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Volumn 4, Issue 6, 1997, Pages 391-400

Yeast recombinant factor C from horseshoe crab binds endotoxin and causes bacteriostasis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; DACTINOMYCIN; ENDOTOXIN; FACTOR C; LIPID A; RECOMBINANT ENZYME; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 0031399222     PISSN: 09680519     EISSN: None     Source Type: Journal    
DOI: 10.1177/096805199700400602     Document Type: Article
Times cited : (20)

References (39)
  • 1
    • 0026989386 scopus 로고
    • Bacterial endotoxins
    • August
    • Rietschel E.T., Brade H. Bacterial endotoxins. Sci Am 1992; August: 26-33.
    • (1992) Sci Am , pp. 26-33
    • Rietschel, E.T.1    Brade, H.2
  • 2
    • 0022462376 scopus 로고
    • Isolation of a lipopolysaccharide-binding acute phase reactant from rabbit serum
    • Tobias P.S., Soldau K., Ulevitch R.J. Isolation of a lipopolysaccharide-binding acute phase reactant from rabbit serum. J Exp Med 1986; 164: 777-793.
    • (1986) J Exp Med , vol.164 , pp. 777-793
    • Tobias, P.S.1    Soldau, K.2    Ulevitch, R.J.3
  • 3
    • 0025156953 scopus 로고
    • Bactericidal/permeability increasing protein has endotoxin-neutralizing activity
    • Marra M.N., Wilde C.G., Griffith J.E., Snable J.L., Scott R.W. Bactericidal/permeability increasing protein has endotoxin-neutralizing activity. J Immunol 1990; 144: 662-666.
    • (1990) J Immunol , vol.144 , pp. 662-666
    • Marra, M.N.1    Wilde, C.G.2    Griffith, J.E.3    Snable, J.L.4    Scott, R.W.5
  • 4
    • 0026599845 scopus 로고
    • The role of bactericidal/permeability-increasing protein as a natural inhibitor of bacterial endotoxin
    • Marra M.N., Wilde C.G., Collins M.S., Snable J.L., Thornton M.B., Scott R.W. The role of bactericidal/permeability-increasing protein as a natural inhibitor of bacterial endotoxin. J Immunol 1992; 148: 532-537.
    • (1992) J Immunol , vol.148 , pp. 532-537
    • Marra, M.N.1    Wilde, C.G.2    Collins, M.S.3    Snable, J.L.4    Thornton, M.B.5    Scott, R.W.6
  • 5
    • 0024316023 scopus 로고
    • Identification of a lipid A binding site in the acute phase reactant lipopolysaccharide binding protein
    • Tobias P.S., Soldau K., Ulevitch R.J. Identification of a lipid A binding site in the acute phase reactant lipopolysaccharide binding protein. J Biol Chem 1989; 264: 10867-10871.
    • (1989) J Biol Chem , vol.264 , pp. 10867-10871
    • Tobias, P.S.1    Soldau, K.2    Ulevitch, R.J.3
  • 6
    • 0027478331 scopus 로고
    • Bactericidal/permeability increasing protein and host defense against Gram-negative bacteria and endotoxin
    • Elsbach P., Weiss J. Bactericidal/permeability increasing protein and host defense against Gram-negative bacteria and endotoxin. Curr Opin Immunol 1993; 5: 103-107.
    • (1993) Curr Opin Immunol , vol.5 , pp. 103-107
    • Elsbach, P.1    Weiss, J.2
  • 7
    • 0028327687 scopus 로고
    • The role of bactericidal/permeability increasing protein in the treatment of primate bacteria and septic shock
    • Rogy M.A., Oldenburg H.S.A., Calvano S.E. et al. The role of bactericidal/permeability increasing protein in the treatment of primate bacteria and septic shock. J Clin Immunol 1994; 14: 120-133.
    • (1994) J Clin Immunol , vol.14 , pp. 120-133
    • Rogy, M.A.1    Oldenburg, H.S.A.2    Calvano, S.E.3
  • 8
    • 0020416253 scopus 로고
    • Limilus anti-LPS factor: An anticoagulant which inhibits the endotoxin-mediated activation of Limulus coagulation system
    • Tanaka S., Nakamura T., Morita T., Iwanaga S. Limilus anti-LPS factor: an anticoagulant which inhibits the endotoxin-mediated activation of Limulus coagulation system. Biochem Biophys Res Commun 1982; 105: 717-723.
    • (1982) Biochem Biophys Res Commun , vol.105 , pp. 717-723
    • Tanaka, S.1    Nakamura, T.2    Morita, T.3    Iwanaga, S.4
  • 9
    • 0021799698 scopus 로고
    • Isolation and biological activities of Limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS)
    • Morita T.S., Ohtsubo T., Nakamura T. et al. Isolation and biological activities of Limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS). J Biochem 1985; 97: 1611-1620.
    • (1985) J Biochem , vol.97 , pp. 1611-1620
    • Morita, T.S.1    Ohtsubo, T.2    Nakamura, T.3
  • 10
    • 0022887258 scopus 로고
    • Primary structure of Limulus anticoagulant anti-lipopolysaccharide factor
    • Aketagawa J., Miyata T., Ohtsubo S. et al. Primary structure of Limulus anticoagulant anti-lipopolysaccharide factor. J Biol Chem 1986; 261: 7357-7365.
    • (1986) J Biol Chem , vol.261 , pp. 7357-7365
    • Aketagawa, J.1    Miyata, T.2    Ohtsubo, S.3
  • 11
    • 0023352436 scopus 로고
    • Primary structure of antilipopolysaccharide factor from American horseshoe crab, L. polyhemus
    • Muta T., Miyata T., Tokunaga F. et al. Primary structure of antilipopolysaccharide factor from American horseshoe crab, L. polyhemus. J Biochem 1987; 101: 1321-1330.
    • (1987) J Biochem , vol.101 , pp. 1321-1330
    • Muta, T.1    Miyata, T.2    Tokunaga, F.3
  • 12
    • 0026517499 scopus 로고
    • Limulus antilipopolysaccharide factor protects rabbits from meningococcal endotoxin shock
    • Alpert G., Baldwin G., Thompson C. et al. Limulus antilipopolysaccharide factor protects rabbits from meningococcal endotoxin shock. J Infect Dis 1992; 165: 494-500.
    • (1992) J Infect Dis , vol.165 , pp. 494-500
    • Alpert, G.1    Baldwin, G.2    Thompson, C.3
  • 13
    • 0026780772 scopus 로고
    • Binding and neutralization of endotoxin by Limulus antilipopolysaccharide factor
    • Warren H.S., Glennon M.L., Wainwright N. et al. Binding and neutralization of endotoxin by Limulus antilipopolysaccharide factor. Infect Immun 1992; 60: 2506-2513.
    • (1992) Infect Immun , vol.60 , pp. 2506-2513
    • Warren, H.S.1    Glennon, M.L.2    Wainwright, N.3
  • 15
    • 0028110893 scopus 로고
    • Effect of a recombinant endotoxin-neutralizing protein on endotoxin shock in rabbits
    • Garcia C., Saladino R., Thompson C. et al. Effect of a recombinant endotoxin-neutralizing protein on endotoxin shock in rabbits. Crit Care Med 1994; 22: 1211-1218.
    • (1994) Crit Care Med , vol.22 , pp. 1211-1218
    • Garcia, C.1    Saladino, R.2    Thompson, C.3
  • 16
    • 0023700978 scopus 로고
    • Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure
    • Nakamura T., Furunaka H., Miyata T., Tokunaga F., Muta T., Iwanaga S. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure. J Biol Chem 1988; 263: 16709-16713.
    • (1988) J Biol Chem , vol.263 , pp. 16709-16713
    • Nakamura, T.1    Furunaka, H.2    Miyata, T.3    Tokunaga, F.4    Muta, T.5    Iwanaga, S.6
  • 17
    • 0024741960 scopus 로고
    • Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyhemusins I and II: Chemical structures and biological activity
    • Miyata T., Tokunaga F., Yoneya T. et al. Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyhemusins I and II: Chemical structures and biological activity. J Biochem 1989; 106: 663-668.
    • (1989) J Biochem , vol.106 , pp. 663-668
    • Miyata, T.1    Tokunaga, F.2    Yoneya, T.3
  • 18
    • 0029020955 scopus 로고
    • A novel big defensin identified in horseshoe crab hemocytes: Isolation, amino acid sequence, and antibacterial activity
    • Saito T., Kawabata S., Shigenaga T. et al. A novel big defensin identified in horseshoe crab hemocytes: isolation, amino acid sequence, and antibacterial activity. J Biochem 1995; 117: 1131-1137.
    • (1995) J Biochem , vol.117 , pp. 1131-1137
    • Saito, T.1    Kawabata, S.2    Shigenaga, T.3
  • 19
    • 0029257172 scopus 로고
    • Molecular cloning and sequence analysis of factor C cDNA from the Singapore horseshoe crab, Carcinoscorpius rotundicauda
    • Ding J.L., Navas III M.A.A., Ho B. Molecular cloning and sequence analysis of factor C cDNA from the Singapore horseshoe crab, Carcinoscorpius rotundicauda. Mol Mar Biol Biotech 1995; 4: 90-103.
    • (1995) Mol Mar Biol Biotech , vol.4 , pp. 90-103
    • Ding, J.L.1    Navas III, M.A.A.2    Ho, B.3
  • 20
    • 0030438090 scopus 로고    scopus 로고
    • Expression of Carcinoscorpius rotundicauda factor C in Pichia pastoris
    • Roopashree S.D., Ho B., Ding J.L. Expression of Carcinoscorpius rotundicauda factor C in Pichia pastoris. Mol Mar Biol Biotech 1996; 5: 334-343.
    • (1996) Mol Mar Biol Biotech , vol.5 , pp. 334-343
    • Roopashree, S.D.1    Ho, B.2    Ding, J.L.3
  • 21
    • 0000631035 scopus 로고
    • The role of endotoxin in the extracellular coagulation of Limulus blood
    • Levin J., Bang F.B. The role of endotoxin in the extracellular coagulation of Limulus blood. Bull John Hopkins Hosp 1964; 115: 265-274.
    • (1964) Bull John Hopkins Hosp , vol.115 , pp. 265-274
    • Levin, J.1    Bang, F.B.2
  • 22
    • 0023040655 scopus 로고
    • Lipopolysaccharide sensitive serine-protease zymogen (factor C) found in Limulus hemocytes: Isolation and characterisation
    • Nakamura T., Morita T., Iwanaga S. Lipopolysaccharide sensitive serine-protease zymogen (factor C) found in Limulus hemocytes: isolation and characterisation. Eur J Biochem 1986; 154: 511-521.
    • (1986) Eur J Biochem , vol.154 , pp. 511-521
    • Nakamura, T.1    Morita, T.2    Iwanaga, S.3
  • 23
    • 0023656119 scopus 로고
    • Lipopolysaccharide-sensitive serine protease zymogen (factor C) in horseshoe crab hemocytes: Identification and alignment of proteolytic fragments produced during the activation show that it is a novel type of serine protease
    • Tokunaga F., Miyata T., Nakamura T., Morita T., Kuma K. Lipopolysaccharide-sensitive serine protease zymogen (factor C) in horseshoe crab hemocytes: identification and alignment of proteolytic fragments produced during the activation show that it is a novel type of serine protease. Eur J Biochem 1987; 167: 405-416.
    • (1987) Eur J Biochem , vol.167 , pp. 405-416
    • Tokunaga, F.1    Miyata, T.2    Nakamura, T.3    Morita, T.4    Kuma, K.5
  • 24
    • 0021015452 scopus 로고
    • An improved Limulus gelation assay
    • Ho B. An improved Limulus gelation assay. Microbios Lett 1983; 24: 81-84.
    • (1983) Microbios Lett , vol.24 , pp. 81-84
    • Ho, B.1
  • 25
  • 26
    • 0030969606 scopus 로고    scopus 로고
    • Expression of full length and deletion homologs of Carcinoscorpius rotundicauda factor C in Saccharomyces cerevisiae: Immunoreactivity and endotoxin-binding
    • Ding J.L., Chai C., Fui A.W.M., Ho B. Expression of full length and deletion homologs of Carcinoscorpius rotundicauda factor C in Saccharomyces cerevisiae: immunoreactivity and endotoxin-binding. J Endotoxin Res 1997; 4: 33-43.
    • (1997) J Endotoxin Res , vol.4 , pp. 33-43
    • Ding, J.L.1    Chai, C.2    Fui, A.W.M.3    Ho, B.4
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for quantitation of microgram quantities of protein utilising the principle of protein-dye binding. Anal Biochem 1976; 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-684.
    • (1970) Nature , vol.227 , pp. 680-684
    • Laemmli, U.K.1
  • 30
    • 0014753036 scopus 로고
    • A simple method for the quantitation of submicrogram amounts of bacterial endotoxin
    • Pieroni R.E., Broderick E.J., Bundeally A., Levine L. A simple method for the quantitation of submicrogram amounts of bacterial endotoxin. Proc Soc Exp Biol Med 1971; 133: 790-794.
    • (1971) Proc Soc Exp Biol Med , vol.133 , pp. 790-794
    • Pieroni, R.E.1    Broderick, E.J.2    Bundeally, A.3    Levine, L.4
  • 31
    • 0020396289 scopus 로고
    • Possible alteration of normal mechanisms of endotoxin toxicity in vivo by actinomycin D
    • Brown D.E., Morrison D.C. Possible alteration of normal mechanisms of endotoxin toxicity in vivo by actinomycin D. J Infect Dis 1982; 146: 746-750.
    • (1982) J Infect Dis , vol.146 , pp. 746-750
    • Brown, D.E.1    Morrison, D.C.2
  • 34
    • 0023955490 scopus 로고
    • Interaction between lipopolysaccharide and intracellular serine protease zymogen, factor C, from horseshoe crab (Tachypleus tridentatus) hemocytes
    • Nakamura T., Tokunaga F., Morita T., Iwanaga S. Interaction between lipopolysaccharide and intracellular serine protease zymogen, factor C, from horseshoe crab (Tachypleus tridentatus) hemocytes. J Biochem 1988; 103: 370-374.
    • (1988) J Biochem , vol.103 , pp. 370-374
    • Nakamura, T.1    Tokunaga, F.2    Morita, T.3    Iwanaga, S.4
  • 35
    • 0027166219 scopus 로고
    • Selective removal of free dodecyl sulfate from 2-mercaptoethanol-SDS-solubilized proteins before KDS-protein precipitation
    • Sandri M., Rizzi C., Catani C., Carraro U. Selective removal of free dodecyl sulfate from 2-mercaptoethanol-SDS-solubilized proteins before KDS-protein precipitation. Anal Biochem 1993; 213: 34-39.
    • (1993) Anal Biochem , vol.213 , pp. 34-39
    • Sandri, M.1    Rizzi, C.2    Catani, C.3    Carraro, U.4
  • 36
    • 0020055346 scopus 로고
    • A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels
    • Tsai C.M., Frasch C.E. A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels. Anal Biochem 1982; 119: 115-119.
    • (1982) Anal Biochem , vol.119 , pp. 115-119
    • Tsai, C.M.1    Frasch, C.E.2
  • 37
    • 0025735356 scopus 로고
    • An endotoxin sensitive serine protease zymogen with a mosaic structure of complement-like, epidermal growth factor-like and lectin-like domains
    • Muta T., Miyata T., Misumi Y. et al. An endotoxin sensitive serine protease zymogen with a mosaic structure of complement-like, epidermal growth factor-like and lectin-like domains. J Biol Chem 1991; 266: 6554-6561.
    • (1991) J Biol Chem , vol.266 , pp. 6554-6561
    • Muta, T.1    Miyata, T.2    Misumi, Y.3
  • 38
    • 0026496324 scopus 로고
    • Preparation and properties of monoclonal antibodies against lipopolysaccharide-sensitive serine protease zymogen, factor C, from horseshoe crab (Tachypleus tridentatus) hemocytes
    • Miura Y., Tokunaga F., Miyata T., Moriyasu M., Yoshikawa K., Iwanaga S. Preparation and properties of monoclonal antibodies against lipopolysaccharide-sensitive serine protease zymogen, factor C, from horseshoe crab (Tachypleus tridentatus) hemocytes. J Biochem 1992; 112: 476-481.
    • (1992) J Biochem , vol.112 , pp. 476-481
    • Miura, Y.1    Tokunaga, F.2    Miyata, T.3    Moriyasu, M.4    Yoshikawa, K.5    Iwanaga, S.6
  • 39
    • 21144466610 scopus 로고
    • An antimicrobial factor from the plasma of the horseshoe crab, Carcinoscorpius rotundicauda
    • Yeo D.S.A., Ding J.L., Ho B. An antimicrobial factor from the plasma of the horseshoe crab, Carcinoscorpius rotundicauda. Microbios 1993; 73: 45-58.
    • (1993) Microbios , vol.73 , pp. 45-58
    • Yeo, D.S.A.1    Ding, J.L.2    Ho, B.3


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