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Volumn 259, Issue 2, 2006, Pages 215-220

The substrate specificity of cruzipain 2, a cysteine protease isoform from Trypanosoma cruzi

Author keywords

Chagas Disease; Cysteine protease; Isoform; Specificity; Trypanosome

Indexed keywords

CRUZIPAIN; CRUZIPAIN 2; CYSTEINE PROTEINASE; ISOENZYME; UNCLASSIFIED DRUG;

EID: 33744813530     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2006.00267.x     Document Type: Article
Times cited : (25)

References (31)
  • 1
    • 4644357065 scopus 로고    scopus 로고
    • A new cruzipain-dependent pathway of human cell invasion by Trypanosoma cruzi requiring trypomastigote membranes
    • Aparicio IM, Scharfstein J Lima APCA 2004 A new cruzipain-dependent pathway of human cell invasion by Trypanosoma cruzi requiring trypomastigote membranes. Infect Immun 72: 5892 5902.
    • (2004) Infect Immun , vol.72 , pp. 5892-5902
    • Aparicio, I.M.1    Scharfstein, J.2    Apca, L.3
  • 3
    • 0034662749 scopus 로고    scopus 로고
    • A target within the target
    • probing cruzain's P′1 site to define structural determinants for the Chagas' disease protease.
    • Brinen LS, Hansell E, Cheng J, Roush WR, McKerrow JH Fletterick RJ 2000 A target within the target: probing cruzain's P′1 site to define structural determinants for the Chagas' disease protease. Structure 8: 831 840.
    • (2000) Structure , vol.8 , pp. 831-840
    • Brinen, L.S.1    Hansell, E.2    Cheng, J.3    Roush, W.R.4    McKerrow, J.H.5    Fletterick, R.J.6
  • 4
    • 0026570815 scopus 로고
    • The major cysteine proteinase (cruzipain) from Trypanosoma cruzi is encoded by multiple polymorphic tandemly organized genes located on different chromosomes
    • Campetella O, Henriksson J, Aslund L, Frasch ACC, Pettterson U Cazzulo JJ 1992 The major cysteine proteinase (cruzipain) from Trypanosoma cruzi is encoded by multiple polymorphic tandemly organized genes located on different chromosomes. Mol Biochem Parasitol 50: 225 234.
    • (1992) Mol Biochem Parasitol , vol.50 , pp. 225-234
    • Campetella, O.1    Henriksson, J.2    Aslund, L.3    Frasch, A.C.C.4    Pettterson, U.5    Cazzulo, J.J.6
  • 7
    • 0030178647 scopus 로고    scopus 로고
    • Hydrolysis of synthetic peptides by cruzipain, the major cysteine proteinase from Trypanosoma cruzi, provides evidence for self-processing and the possibility of more specific substrates for the enzyme
    • Cazzulo JJ, Bravo M, Raimondi A, Engstrom U, Lindeberg G Hellman U 1996 Hydrolysis of synthetic peptides by cruzipain, the major cysteine proteinase from Trypanosoma cruzi, provides evidence for self-processing and the possibility of more specific substrates for the enzyme. Cell Mol Biol 42: 691 696.
    • (1996) Cell Mol Biol , vol.42 , pp. 691-696
    • Cazzulo, J.J.1    Bravo, M.2    Raimondi, A.3    Engstrom, U.4    Lindeberg, G.5    Hellman, U.6
  • 8
    • 0031049020 scopus 로고    scopus 로고
    • Cruzipain, the major cysteine proteinase from the protozoan parasite Trypanosoma cruzi
    • Cazzulo JJ, Stoka V Turk V 1997 Cruzipain, the major cysteine proteinase from the protozoan parasite Trypanosoma cruzi. Biol Chem 378: 1 10.
    • (1997) Biol Chem , vol.378 , pp. 1-10
    • Cazzulo, J.J.1    Stoka, V.2    Turk, V.3
  • 9
    • 0026781519 scopus 로고
    • The sequence, organization, and expression of the major cysteine protease (Cruzain) from Trypanosoma cruzi
    • Eakin RE, Mills RR, Harth G, McKerrow JH Craik CS 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, R.E.1    Mills, R.R.2    Harth, G.3    McKerrow, J.H.4    Craik, C.S.5
  • 10
    • 0032541311 scopus 로고    scopus 로고
    • Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection
    • Engel JC, Doyle PS, Hsieh I McKerrow JH 1998 Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection. J Exp Med 188: 725 734.
    • (1998) J Exp Med , vol.188 , pp. 725-734
    • Engel, J.C.1    Doyle, P.S.2    Hsieh, I.3    McKerrow, J.H.4
  • 11
    • 0030841381 scopus 로고    scopus 로고
    • Structural determinants of specificity in the cysteine protease cruzain
    • Gillmor SR, Craik CS Fletterick RJ 1997 Structural determinants of specificity in the cysteine protease cruzain. Prot Sci 6: 1603 1611.
    • (1997) Prot Sci , vol.6 , pp. 1603-1611
    • Gillmor, S.R.1    Craik, C.S.2    Fletterick, R.J.3
  • 12
    • 0027398184 scopus 로고
    • Peptide-fluoromethyl ketones arrest intracellular replication and intercellular transmission of T. cruzi
    • Harth G, Andrews N, Mills RR, Engel JC, Smith R McKerrow JH 1993 Peptide-fluoromethyl ketones arrest intracellular replication and intercellular transmission of T. cruzi. Mol Biochem Parasitol 58: 17 24.
    • (1993) Mol Biochem Parasitol , vol.58 , pp. 17-24
    • Harth, G.1    Andrews, N.2    Mills, R.R.3    Engel, J.C.4    Smith, R.5    McKerrow, J.H.6
  • 13
    • 0035660408 scopus 로고    scopus 로고
    • Comparison of the specificity, stability and individual rate constants with respective activation parameters for the peptidase activity of cruzipain and its recombinant form, cruzain, from Trypanosoma cruzi
    • Judice WA, Cezari MHS, Lima APCA, Scharfstein J, Chagas JR, Tersariol ILS, Juliano MA Juliano L 2001 Comparison of the specificity, stability and individual rate constants with respective activation parameters for the peptidase activity of cruzipain and its recombinant form, cruzain, from Trypanosoma cruzi. Eur J Biochem 268: 6578 6586.
    • (2001) Eur J Biochem , vol.268 , pp. 6578-6586
    • Judice, W.A.1    Cezari, M.H.S.2    Apca, L.3    Scharfstein, J.4    Chagas, J.R.5    Tersariol, I.L.S.6    Juliano, M.A.7    Juliano, L.8
  • 14
    • 0026620531 scopus 로고
    • Temperature dependent substrate inhibition of the cysteine proteinase (GP57/51) from Trypanosoma cruzi
    • Lima APCA, Scharfstein J, Storer AC 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
    • Apca, L.1    Scharfstein, J.2    Storer, A.C.3    Ménard, R.4
  • 18
    • 0026606269 scopus 로고
    • Inhibitors of the major cysteinyl proteinase (GP57/51) impair host cell invasion and arrest the intracellular development of Trypanosoma cruziin vitro
    • Meirelles MNL, Juliano L, Carmona E, Silva SG, Costa EM, Murta AC Scharfstein J 1992 Inhibitors of the major cysteinyl proteinase (GP57/51) impair host cell invasion and arrest the intracellular development of Trypanosoma cruziin 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.6    Scharfstein, J.7
  • 19
    • 0032037456 scopus 로고    scopus 로고
    • Inhibition of cruzipain visualized in a fluorescence quenched solid-phase inhibitor library assay. d-amino acid inhibitors for cruzipain, cathepsin B and cathepsin L
    • Meldal M, Svendsen IB, Juliano L, Juliano MA, Nery ED Scharfstein J 1998 Inhibition of cruzipain visualized in a fluorescence quenched solid-phase inhibitor library assay. d-amino acid inhibitors for cruzipain, cathepsin B and cathepsin L. J Peptide Sci 4: 83 91.
    • (1998) J Peptide Sci , vol.4 , pp. 83-91
    • Meldal, M.1    Svendsen, I.B.2    Juliano, L.3    Juliano, M.A.4    Nery, E.D.5    Scharfstein, J.6
  • 21
    • 0037810410 scopus 로고    scopus 로고
    • Family C1 cysteine proteases
    • biological diversity or redundancy?
    • Nagler DK Ménard R 2003 Family C1 cysteine proteases: biological diversity or redundancy? Biol Chem 384: 837 843.
    • (2003) Biol Chem , vol.384 , pp. 837-843
    • Nagler, D.K.1    Ménard, R.2
  • 22
    • 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
    • Nery ED, Juliano MA, 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
    • Nery, E.D.1    Juliano, M.A.2    Meldal, M.3    Svendsen, I.4    Scharfstein, J.5    Walmsley, A.6    Juliano, L.7
  • 23
    • 0028919880 scopus 로고
    • The presence of complex-type oligosaccharides at the C-terminal domain glycosylation site of some molecules of cruzipain
    • Parodi AJ, Labriola C Cazzulo JJ 1995 The presence of complex-type oligosaccharides at the C-terminal domain glycosylation site of some molecules of cruzipain. Mol Biochem Parasitol 69: 247 255.
    • (1995) Mol Biochem Parasitol , vol.69 , pp. 247-255
    • Parodi, A.J.1    Labriola, C.2    Cazzulo, J.J.3
  • 24
    • 0036178381 scopus 로고    scopus 로고
    • Cysteine proteases of parasitic organisms
    • Sajid M McKerrow JH 2002 Cysteine proteases of parasitic organisms. Mol Biochem Parasitol 120: 1 21.
    • (2002) Mol Biochem Parasitol , vol.120 , pp. 1-21
    • Sajid, M.1    McKerrow, J.H.2
  • 25
    • 4644328413 scopus 로고    scopus 로고
    • Activation of bradykinin-receptors by Trypanosoma cruzi
    • a role for cruzipain in microvascular pathology. Kelly J.M., ed), pp. Landes Bioscience, Austin, TX.
    • Scharfstein J 2003 Activation of bradykinin-receptors by Trypanosoma cruzi: a role for cruzipain in microvascular pathology. Molecular Pathogenesis of Chagas' Disease Kelly J.M., ed), pp. 111 137. Landes Bioscience, Austin, TX.
    • (2003) Molecular Pathogenesis of Chagas' Disease , pp. 111-137
    • Scharfstein, J.1
  • 27
    • 0030034874 scopus 로고    scopus 로고
    • Investigation of the substrate specificity of cruzipain, the major cysteine proteinase of T. cruzi, through the use of cystatin-derived substrates and inhibitors
    • Serveau C, Lalmanach G, Juliano MA, Scharfstein J, Juliano L Gauthier F 1996 Investigation of the substrate specificity of cruzipain, the major cysteine proteinase of T. cruzi, through the use of cystatin-derived substrates and inhibitors. Biochem J 313: 951 1956.
    • (1996) Biochem J , vol.313 , pp. 951-1956
    • Serveau, C.1    Lalmanach, G.2    Juliano, M.A.3    Scharfstein, J.4    Juliano, L.5    Gauthier, F.6
  • 28
    • 0033555294 scopus 로고    scopus 로고
    • 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
    • Serveau C, Lalmanach G, Hirata I, Scharfstein J, Juliano MA Gauthier F 1999 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. Eur J Biochem 259: 275 280.
    • (1999) Eur J Biochem , vol.259 , pp. 275-280
    • Serveau, C.1    Lalmanach, G.2    Hirata, I.3    Scharfstein, J.4    Juliano, M.A.5    Gauthier, F.6
  • 29
    • 0029978872 scopus 로고    scopus 로고
    • Stage-regulated expression of cruzipain, the major cysteine protease of Trypanosoma cruzi is independent of the level of RNA
    • Tomas A Kelly JM 1996 Stage-regulated expression of cruzipain, the major cysteine protease of Trypanosoma cruzi is independent of the level of RNA. Mol Biochem Parasitol 76: 91 103.
    • (1996) Mol Biochem Parasitol , vol.76 , pp. 91-103
    • Tomas, A.1    Kelly, J.M.2
  • 30
    • 0345310073 scopus 로고    scopus 로고
    • Revised definition of binding sites of papain-like cysteine proteases
    • Turk D, Guncar G, Podohnick M Turk B 1998 Revised definition of binding sites of papain-like cysteine proteases. Biol Chem 379: 137 147.
    • (1998) Biol Chem , vol.379 , pp. 137-147
    • Turk, D.1    Guncar, G.2    Podohnick, M.3    Turk, B.4
  • 31
    • 0033610817 scopus 로고    scopus 로고
    • Human cathepsin F, molecular cloning, functional expression, tissue localization, and enzymatic characterization
    • Wang B, Shi GP, Yao PM, Li Z, Chapman HA Bromme D 1998 Human cathepsin F, molecular cloning, functional expression, tissue localization, and enzymatic characterization. J Biol Chem 273: 32000 32008.
    • (1998) J Biol Chem , vol.273 , pp. 32000-32008
    • Wang, B.1    Shi, G.P.2    Yao, P.M.3    Li, Z.4    Chapman, H.A.5    Bromme, D.6


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