R. J., James M. N. G. The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Structure. 2:1994;679-689.
13. Hunt J. E., Stevens R. L. Mouse mast cell proteases. Kitamura Y., Yamamoto S., Galli S. J., Greaves M. W. Biological and Molecular Aspects of Mast Cell and Basophil Differentiation. 1995;149-160 Raven Press, New York.
14. Kennedy A. R. Chemopreventive agents: Protease inhibitors. Pharmacology Therapy. 78:1998;176-209.
15. Kozak M. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell. 44:1986;283-292.
16. 1-antichymotrypsin and human leukocyte cathepsin G: Complex formation and production of a modified nhibitor. Biochemical and Biophysical Research Communication. 105:1982;186-193.
17. Larionova N. I., Gladysheva I. P., Tikhonova T. V., Kazanskaya N. F. Inhibition of cathepsin G and human granulocyte elastase by mutiple forms of Bowman-Birk type soybean inhibitor. Biokhimiya. 58:1994;1437-1444.
18. Lu C. C., Nguyen T., Morris S, Hill D., Sakanari J. A. Anisakis simplex: Mutational bursts in the reactive site centers of serine protease inhibitors from an Ascarid nematode. Experimental Parasitology. 89:1998;257-261.
19. Macen J. L., Upton C., Nation N., McFadden G. SERP1, a serine proteinase inhibitor encoded by myxoma virus, is a secreted glycoprotein that interferes with inflammation. Virology. 195:1993;348-363.
20. Mansfield L. S., Urban J. F. Jr. The pathogenesis of necrotic proliferative colitis in swine is linked to whipworm induced suppression of mucosal immunity to resident bacteria. Veterinary Immunology and Immunopathology. 50:1996;1-17.
21. Mignogna G., Pascarella S., Wechselberger C., Hinterleitner C., Mollay C., Amiconi G., Barra D., Kreil G. BSTI, a trypsin inhibitor from skin secretions of Bombina bombina related to protease inhibitors of nematodes. Protein Science. 5:1996;357-362.
22. Miller H. R. P. The protective mucosal response against gastroin testinal nematodes in ruminants and laboratory animals. Veterinary Immunology and Immunopathology. 6:1984;176-259.
23. Miller H. R. P. Mucosal mast cells and the allergic response against nematode parasites. Veterinary Immunology and Immunopathology. 54:1996;331-336.
24. Mizutani H., Schechter N. M., Lazarus G., Black R. A., Kupper T. S. Rapid and specific conversion of precursor interleukin 1β (IL-1β) to an active IL-1 species by human mast cell chymase. Journal of Experimental Medicine. 174:1991;821-825.
25. Murohara T., Guo J., Lefer A. M. Cardioprotection by a novel recombinant serine protease inhibitor in myocardial ischemia and reperfusion injury. Journal of Pharmacological Experimental Therapy. 274:1995;1246-1253.
26. Peanasky R. J., Martzen M. R., Homandberg G. A., Cash J. M., Babin D. R., Litweiler B. Proteinase inhibitors from intestinal parasitic helminths: Structure and indications of some possible functions. MacInnis A. J. Molecular Paradigms for Eradicating Helminthic Parasites. 1987;349-366 A. R. Liss, New York.
27. Ray C. A., Black R. A., Kronheim S. R., Greenstreet T. A., Sleath P. R., Salvesen G. S., Pickup D. J. Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1β converting enzyme. Cell. 69:1992;597-604.
28. Reynolds D. S., Stevens R. L., Lane W. S., Carr M. H., Austen K. F., Serafin W. E. Different mouse mast cell populations express various combinations of at least six distinct mast cell serine proteases. Proceedings of the National Academy of Science USA. 87:1990;3230-3234.
29. Rhoads M. L., Fetterer R. H., Hill D. E. Trichuris suis: A secretory serine protease inhibitor. Experimental Parasitology. 94:2000;1-7.
30. Scalia R., Gauthier T. W., Lefer A. M. Beneficial effects of LEX032, a novel recombinant serine protease inhibitor, in murine traumatic shock. Shock. 4:1995;251-256.
31. Schwartz L. B., Austen K. F. Structure and function of the chemical mediators of mast cells. Progress in Allergy. 34:1984;271-321.
32. Scudamore C. L., Jepson M. A., Hirst B. H., Miller H. R. P. The rat mucosal mast cell chymase, RMCP-II, alters epithelial cell monolayer permeability in association with altered distribution of the tight junction proteins ZO-1 and occludin. European Journal of Cell Biology. 75:1998;321-330.
33. Stevens R., Friend D., DeSanctis G., Huang C. Mast cells (MC) express multiple tryptases to independently control the extravasation of neutrophils and eosinophils into tissues. Type 2 Cytokines in Allergy and Helminthic Infections. 1999;Keystone Symposia, Tahoe.
34. Stevens R. L., Friend D. S., McNeil H. P., Schiller V., Ghildyal N., Austen K. F. Strain specific and tissue specific expression of mouse mast cell secretory granule proteases. Proceedings of the National Academy of Science USA. 91:1994;128-132.
35. Stoschek C. M. Quantitation of protein. Deutscher M. P. Methods of Enzymology. 182:1990;50-68 Academic Press, San Diego.
36. Urban J. F. Jr., Mansfield L. S., Shea-Donohue T., Gause W. C., Finkelman F. D. Mechanisms of the intestinal immunity to nematode parasites and the consequences to invasion by opportunistic bacteria. Heidt P. J., Cebra J. C., Rusch V. D., Van der Waaij D., Walker R. I. Old Herborn University Seminar Monograph II: Immunomodulation of the Gastrointestinal Mucosa. 1998;59-69 Herborn Letterae, Herborn-Dill.
37. Von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Research. 14:1986;4683-4691.
38. Walls A. F., He S., Teran L., Holgate S. T. Mast cell proteases as mediators of vascular leakage and cell accumulation. Journal of Allergy and Clinical Immunology. 91:1993;256.
39. Ware J. H., Wan X. S., Rubin H., Schechter N. M., Kennedy A. R. Soybean Bowman-Birk protease inhibitor is a highly effective inhibitor of human mast cell chymase. Archives of Biochemistry and Biophysics. 344:1997;133-138.
40. Wastling J. M., Scudamore C. L., Thornton E. M., Newlands G. F. J., Miller H. R. P. Constitutive expression of mouse mast cell protease-1 in normal BALB/c mice and its up-regulation during intestinal nematode infection. Immunology. 90:1997;308-313.
41. Zarlenga D. S., Gamble H. R. Simultaneous isolation of preparative amounts of RNA and DNA from Trichinella spiralis by cesium trifluoroacetate isopycnic centrifugation. Analytical Biochemistry. 162:1987;569-574.