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Volumn 259, Issue 1-2, 1999, Pages 275-280

Discrimination of cruzipain, the major cysteine proteinase of Trypanosoma cruzi, and mammalian cathepsins B and L, by a pH-inducible fluorogenic substrate of trypanosomal cysteine proteinases

Author keywords

Cruzipain; Cysteine proteinase; Enzyme specificity

Indexed keywords

CATHEPSIN B; CRUZIPAIN; CYSTEINE PROTEINASE;

EID: 0033555294     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00032.x     Document Type: Article
Times cited : (22)

References (38)
  • 1
    • 0029045156 scopus 로고
    • The proteases and pathogenicity of parasitic protozoa
    • McKerrow, J.H., McGrath, M.E. & Engel, J.C. (1995) The proteases and pathogenicity of parasitic protozoa. Parasitol. Today 11, 279-282.
    • (1995) Parasitol. Today , vol.11 , pp. 279-282
    • McKerrow, J.H.1    McGrath, M.E.2    Engel, J.C.3
  • 2
    • 0026606269 scopus 로고
    • Inhibitors of the major cysteinyl proteinase (GP57/51) impair host cell invasion and arrest the intracellular developement of Trypanosoma cruzi in vitro
    • Meirelles, M.N.L., Juliano, L., Carmona, E., Silva, S.G., Costa, E.M., Murta, A.C.M. & Scharfstein, J. (1992) Inhibitors of the major cysteinyl proteinase (GP57/51) impair host cell invasion and arrest the intracellular developement of Trypanosoma cruzi in vitro. Mol. Biochem. Parasitol. 52, 175-184.
    • (1992) Mol. Biochem. Parasitol. , vol.52 , pp. 175-184
    • Meirelles, M.N.L.1    Juliano, L.2    Carmona, E.3    Silva, S.G.4    Costa, E.M.5    Murta, A.C.M.6    Scharfstein, J.7
  • 3
    • 0027428152 scopus 로고
    • The cysteine protease of Trypanosoma cruzi as a model for antiparasite drug design
    • McKerrow, J.H., Sun, E., Rosenthal, P.J. & Bouvier, J. (1993) The cysteine protease of Trypanosoma cruzi as a model for antiparasite drug design. Annu. Rev. Microbiol. 47, 821-853.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 821-853
    • McKerrow, J.H.1    Sun, E.2    Rosenthal, P.J.3    Bouvier, J.4
  • 7
    • 0030034874 scopus 로고    scopus 로고
    • Investigation of the substrate specificity of cruzipain, the major cysteine proteinase of Trypanosoma cruzi, through the use of cystatin-derived substrates and inhibitors
    • Serveau, C., Lalmanach, G., Juliano, M.A., Scharfstein, J., Juliano, L. & Gauthier, F. (1996) Investigation of the substrate specificity of cruzipain, the major cysteine proteinase of Trypanosoma cruzi, through the use of cystatin-derived substrates and inhibitors. Biochem. J. 313, 951-956.
    • (1996) Biochem. J. , vol.313 , pp. 951-956
    • Serveau, C.1    Lalmanach, G.2    Juliano, M.A.3    Scharfstein, J.4    Juliano, L.5    Gauthier, F.6
  • 8
    • 0030891637 scopus 로고    scopus 로고
    • Characterization of the substrate specificity of the major cysteine protease (cruzipain) from Trypanosoma cruzi using a portion-mixing combinatorial library and fluorogenic peptides
    • Del Nery, E., Juliano, M.A., Meldal, M., Svendsen, I., Scharfstein, J., Walmsley, A. & Juliano, L. (1997) Characterization of the substrate specificity of the major cysteine protease (cruzipain) from Trypanosoma cruzi using a portion-mixing combinatorial library and fluorogenic peptides. Biochem. J. 323, 427-433.
    • (1997) Biochem. J. , vol.323 , pp. 427-433
    • Del Nery, E.1    Juliano, M.A.2    Meldal, M.3    Svendsen, I.4    Scharfstein, J.5    Walmsley, A.6    Juliano, L.7
  • 9
    • 0028908350 scopus 로고
    • Crystal structure of cathepsin B inhibited with CA030 at 2.0 Å, resolution: A basis for the design of specific epoxysucinyl inhibitors
    • Turk, D., Podobnik, M., Popovic, T., Katunuma, N., Bode, W., Huber, R. & Turk, V. (1995) Crystal structure of cathepsin B inhibited with CA030 at 2.0 Å, resolution: a basis for the design of specific epoxysucinyl inhibitors. Biochemistry 34, 4791-4797.
    • (1995) Biochemistry , vol.34 , pp. 4791-4797
    • Turk, D.1    Podobnik, M.2    Popovic, T.3    Katunuma, N.4    Bode, W.5    Huber, R.6    Turk, V.7
  • 10
    • 0026781519 scopus 로고
    • The sequence, organization and expression of the major cysteine protease (cruzain) from Trypanosoma cruzi
    • Eakin, A.E., Mills, A.A., Harth, G., McKerrow, J. H. & Craik, C.S. (1992) The sequence, organization and expression of the major cysteine protease (cruzain) 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
  • 11
    • 0023900059 scopus 로고
    • Cysteine proteinase inhibiting function of T-kininogen and of its proteolytic fragments
    • Moreau, T., Gutman, N., El Moujahed, A., Esnard, F. & Gauthier, F. (1988) Cysteine proteinase inhibiting function of T-kininogen and of its proteolytic fragments. Eur. J. Biochem. 173, 185-190.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 185-190
    • Moreau, T.1    Gutman, N.2    El Moujahed, A.3    Esnard, F.4    Gauthier, F.5
  • 12
    • 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
  • 13
    • 0019948262 scopus 로고
    • Ltrans-epoxysuccinylleucylamido (4-guanidino) butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
    • Barrett, A.J., Kembhavi, A.A., Brown, M.A., Kirschke, H., Knight, C.G., Tamai, M. & Hanada, K. (1982) Ltrans-epoxysuccinylleucylamido (4-guanidino) butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem. J. 201, 189-198.
    • (1982) Biochem. J. , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3    Kirschke, H.4    Knight, C.G.5    Tamai, M.6    Hanada, K.7
  • 15
    • 34249758919 scopus 로고
    • Internally quenched fluorogenic protease substrates: Solid phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs
    • Hirata, I.Y., Cezari, M.H.S., Nakaie, C.R., Boschcov, P., Ito, A.S., Juliano, M.A. & Juliano, L. (1994) Internally quenched fluorogenic protease substrates: solid phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs. Lett. Pept. Sci. 1, 299-308.
    • (1994) Lett. Pept. Sci. , vol.1 , pp. 299-308
    • Hirata, I.Y.1    Cezari, M.H.S.2    Nakaie, C.R.3    Boschcov, P.4    Ito, A.S.5    Juliano, M.A.6    Juliano, L.7
  • 16
    • 0025967144 scopus 로고
    • Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins
    • Chagas, J.R., Juliano, L. & Prado, E. (1991) Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins. Analyt. Biochem. 192, 419-425.
    • (1991) Analyt. Biochem. , vol.192 , pp. 419-425
    • Chagas, J.R.1    Juliano, L.2    Prado, E.3
  • 20
    • 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. 80, 535-561.
    • (1981) Methods Enzymol. , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 21
    • 0023655650 scopus 로고
    • Enzyme-substrate interaction in the hydrolysis of peptides by cathepsins B and H from rat liver
    • Brömme, D., Bescherer, K., Kirschke, H. & Fittkau, S. (1987) Enzyme-substrate interaction in the hydrolysis of peptides by cathepsins B and H from rat liver. Biochem. J. 245, 381-385.
    • (1987) Biochem. J. , vol.245 , pp. 381-385
    • Brömme, D.1    Bescherer, K.2    Kirschke, H.3    Fittkau, S.4
  • 22
    • 0025802686 scopus 로고
    • A model to explain the pH-dependent specificity of cathepsin B-catalysed hydrolysis
    • Khouri, H.E., Plouffe, C., Hasnain, S., Hirama, T., Storer, A.C. & Ménard, R. (1991) A model to explain the pH-dependent specificity of cathepsin B-catalysed hydrolysis. Biochem. J. 275, 751-757.
    • (1991) Biochem. J. , vol.275 , pp. 751-757
    • Khouri, H.E.1    Plouffe, C.2    Hasnain, S.3    Hirama, T.4    Storer, A.C.5    Ménard, R.6
  • 24
    • 0030841381 scopus 로고    scopus 로고
    • Structural determinants of specificity in the cysteine protease cruzain
    • Gillmor, S.A., Craik, C.S. & Fletterick, R.J. (1997) Structural determinants of specificity in the cysteine protease cruzain. Protein Science 6, 1603-1611.
    • (1997) Protein Science , vol.6 , pp. 1603-1611
    • Gillmor, S.A.1    Craik, C.S.2    Fletterick, R.J.3
  • 26
    • 0030744398 scopus 로고    scopus 로고
    • A comparison of the enzymatic properties of the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi
    • Chagas, J., Authié, E., Serveau, C., Lalmanach, G., Juliano, L. & Gauthier, F. (1997) A comparison of the enzymatic properties of the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi. Mol. Biochem. Parasitol. 88, 85-94.
    • (1997) Mol. Biochem. Parasitol. , vol.88 , pp. 85-94
    • Chagas, J.1    Authié, E.2    Serveau, C.3    Lalmanach, G.4    Juliano, L.5    Gauthier, F.6
  • 27
    • 0028337023 scopus 로고
    • New substrates of papain, based on the conserved sequence of natural inhibitors of the cystatin family
    • Serveau, C., Juliano, L., Bernard, P., Moreau, T., Mayer, R. & Gauthier, F. (1994) New substrates of papain, based on the conserved sequence of natural inhibitors of the cystatin family. Biochimie 76, 153-158.
    • (1994) Biochimie , vol.76 , pp. 153-158
    • Serveau, C.1    Juliano, L.2    Bernard, P.3    Moreau, T.4    Mayer, R.5    Gauthier, F.6
  • 28
    • 0028102744 scopus 로고
    • Clarification of substrate specificity of papain by crystal analyses of complexes with covalent-type inhibitors
    • Matsumoto, K., Murata, M., Sumiya, S., Kitamura, K. & Ishida, T. (1994) Clarification of substrate specificity of papain by crystal analyses of complexes with covalent-type inhibitors. Biochim. Biophys. Acta 1208, 268-276.
    • (1994) Biochim. Biophys. Acta , vol.1208 , pp. 268-276
    • Matsumoto, K.1    Murata, M.2    Sumiya, S.3    Kitamura, K.4    Ishida, T.5
  • 30
    • 0028674466 scopus 로고
    • Catalytic mechanism in papain family of cysteine peptidases
    • Storer, A.C. & Ménard, R. (1994) Catalytic mechanism in papain family of cysteine peptidases. Methods Enzymol. 244, 486-500.
    • (1994) Methods Enzymol. , vol.244 , pp. 486-500
    • Storer, A.C.1    Ménard, R.2
  • 31
    • 0028968184 scopus 로고
    • Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex
    • Jia, Z., Hasnain, S., Hirama, T., Lee, X., Mort, J. S., To, R. & Huber, C.P. (1995) Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. J. Biol. Chem. 270, 5527-5533.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5527-5533
    • Jia, Z.1    Hasnain, S.2    Hirama, T.3    Lee, X.4    Mort, J.S.5    To, R.6    Huber, C.P.7
  • 32
    • 0022474117 scopus 로고
    • Trypanosoma cruzi: Characterization and isolation of a 57/51,000 m.w. surface glycoprotein (GP57/51) expressed by epimastigotes and bloodstream trypomastigotes
    • Scharfstein, J., Schechter, M., Senna, M., Peralta, J.M., Mendonça-Previato, L. & Miles, M.A. (1986) Trypanosoma cruzi: characterization and isolation of a 57/51,000 m.w. surface glycoprotein (GP57/51) expressed by epimastigotes and bloodstream trypomastigotes. J. Immunol., 137, 1336-1341.
    • (1986) J. Immunol. , vol.137 , pp. 1336-1341
    • Scharfstein, J.1    Schechter, M.2    Senna, M.3    Peralta, J.M.4    Mendonça-Previato, L.5    Miles, M.A.6
  • 34
    • 0028171897 scopus 로고
    • Engineering the S2 subsite specificity of human cathepsin S to a cathepsin L- and cathepsin B-like specificity
    • Brömme, D., Bonneau, P.R., Lachance, P. & Storer, A.C. (1994) Engineering the S2 subsite specificity of human cathepsin S to a cathepsin L- and cathepsin B-like specificity. J. Biol. Chem. 269, 30238-30242.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30238-30242
    • Brömme, D.1    Bonneau, P.R.2    Lachance, P.3    Storer, A.C.4
  • 36
    • 0031030808 scopus 로고    scopus 로고
    • Crystal structure of human cathepsin K complexed with a potent inhibitor
    • McGrath, M.E., Klaus, J.L., Barnes, M.G. & Brömme, D. (1997) Crystal structure of human cathepsin K complexed with a potent inhibitor. Nature Structural Biology 4, 105-109.
    • (1997) Nature Structural Biology , vol.4 , pp. 105-109
    • McGrath, M.E.1    Klaus, J.L.2    Barnes, M.G.3    Brömme, D.4
  • 37
    • 0025292469 scopus 로고
    • Cysteine proteinase in Trypanosoma cruzi: Immunocytochemical localization and involvement in parasite-host cell interaction
    • Souto-Padron, T., Campetella, O.E., Cazzulo, J.J. & de Souza, W. 1990 Cysteine proteinase in Trypanosoma cruzi: immunocytochemical localization and involvement in parasite-host cell interaction. J. Cell Sci. 96, 485-490.
    • (1990) J. Cell Sci. , vol.96 , pp. 485-490
    • Souto-Padron, T.1    Campetella, O.E.2    Cazzulo, J.J.3    De Souza, W.4
  • 38
    • 0030055783 scopus 로고    scopus 로고
    • High resolution localization of cruzipain and Ssp4 in Trypanosoma cruzi by replica staining label fracture
    • Nascimento, A.E. & de Souza, W. (1996) High resolution localization of cruzipain and Ssp4 in Trypanosoma cruzi by replica staining label fracture. Biol. Cell 86, 53-58.
    • (1996) Biol. Cell , vol.86 , pp. 53-58
    • Nascimento, A.E.1    De Souza, W.2


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