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Volumn 238, Issue 3, 1996, Pages 728-736

Proteases from Trypanosoma brucei brucei: Purification, characterisation and interactions with host regulatory molecules

Author keywords

cystatin; cysteine proteinase; oligopeptidase; Trypanosoma brucei

Indexed keywords

ALPHA 2 MACROGLOBULIN; CYSTATIN C; NATRIURETIC FACTOR; NEUROTENSIN; PROTEINASE;

EID: 0030017685     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0728w.x     Document Type: Article
Times cited : (88)

References (47)
  • 1
    • 8944255452 scopus 로고
    • Cystatins-protein inhibitors of papain-like cysteine proteinases
    • Abrahamson, M. (1993) Cystatins-protein inhibitors of papain-like cysteine proteinases, Cienc. Cult. Soc. Bras. Progr. Cienc. 445, 299-304.
    • (1993) Cienc. Cult. Soc. Bras. Progr. Cienc. , vol.445 , pp. 299-304
    • Abrahamson, M.1
  • 2
    • 0025016911 scopus 로고
    • Characterisation of an alkaline peptidase of Trypanosoma cruzi and other trypanosomatids
    • Ashall, F. (1990) Characterisation of an alkaline peptidase of Trypanosoma cruzi and other trypanosomatids, Mol. Biochem. Parasitol. 38, 77-88
    • (1990) Mol. Biochem. Parasitol. , vol.38 , pp. 77-88
    • Ashall, F.1
  • 3
    • 0025141107 scopus 로고
    • Substrate specificity and inhibitor sensitivity of a trypanosomatid alkaline peptidase
    • Ashall, R., Harris, D., Roberts, H., Healy, N. & Shaw, E. (1990) Substrate specificity and inhibitor sensitivity of a trypanosomatid alkaline peptidase. Biochem. Biophys. Acta 1035, 293-299.
    • (1990) Biochem. Biophys. Acta , vol.1035 , pp. 293-299
    • Ashall, R.1    Harris, D.2    Roberts, H.3    Healy, N.4    Shaw, E.5
  • 4
    • 0027171858 scopus 로고
    • Antibody response to a 33 kDa cysteine protease of Trypanosoma congolense: Relationship to 'trypanotolerance' in cattle
    • Authié, E., Duvallet, G., Robertson, C. & Williams, D. J. L. (1993) Antibody response to a 33 kDa cysteine protease of Trypanosoma congolense: relationship to 'trypanotolerance' in cattle. Parasite Immunol. 15, 465-474.
    • (1993) Parasite Immunol. , vol.15 , pp. 465-474
    • Authié, E.1    Duvallet, G.2    Robertson, C.3    Williams, D.J.L.4
  • 5
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H and cathepsin L
    • Barrett, A. J. & Kirschke, H. (1981) Cathepsin B, cathepsin H and cathepsin L. Methods Enzymol. 80C, 535-561.
    • (1981) Methods Enzymol. , vol.80 C , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 6
    • 0002486962 scopus 로고
    • Cysteine proteinase inhibitors of the cystatin superfamily
    • Barrett, A. J. & Salvesen, G., eds Elsevier, Amsterdam
    • Barrett, A. J., Rawlings, N. D., Davies, M. B., Machleidt, W., Salvesen, G. & Turk, V. (1986) Cysteine proteinase inhibitors of the cystatin superfamily, in Proteinase inhibitors (Barrett, A. J. & Salvesen, G., eds) pp. 515-569, Elsevier, Amsterdam.
    • (1986) Proteinase Inhibitors , pp. 515-569
    • Barrett, A.J.1    Rawlings, N.D.2    Davies, M.B.3    Machleidt, W.4    Salvesen, G.5    Turk, V.6
  • 7
    • 0019282838 scopus 로고
    • Pathophysiological interpretation of kinetic constants of protease inhibitors
    • Bieth, J. G. (1980) Pathophysiological interpretation of kinetic constants of protease inhibitors. Bull. Eur. Physiopathlol. Respir. 16, 183-195.
    • (1980) Bull. Eur. Physiopathlol. Respir. , vol.16 , pp. 183-195
    • Bieth, J.G.1
  • 8
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins. RNA and DNA in polyacrylamide gels
    • Blum, H., Beier, H. & Gross, H. J. (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    Gross, H.J.3
  • 11
    • 0024491490 scopus 로고
    • Further characterization and partial amino acid sequence of a cysteine proteinase from Trypanosoma cruzi
    • Cazzulo, J. J., Couso, R., Raimondi, A., Wernstedt, C. & Hellman, U. (1989) Further characterization and partial amino acid sequence of a cysteine proteinase from Trypanosoma cruzi. Mol. Biochem. Parasitol. 33, 33-42.
    • (1989) Mol. Biochem. Parasitol. , vol.33 , pp. 33-42
    • Cazzulo, J.J.1    Couso, R.2    Raimondi, A.3    Wernstedt, C.4    Hellman, U.5
  • 13
    • 0017275077 scopus 로고
    • Human kallikrein and prekallikrein
    • Coleman, R. W. & Bagdasarian, A. (1976) Human kallikrein and prekallikrein, in Methods Enzymol. 45B, 303-322.
    • (1976) Methods Enzymol. , vol.45 B , pp. 303-322
    • Coleman, R.W.1    Bagdasarian, A.2
  • 14
    • 0026890596 scopus 로고
    • Characterisation of the activity and stability of single-chain cathepsin L and of proteolytically active cathepsin L/cystatin complexes
    • Dennison, C., Pike, R., Coetzer, T. & Kirk, K. (1992) Characterisation of the activity and stability of single-chain cathepsin L and of proteolytically active cathepsin L/cystatin complexes, Biol. Chem. Hoppe-Seyler 373, 419-425.
    • (1992) Biol. Chem. Hoppe-Seyler , vol.373 , pp. 419-425
    • Dennison, C.1    Pike, R.2    Coetzer, T.3    Kirk, K.4
  • 15
    • 0023992412 scopus 로고
    • Proteolytic specificity of chicken cathepsin L on bovine β-casein
    • Dufour, E. & Ribadeau-Dumas, B. (1988) Proteolytic specificity of chicken cathepsin L on bovine β-casein, Biosci. Rep. 8, 185-191.
    • (1988) Biosci. Rep. , vol.8 , pp. 185-191
    • Dufour, E.1    Ribadeau-Dumas, B.2
  • 16
    • 0026781519 scopus 로고
    • The sequence, organisation and expression of the major cysteine protease (cruzipain) from Trypanosoma cruzi
    • Eakin, A. E., Mills, A. A., Harth, G., McKerrow, J. H. & Craik, C. S. (1992) The sequence, organisation and expression of the major cysteine protease (cruzipain) from Trypanosoma cruzi, J. Biol. Chem. 267, 7411-7420.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7411-7420
    • Eakin, A.E.1    Mills, A.A.2    Harth, G.3    McKerrow, J.H.4    Craik, C.S.5
  • 17
    • 0016167076 scopus 로고
    • The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters
    • Eisenthal, R. & Cornish-Bowden, A. (1974) The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters, Biochem. J. 139, 715-720.
    • (1974) Biochem. J. , vol.139 , pp. 715-720
    • Eisenthal, R.1    Cornish-Bowden, A.2
  • 18
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying pH-dependent processes
    • Ellis, K. J. & Morrison, J. F. (1982) Buffers of constant ionic strength for studying pH-dependent processes, Methods Enzymol. 87C, 405-426.
    • (1982) Methods Enzymol. , vol.87 C , pp. 405-426
    • Ellis, K.J.1    Morrison, J.F.2
  • 19
    • 0029130537 scopus 로고
    • The cDNA and deduced amino acid sequence of a cysteine protease from Trypanosoma (Nannomonas) congolense metacyclic forms
    • Fish, W. R., Nkhungulu, Z. M., Muriuki, C. W., Ndegwa, D. M., Lonsdale-Eccles, J. D. & Steyaert, J. (1995) The cDNA and deduced amino acid sequence of a cysteine protease from Trypanosoma (Nannomonas) congolense metacyclic forms, Gene 161, 125-128.
    • (1995) Gene , vol.161 , pp. 125-128
    • Fish, W.R.1    Nkhungulu, Z.M.2    Muriuki, C.W.3    Ndegwa, D.M.4    Lonsdale-Eccles, J.D.5    Steyaert, J.6
  • 20
    • 0021134026 scopus 로고
    • Human plasma α-cysteine proteinase inhibitor
    • Gounaris, A. D., Brown, M. A. & Barrett, A. J. (1984) Human plasma α-cysteine proteinase inhibitor, Biochem. J. 221, 445-452.
    • (1984) Biochem. J. , vol.221 , pp. 445-452
    • Gounaris, A.D.1    Brown, M.A.2    Barrett, A.J.3
  • 21
    • 0020463847 scopus 로고
    • Isopycnic isolation of African trypanosomes on Percoll gradients formed in situ
    • Grab, D. J. & Bwayo, J. J. (1982) Isopycnic isolation of African trypanosomes on Percoll gradients formed in situ, Acta Trop. 39, 363-366.
    • (1982) Acta Trop. , vol.39 , pp. 363-366
    • Grab, D.J.1    Bwayo, J.J.2
  • 22
    • 8944231947 scopus 로고
    • A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors
    • Henderson, P. J. F. (1972) A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors, Biochem. J. 102, 193-202.
    • (1972) Biochem. J. , vol.102 , pp. 193-202
    • Henderson, P.J.F.1
  • 24
    • 0022843745 scopus 로고
    • Cathepsin L inactivates -proteinase inhibitor by cleavage in the active site region
    • Johnson, D. A., Barrett, A. J. & Mason, R. W. (1986) Cathepsin L inactivates -proteinase inhibitor by cleavage in the active site region, J. Biol. Chem. 261, 14748-14751.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14748-14751
    • Johnson, D.A.1    Barrett, A.J.2    Mason, R.W.3
  • 26
    • 0014884946 scopus 로고
    • Isolation of salivarian trypanosomes from man and other mammals using DEAE-cellulose
    • Lanham, S. M. & Godfrey, D. G (1970) Isolation of salivarian trypanosomes from man and other mammals using DEAE-cellulose. Exp. Parasitol. 25, 521-534.
    • (1970) Exp. Parasitol. , vol.25 , pp. 521-534
    • Lanham, S.M.1    Godfrey, D.G.2
  • 27
    • 0026620531 scopus 로고
    • Temperature-dependent substrate inhibition of the cysteine proteinase (GP57/51) from Trypanosoma cruzi
    • Lima, A. P. C. A., Scharfstein, J., Storer, A. C. & Ménard, R. (1992) Temperature-dependent substrate inhibition of the cysteine proteinase (GP57/51) from Trypanosoma cruzi, Mol. Biochem. Parasitol. 56, 335-338.
    • (1992) Mol. Biochem. Parasitol. , vol.56 , pp. 335-338
    • Lima, A.P.C.A.1    Scharfstein, J.2    Storer, A.C.3    Ménard, R.4
  • 29
    • 0024470378 scopus 로고
    • 2-macroglobulin: Conclusive evidence for the endopeptidase activities of cathepsins B and H
    • 2-macroglobulin: conclusive evidence for the endopeptidase activities of cathepsins B and H, Arch. Biochem. Biophys. 273, 367-374.
    • (1989) Arch. Biochem. Biophys. , vol.273 , pp. 367-374
    • Mason, R.W.1
  • 30
    • 0026320433 scopus 로고
    • Immunolocalisation of a cysteine protease within the lysosomal system of Trypanosoma congolense
    • Mbawa, Z. R., Webster, P. & Lonsdale-Eccles, J. D. (1991) Immunolocalisation of a cysteine protease within the lysosomal system of Trypanosoma congolense, Eur. J. Cell Biol. 56, 243-250.
    • (1991) Eur. J. Cell Biol. , vol.56 , pp. 243-250
    • Mbawa, Z.R.1    Webster, P.2    Lonsdale-Eccles, J.D.3
  • 31
    • 0026541179 scopus 로고
    • Characterisation of a cysteine protease from bloodstream forms of Trypanosoma congolense
    • Mbawa, Z. R., Gumm, I. D., Shaw, E. & Lonsdale-Eccles, J. D. (1992) Characterisation of a cysteine protease from bloodstream forms of Trypanosoma congolense, Eur. J. Biochem. 204, 371-379.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 371-379
    • Mbawa, Z.R.1    Gumm, I.D.2    Shaw, E.3    Lonsdale-Eccles, J.D.4
  • 32
    • 0024329436 scopus 로고
    • A cysteine protease cDNA from Trypanosoma brucei predicts an enzyme with an unusual C-terminal extension
    • Mottram, J. C., North, M. J., Barry, J. D. & Coombs, G. H. (1989) A cysteine protease cDNA from Trypanosoma brucei predicts an enzyme with an unusual C-terminal extension. FEBS Lett. 258, 211-215.
    • (1989) FEBS Lett. , vol.258 , pp. 211-215
    • Mottram, J.C.1    North, M.J.2    Barry, J.D.3    Coombs, G.H.4
  • 35
    • 0024575730 scopus 로고
    • Identification of a developmentally regulated cysteine protease of Trypanosoma brucei
    • Pamer, E. G., So, M. & Davis, C. E. (1989) Identification of a developmentally regulated cysteine protease of Trypanosoma brucei, Mol. Biochem. Parasitol. 33, 27-32.
    • (1989) Mol. Biochem. Parasitol. , vol.33 , pp. 27-32
    • Pamer, E.G.1    So, M.2    Davis, C.E.3
  • 36
    • 0025064553 scopus 로고
    • Cloning and sequencing of the cysteine protease cDNA from Trypanosoma brucei rhodescience
    • Pamer, E. G., Davis, C. E., Eakin, A. & So, M. (1990) Cloning and sequencing of the cysteine protease cDNA from Trypanosoma brucei rhodescience, Nucleic Acids Res. 18, 6164.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6164
    • Pamer, E.G.1    Davis, C.E.2    Eakin, A.3    So, M.4
  • 37
    • 0025977356 scopus 로고
    • Expression and deletion analysis of the Trypanosoma brucei rhodesiense cysteine proteinase in Escherichia coli
    • Pamer, E. G., Davis, C. E. & So, M. (1991) Expression and deletion analysis of the Trypanosoma brucei rhodesiense cysteine proteinase in Escherichia coli. Infect. Immun. 59, 1074-1078.
    • (1991) Infect. Immun. , vol.59 , pp. 1074-1078
    • Pamer, E.G.1    Davis, C.E.2    So, M.3
  • 38
    • 0024503879 scopus 로고
    • Protein fractionation by three-phase partitioning (TPP) in aqueous/t-butanol mixtures
    • Pike, R. N. & Dennison, C. (1989) Protein fractionation by three-phase partitioning (TPP) in aqueous/t-butanol mixtures, Biotech. Bioeng. 33, 221-228.
    • (1989) Biotech. Bioeng. , vol.33 , pp. 221-228
    • Pike, R.N.1    Dennison, C.2
  • 39
    • 0026708693 scopus 로고
    • Proteolytically active complexes of cathepsin L and a cysteine proteinase inhibitor: Purification and demonstration of their formation in vitro
    • Pike, R. N., Coetzer, T. H. T. & Dennison, C. (1992) Proteolytically active complexes of cathepsin L and a cysteine proteinase inhibitor: purification and demonstration of their formation in vitro, Arch. Biochem. Biophys. 294, 623-629.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 623-629
    • Pike, R.N.1    Coetzer, T.H.T.2    Dennison, C.3
  • 40
    • 0023031993 scopus 로고
    • The inactivation of human plasma alpha-1-proteinase inhibitor by proteinases from Staphylococcus aureus
    • Potempa, J., Watorek, W. & Travis, J. (1986) The inactivation of human plasma alpha-1-proteinase inhibitor by proteinases from Staphylococcus aureus, J. Biol. Chem. 261, 14330-14334.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14330-14334
    • Potempa, J.1    Watorek, W.2    Travis, J.3
  • 41
    • 0019776662 scopus 로고
    • Minimization of variation in the response to different proteins of the Coomassie Blue dye-binding assay for protein
    • Read, S. M. & Northcote, D. H. (1981) Minimization of variation in the response to different proteins of the Coomassie Blue dye-binding assay for protein. Anal. Biochem. 116, 53 64.
    • (1981) Anal. Biochem. , vol.116 , pp. 53-64
    • Read, S.M.1    Northcote, D.H.2
  • 42
    • 0028120474 scopus 로고
    • Directional movement of variable surface glycoprotein-antibody complexes in Trypanosoma brucei
    • Russo, D. C. W., Williams, D. J. L. & Grab, D. J. (1994) Directional movement of variable surface glycoprotein-antibody complexes in Trypanosoma brucei, Parasitol. Res. 80, 487 492.
    • (1994) Parasitol. Res. , vol.80 , pp. 487-492
    • Russo, D.C.W.1    Williams, D.J.L.2    Grab, D.J.3
  • 43
    • 0002006941 scopus 로고
    • Inhibition of proteolytic enzymes
    • Benyon. R. J. & Bond, J. S., eds IRL Press, Oxford
    • Salvesen, G. & Nagase, H. (1992) Inhibition of proteolytic enzymes, in Proteolytic enzymes: a practical approach (Benyon. R. J. & Bond, J. S., eds) pp. 83-104, IRL Press, Oxford.
    • (1992) Proteolytic Enzymes: A Practical Approach , pp. 83-104
    • Salvesen, G.1    Nagase, H.2
  • 44
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Shägger, H. & von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368 379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Shägger, H.1    Von Jagow, G.2
  • 46
    • 0018219029 scopus 로고
    • Biologically active products from African trspanosomes
    • Tizard, I., Nielsen, K. H., Seed, J. R. & Hall, J. E. (1978) Biologically active products from African trspanosomes. Microbiol. Rev. 42, 661-681.
    • (1978) Microbiol. Rev. , vol.42 , pp. 661-681
    • Tizard, I.1    Nielsen, K.H.2    Seed, J.R.3    Hall, J.E.4
  • 47
    • 0007729901 scopus 로고
    • Sleeping sickness on the boil in Zaire
    • Walgate, R. (1994) Sleeping sickness on the boil in Zaire. TDR News 46, 6.
    • (1994) TDR News , vol.46 , pp. 6
    • Walgate, R.1


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