Pathogenic mechanisms induced by microbial proteases in microbial infections

Biological Chemistry Hoppe-Seyler

Volumn 377, Issue 4, 1996, Pages 217-226

  Maeda, Hiroshi ^a   Yamamoto, Tetsuro ^a  

^a KUMAMOTO UNIV SCHOOL OF MEDICINE   (Japan)

Author keywords

Bacterial proteases; Bacterial translocation; Bradykinin; Hageman factor; Protease inhibitors; Septicemia; Shock

Indexed keywords

BACTERIAL ENZYME; BACTERIAL TOXIN; BLOOD CLOTTING FACTOR 12; BLOOD CLOTTING FACTOR 12A; BRADYKININ; ENZYME PRECURSOR; FUNGAL PROTEIN; IMMUNOGLOBULIN; KALLIKREIN; KININ; PLASMINOGEN; PREKALLIKREIN; PROCOLLAGENASE; PROTEINASE; RESERPINE; SERINE PROTEINASE INHIBITOR;

BACTERIAL CELL WALL; BACTERIAL INFECTION; BLOOD CLOTTING; COMPLEMENT ACTIVATION; ENZYME ACTIVATION; FIBRINOLYSIS; HOST PARASITE INTERACTION; HUMAN; MYCOSIS; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; REVIEW; SEPTICEMIA;

ANIMALS; BACTERIA; BACTERIAL INFECTIONS; BLOOD COAGULATION; BRADYKININ; COMPLEMENT SYSTEM PROTEINS; ENDOPEPTIDASES; FUNGI; HUMANS; MYCOSES; NEOPLASMS; PROTEASE INHIBITORS;

EID: 0029879578     PISSN: 01773593     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (97)

1. Akaike, T., Molla, A., Ando, M., Araki, S., and Maeda, H. (1989). Molecular mechanism of complex infection of bacteria and virus analyzed by a model using serratiai protease and influenza virus in mice. J. Virol. 63,2252-2259.
2. Akaike, T., Maeda, H., Maruo, K., Sakata, Y, and Sato, K. (1994). Potentiation of infectivity and pathogenesis of influenza A virus by a house dust mite protease. J. Infect. Dis. 170, 1023-1026.
3. Blasi, F. (1988). Surface receptors for urokinase activator. Fibrinolysis2,73-84.
4. Blasi, J., Chapman, E.R., Link, E., Binz, T., Yamasaki, S., DeCamilli, P., Südhof, T.C., Neimann, H., Jahn, R. (1993). Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25. Nature 365,160-163.
5. Chen, Z., Potempa, J., Polanowski, A., Wikstnom, M., and Travis, J. (1992). Purification and characterization of a 50 KDa cysteine proteinase (gingipain) from Porphyromonas gingivalis. J. Biol. Chem. 267,18896-18901.
6. Cleary, P.P., Prahbu, U., Dale, J.B., Wexler, D.E., and Handley, J. (1992). Streptococcal Csa peptidase is highly specific endpeptidase. Infect. Immun. 60,5219-5223.
7. Colman, R. (1969). Activation of plasminogen by human plasma kallikrein. Biochem. Biophys. Res. Commun. 35,273-270.
8. Conese, M., and Blasi, F. (1995). Urokinase/urokinase receptor system: Intrernalization/degradation of urokinase serpin complex: Mechanism and regulation. Biol. Chem. HoppeSeyler 376,143-155.
9. de Bruin, P.A.F., Griffioen, G., Verspaget, H.W., Verheijen, J.H., and Lamers, C.B.H.W. (1987). Plasminogen activators and tumor development in the human colon: activity levels in normal mucosa, adenomatous polyps, and adenocarcinomas. Cancer Res. 47,4654-4657.
10. Desrochers, P.E., Mookhtiar, K., Van Wart, H.E., Hasty, K.A., and Weiss, S.J. (1992). Proteolytic inactivation of arproteinase inhibitor and oi-antichymotrypsin by oxidatively activated human neutrophil metalloproteinases. J. Biol. Chem. 267, 5005-5012.
11. Ferreira, S.H., Lorenzetti, B.B., and Poole, S. (1993). Bradykinin initiates cytokine-mediated inflammatory hyperalgesia. Br. J. Pharmacol. 770,1227-1231.
12. Ghebrehiwet, B., Randazzo, B.P., Dünn, J.T., Silverberg, M., and Kaplan, A.P. (1983). Mechanism of the activation of the classical pathway of complement by Hageman factor fragment. J. Clin. Invest. 71,1450-1456.
13. Gonias, S.L., and Pizzo, S.V. (1983). Characterization of functional human a2-macroglobulin half-molecules isolated by limited reduction with dithiothreitol. Biochemistry 22, 536546.
14. Gordon, V.M., and Leppla, S.H. (1994). Proteolytic activation of bacterial toxins: role of bacterial and host cell proteases. Infect. Immun. 62,333-340.
15. Hasui, Y, Suzumiya, F., Marutsuka, K., Sumiyoshi, A., Hashida, S., and Ishikawa, E. (1989). Comparative study of plasminogen activators in cancers and normal mucosae of human urinary bladder. Cancer Res. 49,1067-1070.
16. Hill, H.R., Bohnsack, J.F., Morris, E.Z., Augustine, N.H., Parker, C.J., Cleary, P.P., and Wu, J.T. (1988). Group B streptococci inhibits the chemotactic activity of the fifth component of complement. J. Immunol. 141,3551 -3556.
17. Hinode, D., Hayashi, H., and Nakamura, R. (1991). Purification and characterization of three types of proteases from culture supernatant of Porphyromonas gingivalis. Infect. Immun. 59, 3060-3068.
18. Holder, I.A., and Haidaris, G.G. (1979). Experimental studies of the pathogenesis of infections due to Pseudomonas aeruginosa: extracellular protease and elastase as in vivo virulence factors. Can. J. Microbiol. 25,593-599.
19. Holder, I.A., and Neely, A.N. (1989). Pseudomonas elastase acts as a virulence factor in burned hosts by Hageman factor-dependent activation of the host kinin cascade. Infect. Immun. 57,3345-3348.
20. Holder, I.A., and Neely, A.N. (1990). Hageman factor-dependent kinin activation in burns and its theoretical relationship to postburn immunosuppression syndrome and infection. J. Burn Care & Rehabilitation 11,486-503.
21. Holder, I.A., and Neely, A.N. (1992). Hageman factor dependent activation and its relationship to lethal Pseudomonas aeruginosa burn wound infections. In: Recent Progress on Kinins. Agents and Actions Supplements 38/III. G. Bonner, H. Fritz, B. Schoelkens, G. Dietze and K. Luppertz, eds. (Basel, Switzerland: Birkhäuser Verlag), pp. 329-342.
22. Ijiri, Y., Yamamoto, T., Kamata, R., Aoki, H., Matsumoto, K., Kambara, T., and Okamura, R. (1993). The role of Pseudomonas aeruginosa elastase in corneal ring abscess formation of pseudomonal keratitis. Graefe. Arch. Clin. Exp. Ophtnalmol. 237,521-528.
23. Ijiri, Y., Matsumoto, K., Kamata, R., Nishino, N., Okamura, R., Kambara, T., and Yamamoto, T. (1994). Suppression of polymorphonuclear leukocyte chemotaxis by Pseudomonas aeruginosa elastase in vitro', a study of the mechanism and the correlation with ring abscess in pseudomonal keratitis. Int. J. Exp. Path. 75,441-451.
24. Imamura, T., Pike, R.N., Potempa, J., and Travis, J. (1994). Pathogenesis of periodontitis: a major arginine-specific cysteine proteinase from Porphyromonas gingivalis induces vascular permeability enhancement through activation of the kallikrein/ kinin pathway. J. Clin. Invest. 94,361 -367.
25. Imamura, T., Potempa, J., Pike, R.N., and Travis, J. (1995). Dependent of vascular permeability enhancement on cysteine proteinases in vesicles of Porphyromonas gingivalis. Infect. Immun. 63,1999-2003.
26. Kamata, R., Matsumoto, K., Okamura, R., Yamamoto, T., and Maeda, H. (1985a). The serratial 56K protease as a major pathogenic factor in serratial keratitis. Ophthalmology 92, 1452-1459.
27. Kamata, R., Yamamoto, T., Matsumoto, K., and Maeda, H. (1985b). A serratial protease causes vascular permeability reaction by activation of the Hageman factor dependent pathway in guinea pigs. Infect. Immun. 48,747-753.
28. Kaminishi, H., Tanaka, M., Cho, T., Maeda, H., and Hagihara, Y. (1990). Activation of the plasma kallikrein-kinin system by Candida albicans protease. Infect. Immun. 58,2139-2143.
29. Kaminishi, H., Cho, T., Itoh, T., Iwata, A., Kawasaki, K., Hagihara, Y, and Maeda, H. (1993). Vascular permeability enhancing activity of Porphyromonas gingivalis protease in guinea pigs. FEMS-Microbiol. Lett. 114.109-114.
30. Kaminishi, H., Hamatake, T., Cho, T., Tamaki, T., Suenaga, N., Fujii, T., Hagihara, Y, and Maeda, H. (1994). Activation of the blood clotting factors by microbial proteinases. FEMS-Microbiol. Lett. 121,327-332.
31. Kaminishi, H., Miyaguchi, H., Tamaki, T., Suenaga, N., Hisamitsu, M., Mihashi, I., Matsumoto, H., Maeda, H., and Hagihara, Y. (1995). Degradation of humoral host defense by Candida albicans proteinase. Infect. Immun. 63,984-988.
32. Katori, M., Majima, M., Odoi-Adome, R., Sunahara, N., and Uchida, Y. (1989). Evidence for the involvement of a kallikreinkinin system in the immediate hypotension produced by endotoxin. Br. J. Pharmacol. 98,1381-1391.
33. Khan, M.M.H., Yamamoto, T., Araki, H., Shibuya, Y, and Kam-bara, T. (1993). Role of Hageman factor/kallikrein-kinin system in pseudomonal elastase-induced shock model. Biochim. Biophys.Acta 1157,119-126.
34. Khan, M.M.H., Shibuya, Y., Nakagaki, T., Kambara, T., and Yamamoto, T. (1994). Alpha-2-macroglobulin as the major defence in acute pseudomonal septic shock in the guinea-pig model. Int. J. Exp. Path. 75,285-293.
35. Khan, M.M.H., Shibuya, Y, Kambara, T., and Yamamoto, T. (1995). Role of alpha-2-macroglobulin and bacterial elastase in guinea-pig pseudomonal septic shock. Int. J. Exp. Path. 76, 21-28.
36. Lottenberg, R., Minning-Wenz, D., and Boyle, M.D.R (1994). Capturing host plasmin(ogen): a common mechanism for invasive pathogen. Trends in Microbiol. 20,20-24.
37. Lowson, D.A., and Meyer, T.F. (1992). Biochemical characterization of Porphyromonas (Bacteroides) gingivalis collagenase. Infect. Immun. 60,1524-1529.
38. Maeda, H., and Molla, A. (1989). Pathogenic potentials of bacterial proteases. Clin. Chim. Acta 185,357-368.
39. Maeda, H., Molla, A., Oda, T., and Katsuki, T. (1987a). Internalization of serratial protease into cells as an enzyme inhibitor complex with a2-macroglobulin and regeneration of protease activity and cytotoxicity. J. Biol. Chem. 262,10946-10950.
40. Maeda, H., Matsumura, Y, and Molla, A. (1987b). Antitumor activity of some bacterial proteases: eradication of solid tumors in mice by intratumor injection. Cancer Res. 47,563-566.
41. Maeda, H., Matsumura, Y, and Kato, H. (1988). Purification and identification of [hydroxyprolyl]3-bradykinin in ascitic fluid from a patient with gastric cancer. J. Biol. Chem. 263, 16051-16054.
42. Maeda, H., Molla, A., Sakamoto, K., Murakami, A., Matsumura, Y. (1989). Cytotoxicity of bacterial proteases in various tumor cells mediated through a2-macroglobulin receptor. Cancer Res. 49, 660-664.
43. Maeda, H., Maruo, K., Akaike, T., Kaminishi, H., and Hagiwara, Y. (1992). Microbial proteinases as an universal trigger of kinin generation in microbial infections. In: Recent Progress on Kinins. Agents and Actions Supplement 38/IH. G. Bonner, H. Fritz, B. Schoelkens, G. Dietze and K. Luppertz, eds. (Basel, Switzerland: Birkhäuser Verlag), pp. 362-369.
44. Maeda, H., Akaike, T., Sakata, Y, and Maruo, K. (1993). Role of bradykinin in microbial infection: Enhancement of septicemia by microbial proteases and kinin. In: Protease, Protease Inhibitor and Protease-Derived Peptides: Importance in Human Pathophysiology and Therapeutics. Agents and Actions Supplements 42, U.C. Cheronis and J.E. Repine, eds. (Basel, Switzerland: Birkhäuser Verlag), pp. 159-165.
45. Maeda, H., Noguchi, Y, Sato, K., and Akaike, T. (1994). Enhanced vascular permeability in solid tumor is mediated by nitric oxide and inhibited by both new nitric oxide scavenger and nitric oxide synthase inhibitors. Jpn. J. Cancer Res. 85,331 -334.
46. Maeda, H., Shin, Y.-H., Akaike, T., and Yoshida, M. (1996a). Septic shock: prevention by NO-scavenger (PTIO) and by kinin inhibitor. Shock, in press.
47. Maeda, H., Akaike, T., Wu, J., Noguchi, Y, and Sakata, Y. (1996b). Bradykinin and nitric oxide in infectious disease and cancer. J. Immunopharmacol., in press.
48. Marian, B., Harvey, S., Infante, D., Markus, G., Winawer, S., and Friedman, E. (1990). Urokinase secretion from human colon carcinomas induced by endogenous diglycerides. Cancer Res. 50,2245-2250.
49. Maruo, K., Akaike, T., Matsushima, Y, Kohmoto, S., Inada, Y, Ono, T., Arao, T., and Maeda, H. (1991 ). Triggering of the vascular permeability reaction by activation of the Hageman factor-prekallikrein system by house dust mite proteinase. Biochim. Biophys. Acta 7074,62-68.
50. Maruo, K., Maeda, H., Akaike, T., Inada, Y., Ohkubo, I., and Ono, T. (1993). Effect of microbial and mite proteases on low- and high-molecular-weight kininogens: Generation of kinin and inactivation of thiol-protease inhibitory activity. J. Biol. Chem. 260,17711-17715.
51. Matsumoto, K.,Yamamoto,T., Kamata, R., and Maeda, H.(1984). Pathogenesis of serratial infection: Activation of the Hageman factor-prekallikrein cascade by serratial protease. J. Biochem. 96,739-749.
52. Matsumoto, K., Shams, N.B.K., Hanninen, L.A., and Kenyon, K.R. (1992). Proteolytic activation of corneal matrix metalloproteinase by Pseudomonas aeruginosa elastase. Current Eye Res. 17,1105-1109.
53. Matsumoto, K., Miyagawa, S., Okamura, R., and Maeda, H. (1996). Production of the protease in experimental Serratia keratitis in guinea pigs, and spreading in the tissue: An immunohistochemical study. Current Eye Res., in press.
54. Matsumura, Y, Kimura, M., Yamamoto, T., and Maeda, H. (1988). Involvement of the kinin-generating cascade in enhanced vascular permeability in tumor tissue. Jpn. J. Cancer Res. 79, 1327-1334.
55. Matsumura, Y, Maruo, K., Kimura, M., Yamamoto, T., Konno, T., and Maeda, H. (1991). Kinin-generating cascade in advanced cancer patients and in vitro study. Jpn. J. Cancer Res. 82, 732-741.
56. Miyagawa, S., Kamata, R., Matsumoto, K., Okamura, R., and Maeda, H. (1991 a). Inhibitory effects of ovomacroglobulin on bacterial keratitis in rabbits. Graefe's Arch. Ophthalmol. 229, 281-286.
57. Miyagawa, S., Matsumoto, K., Kamata, R., Okamura, R., and Maeda, H. (1991 b). Serratia marcescens in experimental keratitis and growth suppression by chicken egg white ovomacroglobulin. Jpn. J. Ophthalmol. 35,402-410.
58. Miyagawa, S., Nishino, N., Okamura, R., and Maeda, H. (1991c). Effects of protease inhibitors on growth of Serratia marcescens and Pseudomonas aeruginosa: Chicken egg white ovomacroglobulin is a potent growth suppressor. Microbial Pathogenesis 11,137-141.
59. Miyagawa, S., Kamata, R., Matsumoto, K., Okamura, R., and Maeda, H. (1994). Therapeutic intervention with chicken egg white ovomacroglobulin and a new quinolone on experimental Pseudomonas keratitis. Graefe's Arch. Clin. Exp. Ophthalmol. 232,488-493.
60. Molla, A., Matsumoto, K., Oyamada, I., Katsuki,T.,and Maeda, H. (1986). Degradation of protease inhibitors, immunoglobulins, and other serum proteins by Serratia protease and its toxicity to fibroblasts in culture. Infect. Immun. 53,522-529.
61. Molla, A., Matsumura, Y, Yamamoto, T., Okamura, R., and Maeda, H. (1987a). Pathogenic capacity of proteases from Serratia marcescens and Pseudomonas aeruginosa and suppression by chicken egg white ovomacroglobulin. Infect. Immun. 55,2509-2517.
62. Molla, A., Oda, T., and Maeda, H. (1987b). Different binding kinetics of Serratia 56K protease with plasma a2-macroglobulin and chicken egg white ovomacroglobulin. J. Biochem. 101, 199-205.
63. Molla, A., Yamamoto, T., Akaike, T., Miyoshi, S., and Maeda, H. (1989a). Activation of Hageman factor and prekallikrein and generation of kinin by various microbial proteinases. J. Biol. Chem. 264,10589-10594.
64. Molla, A., Akaike, T., and Maeda, H. (1989b). Inactivation of various proteinase inhibitors and the complement system in human plasma by the 56-kilodalton proteinase from Serratia marcescens. Infect. Immun. 57,1868-1871.
65. Montecucco, C., and Schiavo, G. (1993). Tetanus toxin and botulism neurotoxin: a new group of zinc proteases. TIBS 18, 324-327.
66. Morihara, K., Tsuzuki, M., and Oka, T. (1979). Protease and elastase of Pseudomonas aeruginosa: inactivation of human plasma a, proteinase inhibitor. Infect. Immun. 24, 188-193.
67. Mulks, M.H. (1983). Microbial IgA proteases, In: Bacterial Enzymes and Virulence, J.A. Holder, éd. (Boca Raton, FI, USA: CRC Press), pp. 82-101.
68. Murakami, A., Sakamoto, K., Kojima, Y, Sasaki, Y, and Maeda, H. (1992). Antitumor effect of bacterial proteases on various human cancer xenografts in nude mice. Reg. Cancer Treatment 4,200-206.
69. Nagaoka and Katori. (1975). Inhibition of kinin formation by a kallikrein inhibitor during extracorpored circulation in open heart surgery. Circulation 52,325-331.
70. Nagase, H., Enghild, J.J., Suzuki, K., and Salvesen, G. (1990). Stepwise activation mechanism of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl) mercuric acetate. Biochemistry 29,5783-5789.
71. Neeiy, A.N., and Holder, I.A. (1990). Effect of proteolytic activity on virulence of Candida albicans in burned mice. Infect. Immun. 58,1527-1531.
72. Oda, T., Kojima, Y, Akaike, T., Ijiri, S., Molla, A., and Maeda, H. (1990). Inactivation of chemotactic activity of C5a by serratial 56-kilodalton protease. Infect. Immun. 58,1269-1272.
73. Palmer, R.M.J., Ferrige, A.G., and Moncada, S. (1987). Nitric oxide release accounts for the biological activity of endothelium derived relaxing factor. Nature 327,524-526.
74. Flaut, A.G. (1983). The IgA, proteases of pathogenic bacteria. Ann. Rev. Microbiol. 37,603-622.
75. Potempa, J., Watorek, W., and Travis, J. (1986). Inactivation of human plasma aiproteinase inhibitor by proteinases from Staphylococcus aureus. J. Biol. Chem. 267,4330-4334.
76. Proud, D., Nuclerio, R.M., Gwaltney, J.M., and Hendley, J.O. (1990). Kinins are generated in nasal secretions during natural rhinovirus cold. J. Inf. Dis. 161,120-123.
77. Saari, H., Suomalainen, K., Lindy, O., Konttinen, Y.T., and Sorsa, T. (1990). Activation of latent human neutrophil collagenase by reactive oxygen species and serine proteases. Biochem. Biophys. Res. Commun. 171,979-987.
78. Sakata, Y, Akaike, T., Suga, M., Ijiri, S., Ando, M., and Maeda, H. (1996). Bradykinin generation triggered by Pseudomonas proteases facilitates invasion into the systemic circulation by Pseudomonas aeruginosa. Microbiol. Immunol., in press.
79. Schiavo, G., Benfenati, F., Pouiais, B., Rossetto, O., deLaureto, P.P., Das Gupta, B.R., and Montecucco, C. (1992). Tetanus and botulinum-B neurotoxins block neurotransmitter released by proteolytic cleavage of synapthobrevin. Nature 359, 832835.
80. Schlechte, W., Murano, G., and Boyd, D. (1989). Examination of the role of the urokinase receptor in human colon cancer mediated laminin degradation. Cancer Res. 49,6064-6069.
81. Scott, C.F., Whitaker, E.J., Hammond, F., and Colman, R. (1993). Purification and characterization of a potent 70 KDa thiol lysyl-protein are (lys-gingivain) from Porphyromonasgingivalis that cleaves kininogen and fibrinogen. J. Biol. Chem. 268, 7935-7942.
82. Shibuya, Y, Tanaka, H., Nishino, N., Okabe, H., Kambara, T, and Yamamoto, T. (1991). Activation of human plasma prekallikrein by Pseudomonas aeruginose elastase in vitro. Biochim. Biophys.Acta 1097,23-27.
83. Shimada, T., Kato, H., Maeda, H., and Iwanaga, S. (1985). Interaction of factor XII, high-molecular-weight (HMW) kininogen and prekallikrein with sulfatide; Analysis by fluorescence polarization. J. Biochem. 97,1637-1644.
84. Shin, Y.-H., Akaike, T., Khan, Md.M.H., Sakata, Y, and Maeda, H. (1996). Further evidence of bradykinin involvement in septic shock: Reduction of kinin production in vivo and improved survival rate by use of polymer tailored SBTI with longer T1/2- J. Immunopharmacol., in press.
85. Siebeck, M., Whalley, E.T., Hoffmann, H., Weipert, J.,and Fritz, H. (1989). The hypotensive response to des-Arg9-bradykinin increases during E. co//septicemia in the pig. In: Kinin V. K. Abe, H. Moriya, and S. Fujii, (New York, USA: Plenum Publ. Co.), pp. 389-393.
86. Siebeck, M., Fink, E., Weipert, J., Jochum, M., Fritz, H., Spanagl, M., Kroworsch, P., Shimamoto, K., and Schweiberer, L. (1993). Inhibition of plasma kallikrein with approtinin in porcine endotoxin shock. J. Trauma 34,193-198.
87. Sorsa.T., Ingman.T., Suomalainen, K., Haapasalo, M., Konttinen, Y, Lindy, O., Saari, H., and Uitto, V.-J. (1992). Identification of proteases from periodontapathogenic bacteria as activators of latent human neutrophil and fibroblast-type interstitial collagenases. Infect. Immun. 60,4491 -4495.
88. Tanaka, H., Yamamoto, T., Shibuya, Y, Nishino, N., Tanase, S., Miyauchi, Y, and Kambara, T. (1992). Activation of human plasma prekallikrein by Pseudomonas aeruginosa elastase II. Kinetic analysis and identification of scissile bond of prekallikrein in the activation. Biochim. Biophys. Acta 1138,243-250.
89. Tiffany, C.W., and Burch, P.M. (1989). Bradykinin stimulates tumor necrosis factor and interleukin-1 release from macrophages. FEES Lett. 247,189-192.
90. Travis, J., and Salvesen, G.S. (1983). Human plasma proteinase inhibitors. Ann. Rev. Biochem. 52,655-709.
91. Travis, J., Potempa, J., and Maeda, H. (1995). Are bacterial proteinases pathogenic factors? Trends in Microbiol. 3,405-407.
92. Uitto, V.-J., Larjava, H., Heino, J., Sorsa, T. (1989). A protease of Bacteroides gingivalis degrades cell surfaced and matrix glycoproteins of cultured gingival fibroblasts and induces secretion of collagenase and plasminogen activator. Infect. Immun. 57,213-218.
93. Vandekerckhove, F., Opdenakker, G., Van Ranst, M., Lenaerts, J.-P., Put, W., Billiau, A., and Van Damme, J. (1991). Bradykinin induces interleukin-6 and synergizes with interleukin-1. Lymphokine and Cytokine Res. 10,285-289.
94. Wachtfogel, Y.T., Kucich, U., James, H.L, Scott, C.F., Schapira, M., Zimmerman, M., Cohen, A.B., and Colman, R.W. (1983). Human plasma kallikrein releases neutrophil elastase during blood coagulation. J. Clin. Inv. 72,1672-1677.
95. Weipert, J., Hoffmann, H., Siebeck, M., and Whalley, E.T. (1988). Attenuation of arterial blood pressure fall in endotoxin shock in the rat using the competitive bradykinin antagonist Lys-Lys[Hyp2-Thi5'8, DPhe7]-BK(B4148). Br. J. Pharmacol. 94, 282284.
96. Weiss, S.J., Peppin, G., Ortiz, Y, Ragsdaie, C., and Test, ST. (1985). Oxidative autoactivation of latent collagenase by human neutrophils. Science 227, 747-749.
97. Yamamoto, T, Shibuya, Y, Nishino, N., Okabe, H., and Kambara, T. (1990). Activation of human Hageman factor by Pseudomonas aeruginosa elastase in the presence or absence of negatively charged substance in vitro. Biochim. Biophys. Acta 1038,231 -239.