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Volumn 141, Issue 1, 2005, Pages 71-79

Cysteine-protease activity elicited by Ca2+ stimulus in Plasmodium

Author keywords

Calcium; Calpain; Cysteine protease; Malaria; Melatonin

Indexed keywords

CALCIUM CHELATING AGENT; CALCIUM ION; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; ETHYLENE GLYCOL 1,2 BIS(2 AMINOPHENYL) ETHER N,N,N',N' TETRAACETIC ACID; FLUORESCEIN ISOTHIOCYANATE; IONOMYCIN; MELATONIN; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; NIGERICIN; PROTEIN INHIBITOR; THAPSIGARGIN;

EID: 16244399550     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2005.01.015     Document Type: Article
Times cited : (39)

References (53)
  • 1
    • 0015404943 scopus 로고
    • The asexual and sexual circadian rhythms of Plasmodium vinckei chabaudi, of P. berghei and of P. gallinaceum
    • F. Hawking, K. Gammage, and M.J. Worms The asexual and sexual circadian rhythms of Plasmodium vinckei chabaudi, of P. berghei and of P. gallinaceum Parasitology 65 1972 189 201
    • (1972) Parasitology , vol.65 , pp. 189-201
    • Hawking, F.1    Gammage, K.2    Worms, M.J.3
  • 2
    • 0034782804 scopus 로고    scopus 로고
    • Tertian and quartan fevers: Temporal regulation in malarial infection
    • C.R. Garcia, R.P. Markus, and L. Madeira Tertian and quartan fevers: temporal regulation in malarial infection J Biol Rhythms 16 2001 436 443
    • (2001) J Biol Rhythms , vol.16 , pp. 436-443
    • Garcia, C.R.1    Markus, R.P.2    Madeira, L.3
  • 3
    • 0025166184 scopus 로고
    • Effects of melatonin on vertebrate circadian systems
    • V.M. Cassone Effects of melatonin on vertebrate circadian systems Trends Neurosci 13 1990 457 464
    • (1990) Trends Neurosci , vol.13 , pp. 457-464
    • Cassone, V.M.1
  • 4
    • 0037379997 scopus 로고    scopus 로고
    • Melatonin: From seasonal to circadian signal
    • P. Pevet Melatonin: from seasonal to circadian signal J Neuroendocrinol 15 2003 422 426
    • (2003) J Neuroendocrinol , vol.15 , pp. 422-426
    • Pevet, P.1
  • 5
    • 0033780574 scopus 로고    scopus 로고
    • Calcium dependent modulation by melatonin of the circadian rhythm in malarial parasites
    • C. Hotta, M.L. Gazarini, and F.H. Beraldo Calcium dependent modulation by melatonin of the circadian rhythm in malarial parasites Nat Cell Biol 2 2000 466 468
    • (2000) Nat Cell Biol , vol.2 , pp. 466-468
    • Hotta, C.1    Gazarini, M.L.2    Beraldo, F.H.3
  • 6
    • 0242490894 scopus 로고    scopus 로고
    • Melatonin and N-acetyl-serotonin cross the red blood cell membrane and evoke calcium mobilization in malarial parasites
    • C.T. Hotta, R.P. Markus, and C.R. Garcia Melatonin and N-acetyl-serotonin cross the red blood cell membrane and evoke calcium mobilization in malarial parasites Braz J Med Biol Res 36 2003 1583 1587
    • (2003) Braz J Med Biol Res , vol.36 , pp. 1583-1587
    • Hotta, C.T.1    Markus, R.P.2    Garcia, C.R.3
  • 7
    • 0028283948 scopus 로고
    • Molecular and cellular physiology of intracellular calcium stores
    • T. Pozzan, R. Rizzuto, P. Volpe, and J. Meldolesi Molecular and cellular physiology of intracellular calcium stores Physiol Rev 74 1994 595 636
    • (1994) Physiol Rev , vol.74 , pp. 595-636
    • Pozzan, T.1    Rizzuto, R.2    Volpe, P.3    Meldolesi, J.4
  • 10
    • 0029069735 scopus 로고
    • Cloning of a new cation ATPase from Plasmodium falciparum: Conservation of critical amino acids involved in calcium binding in mammalian organellar Ca(2+)-ATPases
    • F. Trottein, J. Thompson, and A.F. Cowman Cloning of a new cation ATPase from Plasmodium falciparum: conservation of critical amino acids involved in calcium binding in mammalian organellar Ca(2+)-ATPases Gene 158 1995 133 137
    • (1995) Gene , vol.158 , pp. 133-137
    • Trottein, F.1    Thompson, J.2    Cowman, A.F.3
  • 11
    • 0033485874 scopus 로고    scopus 로고
    • Calcium homeostasis and signaling in the blood-stage malaria parasite
    • C.R. Garcia Calcium homeostasis and signaling in the blood-stage malaria parasite Parasitol Today 15 1999 488 491
    • (1999) Parasitol Today , vol.15 , pp. 488-491
    • Garcia, C.R.1
  • 12
    • 0025148986 scopus 로고
    • 2+-ATPase of rabbit skeletal muscle sarcoplasmic reticulum
    • 2+-ATPase of rabbit skeletal muscle sarcoplasmic reticulum J Cell Sci 97 1990 487 495
    • (1990) J Cell Sci , vol.97 , pp. 487-495
    • Murakami, K.1    Tanabe, K.2    Takada, S.3
  • 14
    • 0031283090 scopus 로고    scopus 로고
    • 2+ transport activity associated with a non-mitochondrial calcium pool in the rodent malaria parasite P. chabaudi
    • 2+ transport activity associated with a non-mitochondrial calcium pool in the rodent malaria parasite P. chabaudi Biochem Mol Biol Int 42 1997 919 925
    • (1997) Biochem Mol Biol Int , vol.42 , pp. 919-925
    • Passos, A.P.1    Garcia, C.R.2
  • 15
    • 0032492553 scopus 로고    scopus 로고
    • 2+ release from chloroquine-sensitive and -insensitive intracellular stores in the intraerythrocytic stage of the malaria parasite P. chabaudi
    • 2+ release from chloroquine-sensitive and -insensitive intracellular stores in the intraerythrocytic stage of the malaria parasite P. chabaudi Biochem Biophys Res Commun 245 1998 155 160
    • (1998) Biochem Biophys Res Commun , vol.245 , pp. 155-160
    • Passos, A.P.1    Garcia, C.R.2
  • 17
    • 0034788662 scopus 로고    scopus 로고
    • Calcium regulation in the intraerythrocytic malaria parasite Plasmodium falciparum
    • L.M. Alleva, and K. Kirk Calcium regulation in the intraerythrocytic malaria parasite Plasmodium falciparum Mol Biochem Parasitol 117 2001 121 128
    • (2001) Mol Biochem Parasitol , vol.117 , pp. 121-128
    • Alleva, L.M.1    Kirk, K.2
  • 18
    • 0042860063 scopus 로고    scopus 로고
    • Artemisinins target the SERCA of Plasmodium falciparum
    • U. Eckstein-Ludwig, R.J. Webb, and I.D. Van Goethem Artemisinins target the SERCA of Plasmodium falciparum Nature 424 2003 957 961
    • (2003) Nature , vol.424 , pp. 957-961
    • Eckstein-Ludwig, U.1    Webb, R.J.2    Van Goethem, I.D.3
  • 22
    • 0344805645 scopus 로고    scopus 로고
    • Calcium signaling in a low calcium environment: How the intracellular malaria parasite solves the problem
    • M.L. Gazarini, A.P. Thomas, T. Pozzan, and C.R.S. Garcia Calcium signaling in a low calcium environment: how the intracellular malaria parasite solves the problem J Cell Biol 161 2003 103 110
    • (2003) J Cell Biol , vol.161 , pp. 103-110
    • Gazarini, M.L.1    Thomas, A.P.2    Pozzan, T.3    Garcia, C.R.S.4
  • 23
    • 0033042010 scopus 로고    scopus 로고
    • Proteases of protozoan parasites
    • P.J. Rosenthal Proteases of protozoan parasites Adv Parasitol 43 1999 105 159
    • (1999) Adv Parasitol , vol.43 , pp. 105-159
    • Rosenthal, P.J.1
  • 24
    • 0034232515 scopus 로고    scopus 로고
    • Proteases involved in erythrocyte invasion by the malaria parasite: Function and potential as chemotherapeutic targets
    • M.J. Blackman Proteases involved in erythrocyte invasion by the malaria parasite: function and potential as chemotherapeutic targets Curr Drug Targets 1 2000 59 83
    • (2000) Curr Drug Targets , vol.1 , pp. 59-83
    • Blackman, M.J.1
  • 25
    • 0035997361 scopus 로고    scopus 로고
    • Biological roles of proteases in parasitic protozoa
    • M. Klemba, and D.E. Goldberg Biological roles of proteases in parasitic protozoa Annu Rev Biochem 71 2002 275 305
    • (2002) Annu Rev Biochem , vol.71 , pp. 275-305
    • Klemba, M.1    Goldberg, D.E.2
  • 26
    • 0035986688 scopus 로고    scopus 로고
    • Cysteine proteases of malaria parasites: Targets for chemotherapy
    • P.J. Rosenthal, P.S. Sijwali, A. Singh, and B.R. Shenai Cysteine proteases of malaria parasites: targets for chemotherapy Curr Pharm Des 18 2002 1659 1672
    • (2002) Curr Pharm des , vol.18 , pp. 1659-1672
    • Rosenthal, P.J.1    Sijwali, P.S.2    Singh, A.3    Shenai, B.R.4
  • 30
    • 2242432614 scopus 로고    scopus 로고
    • A role for the protease falcipain 1 in host cell invasion by the human malaria parasite
    • D.C. Greenbaum, A. Baruch, and M. Grainger A role for the protease falcipain 1 in host cell invasion by the human malaria parasite Science 298 2002 2002 2006
    • (2002) Science , vol.298 , pp. 2002-2006
    • Greenbaum, D.C.1    Baruch, A.2    Grainger, M.3
  • 31
    • 1842533231 scopus 로고    scopus 로고
    • Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum
    • P.S. Sijwali, and P.J. Rosenthal Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum Proc Natl Acad Sci USA 101 2004 4384 4389
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4384-4389
    • Sijwali, P.S.1    Rosenthal, P.J.2
  • 32
    • 0035094985 scopus 로고    scopus 로고
    • Regulation of red cell membrane protein interactions: Implications for red cell function
    • Y. Takakuwa Regulation of red cell membrane protein interactions: implications for red cell function Curr Opin Hematol 8 2001 80 84
    • (2001) Curr Opin Hematol , vol.8 , pp. 80-84
    • Takakuwa, Y.1
  • 33
    • 0141509925 scopus 로고    scopus 로고
    • Selective inhibition of a two-step egress of malaria parasites from the host erythrocyte
    • M.E. Wickham, J.G. Culvenor, and A.F. Cowman Selective inhibition of a two-step egress of malaria parasites from the host erythrocyte J Biol Chem 278 2003 37658 37663
    • (2003) J Biol Chem , vol.278 , pp. 37658-37663
    • Wickham, M.E.1    Culvenor, J.G.2    Cowman, A.F.3
  • 34
    • 0035069258 scopus 로고    scopus 로고
    • Membrane transport in the malaria-infected erythrocyte
    • K. Kirk Membrane transport in the malaria-infected erythrocyte Physiol Rev 81 2001 495 537
    • (2001) Physiol Rev , vol.81 , pp. 495-537
    • Kirk, K.1
  • 35
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • W. Trager, and J.B. Jensen Human malaria parasites in continuous culture Science 193 1976 673 675
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 36
    • 0018704491 scopus 로고
    • Synchronization of Plasmodium falciparum erythrocytic stages in culture
    • C. Lambros, and J.P. Vanderberg Synchronization of Plasmodium falciparum erythrocytic stages in culture J Parasitol 65 1979 41 45
    • (1979) J Parasitol , vol.65 , pp. 41-45
    • Lambros, C.1    Vanderberg, J.P.2
  • 37
    • 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
    • I.Y. Hirata, M.H.S. Cezari, and C. Nakaie Internally quenched fluorogenic protease substrates: solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs Lett Peptide Sci 1 1994 299 308
    • (1994) Lett Peptide Sci , vol.1 , pp. 299-308
    • Hirata, I.Y.1    Cezari, M.H.S.2    Nakaie, C.3
  • 38
    • 0034054576 scopus 로고    scopus 로고
    • Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs
    • M. Bogyo, S. Verhelst, V. Bellingard-Dubouchaud, S. Toba, and D. Greenbaum Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs Chem Biol 7 2000 27 38
    • (2000) Chem Biol , vol.7 , pp. 27-38
    • Bogyo, M.1    Verhelst, S.2    Bellingard-Dubouchaud, V.3    Toba, S.4    Greenbaum, D.5
  • 39
    • 0034353198 scopus 로고    scopus 로고
    • Alpha1-antichymotrypsin and kallistatin hydrolysis by human cathepsin D
    • D.C. Pimenta, V.C. Chen, J. Chao, M.A. Juliano, and L. Juliano Alpha1-antichymotrypsin and kallistatin hydrolysis by human cathepsin D J Protein Chem 19 2000 411 418
    • (2000) J Protein Chem , vol.19 , pp. 411-418
    • Pimenta, D.C.1    Chen, V.C.2    Chao, J.3    Juliano, M.A.4    Juliano, L.5
  • 40
    • 0035846971 scopus 로고    scopus 로고
    • Substrate specificity of human cathepsin D using internally quenched fluorescent peptides derived from reactive site loop of kallistatin
    • D.C. Pimenta, A. Oliveira, M.A. Juliano, and L. Juliano Substrate specificity of human cathepsin D using internally quenched fluorescent peptides derived from reactive site loop of kallistatin Biochim Biophys Acta 12 2001 113 122
    • (2001) Biochim Biophys Acta , vol.12 , pp. 113-122
    • Pimenta, D.C.1    Oliveira, A.2    Juliano, M.A.3    Juliano, L.4
  • 41
    • 0034683233 scopus 로고    scopus 로고
    • The substrate specificity of a recombinant cysteine protease from Leishmania mexicana: Application of a combinatorial peptide library approach
    • P.M. St Hilaire, L.C. Alves, and S.J. Sanderson The substrate specificity of a recombinant cysteine protease from Leishmania mexicana: application of a combinatorial peptide library approach Chembiochemistry 18 2000 115 122
    • (2000) Chembiochemistry , vol.18 , pp. 115-122
    • St Hilaire, P.M.1    Alves, L.C.2    Sanderson, S.J.3
  • 42
    • 0014211618 scopus 로고
    • On the size of the active site in proteases
    • I. Schechter, and A. Berger On the size of the active site in proteases Biochem Biophys Res Commun 27 1967 152 162
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 152-162
    • Schechter, I.1    Berger, A.2
  • 43
    • 7444223383 scopus 로고    scopus 로고
    • Of malaria, metabolism and membrane transport
    • K. Becker, and K. Kirk Of malaria, metabolism and membrane transport Trends Parasitol 20 2004 590 596
    • (2004) Trends Parasitol , vol.20 , pp. 590-596
    • Becker, K.1    Kirk, K.2
  • 44
    • 1642442461 scopus 로고    scopus 로고
    • Channels and transporters as drug targets in the Plasmodium-infected erythrocyte
    • K. Kirk Channels and transporters as drug targets in the Plasmodium-infected erythrocyte Acta Trop 89 2004 285 298
    • (2004) Acta Trop , vol.89 , pp. 285-298
    • Kirk, K.1
  • 46
    • 0024198184 scopus 로고
    • Activation of a Plasmodium falciparum protease correlated with merozoite maturation and erythrocyte invasion
    • C. Braun-Breton, and L. Pereira da Silva Activation of a Plasmodium falciparum protease correlated with merozoite maturation and erythrocyte invasion Biol Cell 64 1988 223 231
    • (1988) Biol Cell , vol.64 , pp. 223-231
    • Braun-Breton, C.1    Pereira Da Silva, L.2
  • 47
    • 0347122968 scopus 로고    scopus 로고
    • Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum
    • M. Klemba, W. Beatty, I. Gluzman, and D.E. Goldberg Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum J Cell Biol 164 2004 47 56
    • (2004) J Cell Biol , vol.164 , pp. 47-56
    • Klemba, M.1    Beatty, W.2    Gluzman, I.3    Goldberg, D.E.4
  • 48
    • 0242669367 scopus 로고    scopus 로고
    • Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite
    • Y. Wu, X. Wang, X. Liu, and Y. Wang Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite Genome Res 13 2003 601 616
    • (2003) Genome Res , vol.13 , pp. 601-616
    • Wu, Y.1    Wang, X.2    Liu, X.3    Wang, Y.4
  • 49
    • 85030794993 scopus 로고    scopus 로고
    • Characterization of Plasmodium falciparum calpain gene
    • [abstract #260C].
    • Russo I, Goldberg DE. Characterization of Plasmodium falciparum calpain gene. In: Molecular Parasitology Meeting XV; 2004 [abstract #260C].
    • (2004) Molecular Parasitology Meeting XV
    • Russo, I.1    Goldberg, D.E.2
  • 50
    • 16244396049 scopus 로고    scopus 로고
    • PEST sequences in the malaria parasite Plasmodium falciparum: A genomic study
    • D. Mitchell, and A. Bell PEST sequences in the malaria parasite Plasmodium falciparum: a genomic study Malaria J 23 2004 2 16
    • (2004) Malaria J , vol.23 , pp. 2-16
    • Mitchell, D.1    Bell, A.2
  • 51
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • H. Sorimachi, S. Ishiura, and K. Suzuki Structure and physiological function of calpains Biochem J 328 1997 721 732
    • (1997) Biochem J , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3


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