메뉴 건너뛰기




Volumn 59, Issue 5, 1996, Pages 716-724

Identification of factors from rat neutrophils responsible for cytotoxicity to isolated hepatocytes

Author keywords

cathepsin G; elastase; hepatotoxicity; injury; liver; proteases

Indexed keywords

ALPHA 1 ANTITRYPSIN; CATHEPSIN G; ELASTASE; MYELOPEROXIDASE;

EID: 0029891492     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1002/jlb.59.5.716     Document Type: Article
Times cited : (75)

References (50)
  • 1
    • 0026578080 scopus 로고
    • Neutrophil depletion protects against liver injury from bacterial endotoxin
    • Hewett, J. A., Schultze, A. E., VanCise, S., Roth, R. A. (1992) Neutrophil depletion protects against liver injury from bacterial endotoxin. Lab. Invest. 66, 347-361.
    • (1992) Lab. Invest. , vol.66 , pp. 347-361
    • Hewett, J.A.1    Schultze, A.E.2    VanCise, S.3    Roth, R.A.4
  • 2
    • 0022494581 scopus 로고
    • Corynebacterium parvum elicited hepatic macrophages demonstrate enhanced respiratory burst activity compared with resident Kupffer cells in the rat
    • Arthur, M. J. P., Kowolski-Saunders, P., Wright, R. (1986) Corynebacterium parvum elicited hepatic macrophages demonstrate enhanced respiratory burst activity compared with resident Kupffer cells in the rat. Gastroenterology 91, 174-181.
    • (1986) Gastroenterology , vol.91 , pp. 174-181
    • Arthur, M.J.P.1    Kowolski-Saunders, P.2    Wright, R.3
  • 3
    • 0025924857 scopus 로고
    • An antibody to neutrophils attenuates α-naphthylisothiocyanate-induced liver injury
    • Dahm, L. J., Schultze, A. E., Roth, R. A. (1991) An antibody to neutrophils attenuates α-naphthylisothiocyanate-induced liver injury. J. Pharmacol. Exp. Ther. 256, 412-420.
    • (1991) J. Pharmacol. Exp. Ther. , vol.256 , pp. 412-420
    • Dahm, L.J.1    Schultze, A.E.2    Roth, R.A.3
  • 5
    • 0029925875 scopus 로고    scopus 로고
    • Nitric oxide is not involved in hepatocyte killing by neutrophils activated by fMLP or PMA in vitro
    • Wagner, J. G., Ganey, P. E., Roth, R. A. (1996) Nitric oxide is not involved in hepatocyte killing by neutrophils activated by fMLP or PMA in vitro. Hepatology 23, 803-810.
    • (1996) Hepatology , vol.23 , pp. 803-810
    • Wagner, J.G.1    Ganey, P.E.2    Roth, R.A.3
  • 6
    • 0026713741 scopus 로고
    • Superoxide generation by neutrophils and Kupffer cells during in vivo reperfusion after hepatic ischemia in rats
    • Jaeschke, H., Bautista, A. P., Spolarics, Z., Spitzer, J. J. (1992) Superoxide generation by neutrophils and Kupffer cells during in vivo reperfusion after hepatic ischemia in rats. J. Leukoc. Biol. 52, 377-382.
    • (1992) J. Leukoc. Biol. , vol.52 , pp. 377-382
    • Jaeschke, H.1    Bautista, A.P.2    Spolarics, Z.3    Spitzer, J.J.4
  • 7
    • 0024602827 scopus 로고
    • Tissue destruction by neutrophils
    • Weiss, S. J. (1989) Tissue destruction by neutrophils. N. Engl. J. Med. 320, 365-376.
    • (1989) N. Engl. J. Med. , vol.320 , pp. 365-376
    • Weiss, S.J.1
  • 8
    • 0028596632 scopus 로고
    • Increased oxyradical production during reoxygenation of perfused rat liver: Signal versus injury
    • Brass, C. A., Nunes, F., Nagpal, R. (1994) Increased oxyradical production during reoxygenation of perfused rat liver: Signal versus injury. Transplantation 12, 1329-1335.
    • (1994) Transplantation , vol.12 , pp. 1329-1335
    • Brass, C.A.1    Nunes, F.2    Nagpal, R.3
  • 9
    • 0002282084 scopus 로고
    • Oxygen-independent antimicrobial systems
    • (J.I. Gallin, I.M. Goldstein, and R. Snyderman, eds.), New York, Raven
    • Elsbach, P., Weiss, J. (1992) Oxygen-independent antimicrobial systems. In Inflammation: Basic Principles and Clinical Correlates (J.I. Gallin, I.M. Goldstein, and R. Snyderman, eds.), New York, Raven, 603-636.
    • (1992) Inflammation: Basic Principles and Clinical Correlates , pp. 603-636
    • Elsbach, P.1    Weiss, J.2
  • 11
    • 0019421038 scopus 로고
    • Proteolytic enzymes released by liver macrophages may promote hepatic injury in a rat model of hepatic damage
    • Tanner, A., Keyhani, A., Reiner, R., Holdstock, G., Wright, R. (1981) Proteolytic enzymes released by liver macrophages may promote hepatic injury in a rat model of hepatic damage. Gastroenterology 80, 647-654.
    • (1981) Gastroenterology , vol.80 , pp. 647-654
    • Tanner, A.1    Keyhani, A.2    Reiner, R.3    Holdstock, G.4    Wright, R.5
  • 12
    • 0023882573 scopus 로고
    • In vitro toxicity of polymorphonuclear neutrophils to rat hepatocytes: Evidence for a proteinase-mediated mechanism
    • Mavier, P., Preaux A-M., Guigui, B., Leses, M., Zafrani, E., Dhumeaux, D. (1988) In vitro toxicity of polymorphonuclear neutrophils to rat hepatocytes: evidence for a proteinase-mediated mechanism. Hepatology 8, 254-258.
    • (1988) Hepatology , vol.8 , pp. 254-258
    • Mavier, P.1    Preaux, A.-M.2    Guigui, B.3    Leses, M.4    Zafrani, E.5    Dhumeaux, D.6
  • 13
    • 0027183742 scopus 로고
    • Hepatocyte injury by activated neutrophils in vitro is mediated by proteases
    • Harbrecht, B. G., Billiar, T., Curran, R. D., Stadler, J., Simmons, R. L. (1993) Hepatocyte injury by activated neutrophils in vitro is mediated by proteases. Ann. Surg. 218, 120-128.
    • (1993) Ann. Surg. , vol.218 , pp. 120-128
    • Harbrecht, B.G.1    Billiar, T.2    Curran, R.D.3    Stadler, J.4    Simmons, R.L.5
  • 14
    • 0019857584 scopus 로고
    • Neutrophil-mediated endothelial injury in vitro. Mechanisms of cell detachment
    • Harlam, J. M., Killen, P. D., Harker, L. A., Striker, G. E., Wright, D. G. (1981) Neutrophil-mediated endothelial injury in vitro. Mechanisms of cell detachment. J. Clin. Invest. 68, 1394-1403.
    • (1981) J. Clin. Invest. , vol.68 , pp. 1394-1403
    • Harlam, J.M.1    Killen, P.D.2    Harker, L.A.3    Striker, G.E.4    Wright, D.G.5
  • 16
    • 0024339999 scopus 로고
    • Toxicity of polymorphonuclear neutrophils against hepatocytes: Protective effect of heparin
    • Mavier, P., Preaux, A-M., Rosenbaum, J., Zafrani, E. S., Dhumeaux, D. (1989) Toxicity of polymorphonuclear neutrophils against hepatocytes: protective effect of heparin. Biochem. Pharmacol. 38, 1865-1867.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 1865-1867
    • Mavier, P.1    Preaux, A.-M.2    Rosenbaum, J.3    Zafrani, E.S.4    Dhumeaux, D.5
  • 17
    • 0015752890 scopus 로고
    • Preparation of rat liver cells. III. Enzymatic requirements for dispersion
    • Seglen, P. O. (1973) Preparation of rat liver cells. III. Enzymatic requirements for dispersion. Exp. Cell Res. 82, 391-398.
    • (1973) Exp. Cell Res. , vol.82 , pp. 391-398
    • Seglen, P.O.1
  • 19
    • 0025168159 scopus 로고
    • Purification and N-terminal amino-acid sequence analysis of rat polymorphonuclear leukocyte cathepsin G
    • Björk, P., Ohlsson, K. (1990) Purification and N-terminal amino-acid sequence analysis of rat polymorphonuclear leukocyte cathepsin G. Biol. Chem. Hoppe-Seylers. Arch. 371, 595-601.
    • (1990) Biol. Chem. Hoppe-Seylers. Arch. , vol.371 , pp. 595-601
    • Björk, P.1    Ohlsson, K.2
  • 21
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum, H., Beier, H., Cross, H. (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Cross, H.3
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0018073126 scopus 로고
    • C5a-induced stimulus-specific desensitization and the effects of cytochalasin B
    • Henson, P. M., Zanolati, B., Schwartzman, N. A., Hong, S. K. (1978) C5a-induced stimulus-specific desensitization and the effects of cytochalasin B. J. Immunol. 121, 851-855.
    • (1978) J. Immunol. , vol.121 , pp. 851-855
    • Henson, P.M.1    Zanolati, B.2    Schwartzman, N.A.3    Hong, S.K.4
  • 24
    • 0019853492 scopus 로고
    • The roles of extracellular and intracellular calcium in lysosomal enzyme release and superoxide anion generation by human neutrophils
    • Smolen, J. E., Korchak, H. M., Weissmann, G. (1981) The roles of extracellular and intracellular calcium in lysosomal enzyme release and superoxide anion generation by human neutrophils. Biochim. Biophys. Acta 677, 512-520.
    • (1981) Biochim. Biophys. Acta , vol.677 , pp. 512-520
    • Smolen, J.E.1    Korchak, H.M.2    Weissmann, G.3
  • 27
    • 0025192472 scopus 로고
    • Characterization of two azurophil granule proteases with active-site homology to neutrophil elastase
    • Wilde, C. G., Snable, J. L., Griffin, J. E., Scott, R. W. (1990) Characterization of two azurophil granule proteases with active-site homology to neutrophil elastase. J. Biol. Chem. 265, 2038-2041.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2038-2041
    • Wilde, C.G.1    Snable, J.L.2    Griffin, J.E.3    Scott, R.W.4
  • 28
    • 0024239623 scopus 로고
    • Protease 3. A disinct human polymophonuclear leukocyte proteinase that produces emphysema in hamsters
    • Kao, R. C., Wehner, N. G., Skubitz, K. M., Gray, B. H., Hoidal, J. R. (1988) Protease 3. A disinct human polymophonuclear leukocyte proteinase that produces emphysema in hamsters. J. Clin. Invest. 82, 1963-1973.
    • (1988) J. Clin. Invest. , vol.82 , pp. 1963-1973
    • Kao, R.C.1    Wehner, N.G.2    Skubitz, K.M.3    Gray, B.H.4    Hoidal, J.R.5
  • 29
    • 0017262795 scopus 로고
    • Human leukocyte granule elastase: Rapid isolation and characterization
    • Baugh, R. J., Travis, J. (1976) Human leukocyte granule elastase: rapid isolation and characterization. Biochemistry 15, 836-841.
    • (1976) Biochemistry , vol.15 , pp. 836-841
    • Baugh, R.J.1    Travis, J.2
  • 30
    • 0026896029 scopus 로고
    • The matrix-degrading metalloproteinases
    • Matrisian, L. M. (1992) The matrix-degrading metalloproteinases. BioEssays 14, 455-463.
    • (1992) BioEssays , vol.14 , pp. 455-463
    • Matrisian, L.M.1
  • 31
    • 0022792132 scopus 로고
    • Collagenolytic metalloenzymes of the human neutrophil. Characteristics, regulation and potential function in vivo
    • Weiss, S. J., Peppin, G. J. (1986) Collagenolytic metalloenzymes of the human neutrophil. Characteristics, regulation and potential function in vivo. Biochem. Pharmacol. 35, 3189-3197.
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 3189-3197
    • Weiss, S.J.1    Peppin, G.J.2
  • 32
    • 0025895193 scopus 로고
    • Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan: A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stomelysins-1 and -2 and punctuated metalloproteinase (PUMP)
    • Murphy, G., Crockett, M. I., Ward, R. V., Docherty, A. J. P. (1991) Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan: a quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stomelysins-1 and -2 and punctuated metalloproteinase (PUMP). Biochem. J. 277, 277-279.
    • (1991) Biochem. J. , vol.277 , pp. 277-279
    • Murphy, G.1    Crockett, M.I.2    Ward, R.V.3    Docherty, A.J.P.4
  • 33
    • 0016816987 scopus 로고
    • Antibacterial activity of cationic proteins from human granulocytes
    • Odeberg, H., Ohlsson, I. (1975) Antibacterial activity of cationic proteins from human granulocytes. J. Clin. Invest. 56, 1118-1124.
    • (1975) J. Clin. Invest. , vol.56 , pp. 1118-1124
    • Odeberg, H.1    Ohlsson, I.2
  • 34
    • 0025050764 scopus 로고
    • Identification of the primary antimicrobial domains in human neutrophil cathepsin G
    • Bangalore, N., Travis, J., Onunka, V. C., Pohl, J., Shafer, W. M. (1990) Identification of the primary antimicrobial domains in human neutrophil cathepsin G. J. Biol. Chem. 265, 13584-13588.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13584-13588
    • Bangalore, N.1    Travis, J.2    Onunka, V.C.3    Pohl, J.4    Shafer, W.M.5
  • 36
    • 0028136620 scopus 로고
    • Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3
    • Padrines, M., Wolf, M., Walz, A., Baggiolini, M. (1994) Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3. FEBS Lett. 352, 231-235.
    • (1994) FEBS Lett. , vol.352 , pp. 231-235
    • Padrines, M.1    Wolf, M.2    Walz, A.3    Baggiolini, M.4
  • 37
    • 0025777433 scopus 로고
    • Tumor necrosis factor-α enhances platelet activation via cathepsin G released from neutrophils
    • Renesto, P., Chignard, M. (1991) Tumor necrosis factor-α enhances platelet activation via cathepsin G released from neutrophils. J. Immunol. 146, 2305-2309.
    • (1991) J. Immunol. , vol.146 , pp. 2305-2309
    • Renesto, P.1    Chignard, M.2
  • 38
    • 0023951925 scopus 로고
    • Cathepsin G is a strong platelet agonist released by neutrophils
    • Selak, M. A., Chignard, M., Smith, J. B. (1988) Cathepsin G is a strong platelet agonist released by neutrophils. Biochem. J. 251, 293-299.
    • (1988) Biochem. J. , vol.251 , pp. 293-299
    • Selak, M.A.1    Chignard, M.2    Smith, J.B.3
  • 39
    • 0024207188 scopus 로고
    • Toxicity of phorbol myristate acetate-stimulated polymorphonuclear neutrophils against rat hepalocytes: Demonstration and mechanism
    • Guigui, B., Rosenbaum, J., Préaux, A.-M., Martin, N., Zafrani, E. S., Dhumeaux, D., Mavier, P. (1988) Toxicity of phorbol myristate acetate-stimulated polymorphonuclear neutrophils against rat hepalocytes: Demonstration and mechanism. Lab. Invest. 59, 831-837.
    • (1988) Lab. Invest. , vol.59 , pp. 831-837
    • Guigui, B.1    Rosenbaum, J.2    Préaux, A.-M.3    Martin, N.4    Zafrani, E.S.5    Dhumeaux, D.6    Mavier, P.7
  • 40
    • 0020643467 scopus 로고
    • Human plasma proteinase inhibitors
    • Travis, J., Salvesen, G. S. (1983) Human plasma proteinase inhibitors. Ann. Rev. Biochem. 52, 655-709.
    • (1983) Ann. Rev. Biochem. , vol.52 , pp. 655-709
    • Travis, J.1    Salvesen, G.S.2
  • 41
    • 0026177184 scopus 로고
    • Release of dog polymorphonuclear leukocyte cathepsin G, normally and in endotoxin and pancreatitic shock. Isolation and partial characterization of dog polymorphonuclear leukocyte cathepsin G
    • Björk, P., Axelsson, L., Ohlsson, K. (1991) Release of dog polymorphonuclear leukocyte cathepsin G, normally and in endotoxin and pancreatitic shock. Isolation and partial characterization of dog polymorphonuclear leukocyte cathepsin G. Biol. Chem. Hoppe-Seyler 372, 419-426.
    • (1991) Biol. Chem. Hoppe-Seyler , vol.372 , pp. 419-426
    • Björk, P.1    Axelsson, L.2    Ohlsson, K.3
  • 42
    • 0023840318 scopus 로고
    • Pericellular proteolysis by neutrophils in the presence of proteinase inhibitors: Effects of substrate opsonization
    • Campbell, E. J., Campell, M. A. (1988) Pericellular proteolysis by neutrophils in the presence of proteinase inhibitors: effects of substrate opsonization. J. Cell Biol. 106, 667-676.
    • (1988) J. Cell Biol. , vol.106 , pp. 667-676
    • Campbell, E.J.1    Campell, M.A.2
  • 43
    • 0023470646 scopus 로고
    • Elastase-mediated fibrinogenolysis by chemoattractant-stimulated neutrophils occurs in the presence of physiologic concentrations of antiproteinases
    • Weitz, J. I., Huang, A. J., Landman, S. L., Nicholson, S. C., Silverstein, S. C. (1987) Elastase-mediated fibrinogenolysis by chemoattractant-stimulated neutrophils occurs in the presence of physiologic concentrations of antiproteinases. J. Exp. Med. 166, 1836-1850.
    • (1987) J. Exp. Med. , vol.166 , pp. 1836-1850
    • Weitz, J.I.1    Huang, A.J.2    Landman, S.L.3    Nicholson, S.C.4    Silverstein, S.C.5
  • 44
    • 0021361308 scopus 로고
    • Neutrophils degrade subendothelial matrices in the presence of α1-proteinase inhibitor. Cooperative use of lysosomal proteinases and oxygen metabolites
    • Weiss, S. J., Regiani, S. (1984) Neutrophils degrade subendothelial matrices in the presence of α1-proteinase inhibitor. Cooperative use of lysosomal proteinases and oxygen metabolites. J. Clin. Invest. 73, 1297-1303.
    • (1984) J. Clin. Invest. , vol.73 , pp. 1297-1303
    • Weiss, S.J.1    Regiani, S.2
  • 45
    • 0023736418 scopus 로고
    • Alveolar fluid neutrophil elastase activity in the adult respiratory distress syndrome is complexed to α2-macrogiobulin
    • Wewers, M. D., Herzyk, D. J., Gadek, J. E. (1988) Alveolar fluid neutrophil elastase activity in the adult respiratory distress syndrome is complexed to α2-macrogiobulin. J. Clin. Invest. 82, 1260-1267.
    • (1988) J. Clin. Invest. , vol.82 , pp. 1260-1267
    • Wewers, M.D.1    Herzyk, D.J.2    Gadek, J.E.3
  • 46
    • 0022642346 scopus 로고
    • Levels of free granulocyte elastase in bronchial secretions from patients with cystic fibrosis: Effect of antimicrobial treatment against Pseudomonas aeruginosa
    • Suter, S., Schaad, U. B., Tegner, H., Ohlsson, K., Desgrandchamps, D., Wardvogel, F. A. (1986) Levels of free granulocyte elastase in bronchial secretions from patients with cystic fibrosis: effect of antimicrobial treatment against Pseudomonas aeruginosa. J. Infect. Dis. 153, 902-909.
    • (1986) J. Infect. Dis. , vol.153 , pp. 902-909
    • Suter, S.1    Schaad, U.B.2    Tegner, H.3    Ohlsson, K.4    Desgrandchamps, D.5    Wardvogel, F.A.6
  • 47
    • 0023488690 scopus 로고
    • Degradation in vivo of articular cartilage in rheumatoid arthritis and juvenile chronic arthritis by cat heps in C and elastase from polymorphonuclear leukocytes
    • Velvart, M., Fehr, K. (1987) Degradation in vivo of articular cartilage in rheumatoid arthritis and juvenile chronic arthritis by cat heps in C and elastase from polymorphonuclear leukocytes. Rheumatol. Int. 7, 195-202.
    • (1987) Rheumatol. Int. , vol.7 , pp. 195-202
    • Velvart, M.1    Fehr, K.2
  • 48
    • 0025019499 scopus 로고
    • A sensitive and specific assay for granulocyte elastase in inflammatory tissue fluid using L-pyro-glutamyl-L-propyl-L-valine-p-nitroanuide
    • Tanaka, H., Shimazu, T., Sugimoto, H., Yoshioka, T., Sugimoto, T. (1990) A sensitive and specific assay for granulocyte elastase in inflammatory tissue fluid using L-pyro-glutamyl-L-propyl-L-valine-p-nitroanuide. Clin. Chim. Acta 187, 173-180.
    • (1990) Clin. Chim. Acta , vol.187 , pp. 173-180
    • Tanaka, H.1    Shimazu, T.2    Sugimoto, H.3    Yoshioka, T.4    Sugimoto, T.5
  • 50
    • 0017331772 scopus 로고
    • Demonstration of granulocyte proteases in plasma of patients with acute leukemia and septicemia with coagulation defects
    • Egbring, R., Schmidt, W., Fuchs, G., Havemann, K. (1977) Demonstration of granulocyte proteases in plasma of patients with acute leukemia and septicemia with coagulation defects. Blood 49, 219-231.
    • (1977) Blood , vol.49 , pp. 219-231
    • Egbring, R.1    Schmidt, W.2    Fuchs, G.3    Havemann, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.