메뉴 건너뛰기




Volumn 39, Issue 1, 2006, Pages 28-31

Inhibition of Clostridium histolyticum supernatant cytotoxic activity by protease inhibitors

Author keywords

Clostridium histolyticum; Cytotoxicity; Protease inhibitors

Indexed keywords

AMINO ACIDS; CELLS; CYTOLOGY; ENZYME INHIBITION; FLUORIDE MINERALS; HISTOLOGY; TOXICITY;

EID: 33646021917     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2005.09.002     Document Type: Article
Times cited : (4)

References (27)
  • 2
    • 0036841750 scopus 로고    scopus 로고
    • An outbreak of serious illness and death among injecting drug users in England during
    • Jones J.A., Salmon J.E., and Djuretic D. An outbreak of serious illness and death among injecting drug users in England during. J Med Microbiol 51 (2002) 978-984
    • (2002) J Med Microbiol , vol.51 , pp. 978-984
    • Jones, J.A.1    Salmon, J.E.2    Djuretic, D.3
  • 3
    • 15044365476 scopus 로고    scopus 로고
    • Outbreak of C. histolyticum infections in injecting drug users in England and Scotland
    • Brazier J.S., Gai M., and Morris T.E. Outbreak of C. histolyticum infections in injecting drug users in England and Scotland. Eur Surveill 1 (2004) 1-9
    • (2004) Eur Surveill , vol.1 , pp. 1-9
    • Brazier, J.S.1    Gai, M.2    Morris, T.E.3
  • 4
    • 0013851546 scopus 로고
    • Isolation and characterization of collagenases I and II from Clostridium histolyticum
    • Yoshida E., and Noda H. Isolation and characterization of collagenases I and II from Clostridium histolyticum. Biochim Biophys Acta 105 (1965) 562-574
    • (1965) Biochim Biophys Acta , vol.105 , pp. 562-574
    • Yoshida, E.1    Noda, H.2
  • 5
    • 0015924258 scopus 로고
    • Isolation by affinity chromatography of neutral protease from Clostridium histolyticum
    • Sparrow L.G., and McQuade A.B. Isolation by affinity chromatography of neutral protease from Clostridium histolyticum. Biochim Biophys Acta 302 (1973) 90-94
    • (1973) Biochim Biophys Acta , vol.302 , pp. 90-94
    • Sparrow, L.G.1    McQuade, A.B.2
  • 6
    • 0017278814 scopus 로고
    • Consecutive use of omega-aminoalkylagaroses. Resolution and purification of clostripain and collagenase from Clostridium histolyticum
    • Kula M.R., Hatef-Haghi D., Tauber-Finkelstein M., and Shaltiel S. Consecutive use of omega-aminoalkylagaroses. Resolution and purification of clostripain and collagenase from Clostridium histolyticum. Biochem Biophys Res Commun 69 (1976) 389-396
    • (1976) Biochem Biophys Res Commun , vol.69 , pp. 389-396
    • Kula, M.R.1    Hatef-Haghi, D.2    Tauber-Finkelstein, M.3    Shaltiel, S.4
  • 7
    • 0015933322 scopus 로고
    • A novel aminopeptidase from Clostridium histolyticum
    • Kessler E., and Yaron A. A novel aminopeptidase from Clostridium histolyticum. Biochem Biophys Res Commun 50 (1973) 405-412
    • (1973) Biochem Biophys Res Commun , vol.50 , pp. 405-412
    • Kessler, E.1    Yaron, A.2
  • 8
    • 0015953315 scopus 로고
    • The presence of a factor toxic to pancreatic beta cells in some collagenase preparations
    • Moskalewski S., Sochanska K.R., and Wiwatowski T. The presence of a factor toxic to pancreatic beta cells in some collagenase preparations. Bull Acad Pol Sci Biol 22 (1974) 127-130
    • (1974) Bull Acad Pol Sci Biol , vol.22 , pp. 127-130
    • Moskalewski, S.1    Sochanska, K.R.2    Wiwatowski, T.3
  • 9
    • 0019568482 scopus 로고
    • Enzymatic isolation of cells from bone: cytotoxic enzymes of bacterial collagenase
    • Hefley T., Cushing J., and Brand J.S. Enzymatic isolation of cells from bone: cytotoxic enzymes of bacterial collagenase. Am J Physiol 240 (1981) C234-C238
    • (1981) Am J Physiol , vol.240
    • Hefley, T.1    Cushing, J.2    Brand, J.S.3
  • 10
    • 0014357213 scopus 로고
    • Obtaining highly purified preparations of C. histolyticum lethal factor
    • Shemanova G.F., Vlasova E.V., and Shamraeva S.A. Obtaining highly purified preparations of C. histolyticum lethal factor. Vopr Med Khim 14 (1968) 632-635
    • (1968) Vopr Med Khim , vol.14 , pp. 632-635
    • Shemanova, G.F.1    Vlasova, E.V.2    Shamraeva, S.A.3
  • 11
    • 0021269574 scopus 로고
    • Comparison of in vitro cell cytotoxic assays for tumor necrosis factor
    • Flick D.A., and Gifford G.E. Comparison of in vitro cell cytotoxic assays for tumor necrosis factor. J Immunol Methods 68 (1984) 167-175
    • (1984) J Immunol Methods , vol.68 , pp. 167-175
    • Flick, D.A.1    Gifford, G.E.2
  • 12
    • 0015240482 scopus 로고
    • Studies on the active site of clostripain. The specific inactivation by the chloromethyl ketone derived from a-N-Tosyl-l-Lysine
    • Porter W., Cunningham L., and Mitchell W. Studies on the active site of clostripain. The specific inactivation by the chloromethyl ketone derived from a-N-Tosyl-l-Lysine. J Biol Chem 246 (1971) 7675-7682
    • (1971) J Biol Chem , vol.246 , pp. 7675-7682
    • Porter, W.1    Cunningham, L.2    Mitchell, W.3
  • 13
    • 0025352351 scopus 로고
    • Proteolysis of Clostridium perfringens type A enterotoxin during purification
    • Park K.B., and Labbe R.G. Proteolysis of Clostridium perfringens type A enterotoxin during purification. Infect Immun 58 (1990) 1999-2001
    • (1990) Infect Immun , vol.58 , pp. 1999-2001
    • Park, K.B.1    Labbe, R.G.2
  • 14
    • 77956984806 scopus 로고
    • Bovine trypsin-kallikrein inhibitor
    • Kassel B. Bovine trypsin-kallikrein inhibitor. Method Enzymol 19 (1970) 844-852
    • (1970) Method Enzymol , vol.19 , pp. 844-852
    • Kassel, B.1
  • 15
    • 0019795411 scopus 로고
    • A rationale for the application of trasylol as a protease inhibitor in radioimmunoassay
    • Zyznar E.S. A rationale for the application of trasylol as a protease inhibitor in radioimmunoassay. Life Sci 27 (1981) 1861-1866
    • (1981) Life Sci , vol.27 , pp. 1861-1866
    • Zyznar, E.S.1
  • 16
    • 0025064952 scopus 로고
    • Apropos aprotinin: a review
    • 568
    • Hewlett G. Apropos aprotinin: a review. Biotechnology (NY) 8 (1990) 565-566 568
    • (1990) Biotechnology (NY) , vol.8 , pp. 565-566
    • Hewlett, G.1
  • 17
    • 0028430199 scopus 로고
    • Characterization of striped bass growth hormone receptors by disulfide-bond reduction and cross-linking studies
    • Gray E.S., and Tsai R.W. Characterization of striped bass growth hormone receptors by disulfide-bond reduction and cross-linking studies. J Exp Zool 268 (1994) 428-435
    • (1994) J Exp Zool , vol.268 , pp. 428-435
    • Gray, E.S.1    Tsai, R.W.2
  • 18
    • 0020075452 scopus 로고
    • Cultivation of mouse cerebellar cells in serum free, hormonally defined media: survival of neurons
    • Fischer G. Cultivation of mouse cerebellar cells in serum free, hormonally defined media: survival of neurons. Neurosci Lett 28 (1982) 325-329
    • (1982) Neurosci Lett , vol.28 , pp. 325-329
    • Fischer, G.1
  • 19
    • 0022462360 scopus 로고
    • Collagenase inhibition in colonic mucosa by protease inhibitors
    • Lewin M.R., Chowcat N.L., Jayaraj A.P., and Boulos P.B. Collagenase inhibition in colonic mucosa by protease inhibitors. Br J Exp Pathol 67 (1986) 523-526
    • (1986) Br J Exp Pathol , vol.67 , pp. 523-526
    • Lewin, M.R.1    Chowcat, N.L.2    Jayaraj, A.P.3    Boulos, P.B.4
  • 21
    • 0035696310 scopus 로고    scopus 로고
    • Characterization of an important enzymatic component in collagenase that is essential for the effective digestion of the human and porcine pancreas
    • Chen R.L., and James R.F. Characterization of an important enzymatic component in collagenase that is essential for the effective digestion of the human and porcine pancreas. Cell Transplant 10 (2001) 709-716
    • (2001) Cell Transplant , vol.10 , pp. 709-716
    • Chen, R.L.1    James, R.F.2
  • 22
    • 0036239635 scopus 로고    scopus 로고
    • Proteome and transcriptome analysis of the virulence genes regulated by the VirR/VirS system in Clostridium perfringens
    • Shimizu T., Shima K., Yoshino K., Yonezawa K., Shimizu T., and Hayashi H. Proteome and transcriptome analysis of the virulence genes regulated by the VirR/VirS system in Clostridium perfringens. J Bacteriol 184 (2002) 2587-2594
    • (2002) J Bacteriol , vol.184 , pp. 2587-2594
    • Shimizu, T.1    Shima, K.2    Yoshino, K.3    Yonezawa, K.4    Shimizu, T.5    Hayashi, H.6
  • 24
    • 0025367873 scopus 로고
    • Interaction of Clostridium difficile toxin A with cultured cells: cytoskeletal changes and nuclear polarization
    • Fiorentini C., Malorni W., Paradisi S., Giuliano M., Mastrantonio P., and Donelli G. Interaction of Clostridium difficile toxin A with cultured cells: cytoskeletal changes and nuclear polarization. Infect Immun 58 (1990) 2329-2336
    • (1990) Infect Immun , vol.58 , pp. 2329-2336
    • Fiorentini, C.1    Malorni, W.2    Paradisi, S.3    Giuliano, M.4    Mastrantonio, P.5    Donelli, G.6
  • 25
    • 0022443783 scopus 로고
    • Lysosomal involvement in cellular intoxication with Clostridium difficile toxin B
    • Florin I., and Thelestam M. Lysosomal involvement in cellular intoxication with Clostridium difficile toxin B. Microb Pathogenesis 1 (1986) 373-385
    • (1986) Microb Pathogenesis , vol.1 , pp. 373-385
    • Florin, I.1    Thelestam, M.2
  • 26
    • 0018786290 scopus 로고
    • Chemical chacterization, activity, and thiol content of the highly active form of clostripain
    • Gilles A., Imhoff J., and Keil B. Chemical chacterization, activity, and thiol content of the highly active form of clostripain. J Biol Chem 254 (1979) 1462-1468
    • (1979) J Biol Chem , vol.254 , pp. 1462-1468
    • Gilles, A.1    Imhoff, J.2    Keil, B.3
  • 27
    • 33646042268 scopus 로고
    • The partial purification of the lethal toxin of Clostridium histolyticum
    • Bowen H.E. The partial purification of the lethal toxin of Clostridium histolyticum. Yale J Biol Med 25 (1952) 124-130
    • (1952) Yale J Biol Med , vol.25 , pp. 124-130
    • Bowen, H.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.