메뉴 건너뛰기




Volumn 1, Issue 1, 2008, Pages

Profiling of proteolytic enzymes in the gut of the tick Ixodes ricinus reveals an evolutionarily conserved network of aspartic and cysteine peptidases

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN B; CATHEPSIN D;

EID: 57549115852     PISSN: None     EISSN: 17563305     Source Type: Journal    
DOI: 10.1186/1756-3305-1-7     Document Type: Article
Times cited : (78)

References (58)
  • 1
    • 0021781406 scopus 로고
    • Argasid and nuttalliellid ticks as parasites and vectors
    • 3904345
    • Argasid and nuttalliellid ticks as parasites and vectors. H Hoogstraal, Adv Parasitol 1985 24 135 138 3904345
    • (1985) Adv Parasitol , vol.24 , pp. 135-138
    • Hoogstraal, H.1
  • 2
    • 0033374691 scopus 로고    scopus 로고
    • Pathogen-tick-host interactions: Borrelia bugdorferi and TBE virus
    • 10652716
    • Pathogen-tick-host interactions: Borrelia bugdorferi and TBE virus. PA Nutall, Zentralbl Bakteriol 1999 289 492 505 10652716
    • (1999) Zentralbl Bakteriol , vol.289 , pp. 492-505
    • Nutall, P.A.1
  • 3
    • 0010014128 scopus 로고
    • Blood digestion in Ornithodoros moubata Murray sensu stricto Walton (Ixodoidea: Argasidae) females. I. Biochemical changes in the midgut lumen and ultrastructure of the midgut cells, related to intracellular digestion
    • Blood digestion in Ornithodoros moubata Murray sensu stricto Walton (Ixodoidea: Argasidae) females. I. Biochemical changes in the midgut lumen and ultrastructure of the midgut cells, related to intracellular digestion. O Grandjean, Acarologia 1984 25 147 165
    • (1984) Acarologia , vol.25 , pp. 147-165
    • Grandjean, O.1
  • 4
    • 0004151015 scopus 로고
    • New York: Oxford University Press
    • Biology of Ticks. DE Sonenshine, New York: Oxford University Press 1991 1
    • (1991) Biology of Ticks , vol.1
    • Sonenshine, D.E.1
  • 5
    • 0017931684 scopus 로고
    • Boophilus microplus: Characterization of larval proteases
    • 10.1016/0014-4894(78)90074-7 23954
    • Boophilus microplus: characterization of larval proteases. CI Reich J Zorzopulos, Exp Parasitol 1978 44 1 6 10.1016/0014-4894(78)90074-7 23954
    • (1978) Exp Parasitol , vol.44 , pp. 1-6
    • Reich, C.I.1    Zorzopulos, J.2
  • 8
    • 25144490692 scopus 로고    scopus 로고
    • Tracing heme in a living cell: Hemoglobin degradation and heme traffic in digest cells of the cattle tick Boophilus microplus
    • 10.1242/jeb.01749 16081607
    • Tracing heme in a living cell: hemoglobin degradation and heme traffic in digest cells of the cattle tick Boophilus microplus. FA Lara U Lins GH Bechara PL Oliveira, J Exp Biol 2005 208 3093 3101 10.1242/jeb.01749 16081607
    • (2005) J Exp Biol , vol.208 , pp. 3093-3101
    • Lara, F.A.1    Lins, U.2    Bechara, G.H.3    Oliveira, P.L.4
  • 9
    • 0037506077 scopus 로고    scopus 로고
    • A new intracellular pathway of haem detoxification in the midgut of the cattle tick Boophilus microplus: Aggregation inside a specialized organelle, the hemosome
    • 10.1242/jeb.00334 12682102
    • A new intracellular pathway of haem detoxification in the midgut of the cattle tick Boophilus microplus: aggregation inside a specialized organelle, the hemosome. FA Lara U Lins G Paiva-Silva IC Almeida CM Braga FC Miguens PL Oliveira M Dansa-Petretski, J Exp Biol 2003 206 1707 1715 10.1242/jeb.00334 12682102
    • (2003) J Exp Biol , vol.206 , pp. 1707-1715
    • Lara, F.A.1    Lins, U.2    Paiva-Silva, G.3    Almeida, I.C.4    Braga, C.M.5    Miguens, F.C.6    Oliveira, P.L.7    Dansa-Petretski, M.8
  • 11
    • 0033128927 scopus 로고    scopus 로고
    • Molecular cloning of two Haemaphysalis longicornis cathepsin L-like cysteine proteinase genes
    • 10.1292/jvms.61.497 10379941
    • Molecular cloning of two Haemaphysalis longicornis cathepsin L-like cysteine proteinase genes. A Mulenga C Sugimoto G Ingram K Ohashi M Onuma, J Vet Med Sci 1999 61 497 503 10.1292/jvms.61.497 10379941
    • (1999) J Vet Med Sci , vol.61 , pp. 497-503
    • Mulenga, A.1    Sugimoto, C.2    Ingram, G.3    Ohashi, K.4    Onuma, M.5
  • 12
    • 29144503154 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of an aspartic protease from the hard tick Haemaphysalis longicornis
    • 10.1016/j.ibmb.2005.10.003 16360947
    • Molecular cloning and functional characterization of an aspartic protease from the hard tick Haemaphysalis longicornis. D Boldbaatar C Sikalizyo Sikasunge B Battsetseg X Xuan K Fujisaki, Insect Biochem Mol Biol 2006 36 25 36 10.1016/j.ibmb.2005.10.003 16360947
    • (2006) Insect Biochem Mol Biol , vol.36 , pp. 25-36
    • Boldbaatar, D.1    Sikalizyo Sikasunge, C.2    Battsetseg, B.3    Xuan, X.4    Fujisaki, K.5
  • 14
    • 34547532754 scopus 로고    scopus 로고
    • Characterization of asparaginyl endopeptidase, legumain induced by blood feeding in the ixodid tick Haemaphysalis longicornis
    • 10.1016/j.ibmb.2007.04.010 17681230
    • Characterization of asparaginyl endopeptidase, legumain induced by blood feeding in the ixodid tick Haemaphysalis longicornis. MA Alim N Tsuji T Miyoshi MK Islam X Huang M Motobu K Fujisaki, Insect Biochem Mol Biol 2007 37 911 922 10.1016/j.ibmb.2007.04.010 17681230
    • (2007) Insect Biochem Mol Biol , vol.37 , pp. 911-922
    • Alim, M.A.1    Tsuji, N.2    Miyoshi, T.3    Islam, M.K.4    Huang, X.5    Motobu, M.6    Fujisaki, K.7
  • 15
    • 1942519435 scopus 로고    scopus 로고
    • Blood 'n' guts: An update on schistosome digestive peptidases
    • 10.1016/j.pt.2004.03.004 15105025
    • Blood 'n' guts: an update on schistosome digestive peptidases. CR Caffrey JH McKerrow JP Salter M Sajid, Trends Parasitol 2004 20 241 248 10.1016/j.pt.2004.03.004 15105025
    • (2004) Trends Parasitol , vol.20 , pp. 241-248
    • Caffrey, C.R.1    McKerrow, J.H.2    Salter, J.P.3    Sajid, M.4
  • 18
    • 0029880287 scopus 로고    scopus 로고
    • Characterization of the cathepsin-like cysteine proteinases of Schistosoma mansoni
    • 8606097
    • Characterization of the cathepsin-like cysteine proteinases of Schistosoma mansoni. JP Dalton KA Clough MK Jones PJ Brindley, Infect Immun 1996 64 1328 1334 8606097
    • (1996) Infect Immun , vol.64 , pp. 1328-1334
    • Dalton, J.P.1    Clough, K.A.2    Jones, M.K.3    Brindley, P.J.4
  • 20
  • 22
    • 0036628339 scopus 로고    scopus 로고
    • A novel cathepsin B active site motif is shared by helminth bloodfeeders
    • 10.1016/S0014-4894(02)00105-4 12427461
    • A novel cathepsin B active site motif is shared by helminth bloodfeeders. S Baig RT Damian DS Peterson, Exp Parasitol 2002 101 83 89 10.1016/S0014- 4894(02)00105-4 12427461
    • (2002) Exp Parasitol , vol.101 , pp. 83-89
    • Baig, S.1    Damian, R.T.2    Peterson, D.S.3
  • 23
    • 0000759663 scopus 로고
    • Blood digestion in ticks
    • Oxford: Pergamon Press Obenchain F, Galun R
    • Blood digestion in ticks. S Akov, Physiology of Ticks Oxford: Pergamon Press, Obenchain F, Galun R, 1982 197 211
    • (1982) Physiology of Ticks , pp. 197-211
    • Akov, S.1
  • 24
    • 0029966482 scopus 로고    scopus 로고
    • Boophilus microplus: Multiple proteolytic activities in the midgut
    • 10.1006/expr.1996.0004 8617328
    • Boophilus microplus: multiple proteolytic activities in the midgut. J Mendiola M Alonso MC Marquetti C Finlay, Exp Parasitol 1996 82 27 33 10.1006/expr.1996.0004 8617328
    • (1996) Exp Parasitol , vol.82 , pp. 27-33
    • Mendiola, J.1    Alonso, M.2    Marquetti, M.C.3    Finlay, C.4
  • 28
    • 0036462513 scopus 로고    scopus 로고
    • S2' substrate specificity and the role of His110 and His111 in the exopeptidase activity of human cathepsin B
    • 11802791 10.1042/0264-6021:3610613
    • S2' substrate specificity and the role of His110 and His111 in the exopeptidase activity of human cathepsin B. JC Krupa S Hasnain DK Nagler R Menard JS Mort, Biochem J 2002 361 613 619 11802791 10.1042/0264-6021:3610613
    • (2002) Biochem J , vol.361 , pp. 613-619
    • Krupa, J.C.1    Hasnain, S.2    Nagler, D.K.3    Menard, R.4    Mort, J.S.5
  • 29
    • 0033587689 scopus 로고    scopus 로고
    • Dipeptidyl peptidase i is required for the processing and activation of granzymes A and B in vivo
    • 10411926 10.1073/pnas.96.15.8627
    • Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. CTN Pham TJ Ley, Proc Nat Acad Sci 1999 96 8627 8632 10411926 10.1073/pnas.96.15.8627
    • (1999) Proc Nat Acad Sci , vol.96 , pp. 8627-8632
    • Pham, C.T.N.1    Ley, T.J.2
  • 30
    • 33846839167 scopus 로고    scopus 로고
    • Molecular and reverse genetic characterization of serine proteinase-induced hemolysis in the midgut of the ixodid tick Haemaphysalis longicornis
    • 10.1016/j.jinsphys.2006.12.001 17275020
    • Molecular and reverse genetic characterization of serine proteinase-induced hemolysis in the midgut of the ixodid tick Haemaphysalis longicornis. T Miyoshi N Tsuji MK Islam X Huang M Motobu MA Alim K Fujisaki, J Insect Physiol 2007 53 195 203 10.1016/j.jinsphys.2006.12.001 17275020
    • (2007) J Insect Physiol , vol.53 , pp. 195-203
    • Miyoshi, T.1    Tsuji, N.2    Islam, M.K.3    Huang, X.4    Motobu, M.5    Alim, M.A.6    Fujisaki, K.7
  • 32
    • 0034666301 scopus 로고    scopus 로고
    • A heme-binding aspartic proteinase from the eggs of the hard tick Boophilus microplus
    • 10.1074/jbc.M005675200 10896678
    • A heme-binding aspartic proteinase from the eggs of the hard tick Boophilus microplus. MH Sorgine C Logullo RB Zingali GO Paiva-Silva L Juliano PL Oliveira, Biol Chem 2000 275 28659 28665 10.1074/jbc.M005675200 10896678
    • (2000) Biol Chem , vol.275 , pp. 28659-28665
    • Sorgine, M.H.1    Logullo, C.2    Zingali, R.B.3    Paiva-Silva, G.O.4    Juliano, L.5    Oliveira, P.L.6
  • 33
    • 15044342339 scopus 로고    scopus 로고
    • The Ixodes scapularis Genome Project: An opportunity for advancing tick research
    • 10.1016/j.pt.2005.02.004 15780833
    • The Ixodes scapularis Genome Project: an opportunity for advancing tick research. CA Hill SK Wikel, Trends Parasitol 2005 21 151 153 10.1016/j.pt.2005.02.004 15780833
    • (2005) Trends Parasitol , vol.21 , pp. 151-153
    • Hill, C.A.1    Wikel, S.K.2
  • 35
    • 33746238440 scopus 로고    scopus 로고
    • Identification and characterization of an asparaginyl proteinase (legumain) from the parasitic nematode, Haemonchus contortus
    • 10.1017/S0031182006000229 16650340
    • Identification and characterization of an asparaginyl proteinase (legumain) from the parasitic nematode, Haemonchus contortus. EM Oliver PJ Skuce CM McNair DP Knox, Parasitology 2006 133 237 244 10.1017/S0031182006000229 16650340
    • (2006) Parasitology , vol.133 , pp. 237-244
    • Oliver, E.M.1    Skuce, P.J.2    McNair, C.M.3    Knox, D.P.4
  • 36
    • 12744262976 scopus 로고    scopus 로고
    • Cysteine proteases of malaria parasites
    • 10.1016/j.ijpara.2004.10.003 15582526
    • Cysteine proteases of malaria parasites. PJ Rosenthal, Int J Parasitol 2004 34 1489 1499 10.1016/j.ijpara.2004.10.003 15582526
    • (2004) Int J Parasitol , vol.34 , pp. 1489-1499
    • Rosenthal, P.J.1
  • 37
    • 33745041171 scopus 로고    scopus 로고
    • Plasmodium falciparum ensures its amino acid supply with multiple acquisition pathways and redundant proteolytic enzyme systems
    • 16731623 10.1073/pnas.0601876103
    • Plasmodium falciparum ensures its amino acid supply with multiple acquisition pathways and redundant proteolytic enzyme systems. J Liu ES Istvan IY Gluzman J Gross DE Goldberg, Proc Nat Acad Sci 2006 103 8840 8805 16731623 10.1073/pnas.0601876103
    • (2006) Proc Nat Acad Sci , vol.103 , pp. 8840-8805
    • Liu, J.1    Istvan, E.S.2    Gluzman, I.Y.3    Gross, J.4    Goldberg, D.E.5
  • 38
    • 33745654531 scopus 로고    scopus 로고
    • Strategies for development of vaccines for control of ixodid tick species
    • 10.1111/j.1365-3024.2006.00828.x 16842264
    • Strategies for development of vaccines for control of ixodid tick species. J de la Fuente KM Kocan, Parasite Immunol 2006 28 275 283 10.1111/j.1365-3024.2006.00828.x 16842264
    • (2006) Parasite Immunol , vol.28 , pp. 275-283
    • De La Fuente, J.1    Kocan, K.M.2
  • 39
    • 0037266549 scopus 로고    scopus 로고
    • A replacement of the active-site aspartic acid residue 293 in mouse cathepsin D affects its intracellular stability, processing and transport in HEK-293 cells
    • 12350228 10.1042/BJ20021226
    • A replacement of the active-site aspartic acid residue 293 in mouse cathepsin D affects its intracellular stability, processing and transport in HEK-293 cells. S Partanen S Storch HG Löffler A Hasilik J Tyynelä T Braulke, Biochem J 2003 369 55 62 12350228 10.1042/BJ20021226
    • (2003) Biochem J , vol.369 , pp. 55-62
    • Partanen, S.1    Storch, S.2    Löffler, H.G.3    Hasilik, A.4    Tyynelä, J.5    Braulke, T.6
  • 40
    • 33845963935 scopus 로고    scopus 로고
    • Cathepsin D propeptide: Mechanism and regulation of its interaction with the catalytic core
    • 10.1021/bi0614986 17176069
    • Cathepsin D propeptide: mechanism and regulation of its interaction with the catalytic core. M Máa L Mareová JR Vondráek M Horn J Jeek M Mare Biochemistry 2006 45 15474 15482 10.1021/bi0614986 17176069
    • (2006) Biochemistry , vol.45 , pp. 15474-15482
    • Máa, M.1    Mareová, L.2    Vondráek, J.R.3    Horn, M.4    Jeek, J.5    Mare, M.6
  • 41
    • 0019887728 scopus 로고
    • Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases
    • 7007374
    • Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases. GD Green E Shaw, J Biol Chem 1981 256 1923 1928 7007374
    • (1981) J Biol Chem , vol.256 , pp. 1923-1928
    • Green, G.D.1    Shaw, E.2
  • 43
    • 28844500817 scopus 로고    scopus 로고
    • High yield synthesis and characterization of phosphorylated recombinant human procathepsin D expressed in mammalian cells
    • 10.1016/j.pep.2005.07.024 16242956
    • High yield synthesis and characterization of phosphorylated recombinant human procathepsin D expressed in mammalian cells. M Demoz R Castino C Follo A Hasilik BF Sloane C Isidoro, Protein Expr Purif 2006 45 157 167 10.1016/j.pep.2005.07.024 16242956
    • (2006) Protein Expr Purif , vol.45 , pp. 157-167
    • Demoz, M.1    Castino, R.2    Follo, C.3    Hasilik, A.4    Sloane, B.F.5    Isidoro, C.6
  • 44
    • 0019765848 scopus 로고
    • Cathepsin B, Cathepsin H, and Cathepsin L
    • 7043200
    • Cathepsin B, Cathepsin H, and Cathepsin L. AJ Barrett H Kirschke, Methods Enzymol 1981 80 535 561 7043200
    • (1981) Methods Enzymol , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 45
    • 0026752536 scopus 로고
    • Purification and characterization of dipeptidyl peptidase i from human spleen
    • 10.1016/0003-9861(92)90519-3 1586157
    • Purification and characterization of dipeptidyl peptidase I from human spleen. MJ McGuire PE Lipsky DL Thiele, Arch Biochem Biophys 1992 295 280 288 10.1016/0003-9861(92)90519-3 1586157
    • (1992) Arch Biochem Biophys , vol.295 , pp. 280-288
    • McGuire, M.J.1    Lipsky, P.E.2    Thiele, D.L.3
  • 46
    • 0027191298 scopus 로고
    • The two cysteine endopeptidases of legume seeds: Purification and characterization by use of specific fluorometric assays
    • 10.1006/abbi.1993.1274 8512309
    • The two cysteine endopeptidases of legume seeds: purification and characterization by use of specific fluorometric assays. AA Kembhavi DJ Buttle CG Knight AJ Barrett, Arch Biochem Biophys 1993 303 208 213 10.1006/abbi.1993. 1274 8512309
    • (1993) Arch Biochem Biophys , vol.303 , pp. 208-213
    • Kembhavi, A.A.1    Buttle, D.J.2    Knight, C.G.3    Barrett, A.J.4
  • 47
    • 33751538306 scopus 로고    scopus 로고
    • Two secreted cystatins of the soft tick Ornithodoros moubata: Differential expression pattern and inhibitory specificity
    • 10.1515/BC.2006.204 17132111
    • Two secreted cystatins of the soft tick Ornithodoros moubata: differential expression pattern and inhibitory specificity. L Grunclová M Horn M Vancová D Sojka Z Franta M Mare P Kopáek, Biol Chem 2006 387 1635 1644 10.1515/BC.2006.204 17132111
    • (2006) Biol Chem , vol.387 , pp. 1635-1644
    • Grunclová, L.1    Horn, M.2    Vancová, M.3    Sojka, D.4    Franta, Z.5    Mare, M.6    Kopáek, P.7
  • 49
    • 0023927144 scopus 로고
    • Human kidney cathepsins B and L. Characterization and potential role in degradation of glomerular basement membrane
    • 2844149
    • Human kidney cathepsins B and L. Characterization and potential role in degradation of glomerular basement membrane. WH Baricos Y Zhou RW Mason AJ Barrett, Biochem J 1988 252 301 344 2844149
    • (1988) Biochem J , vol.252 , pp. 301-344
    • Baricos, W.H.1    Zhou, Y.2    Mason, R.W.3    Barrett, A.J.4
  • 50
    • 0017255236 scopus 로고
    • Interaction of human cathepsin D with the inhibitor pepstatin
    • 938470
    • Interaction of human cathepsin D with the inhibitor pepstatin. CG Knight AJ Barrett, Biochem J 1976 155 117 125 938470
    • (1976) Biochem J , vol.155 , pp. 117-125
    • Knight, C.G.1    Barrett, A.J.2
  • 51
    • 64949116930 scopus 로고    scopus 로고
    • blastn. http://www.ncbi.nlm.nih.gov/BLAST/
    • Blastn
  • 54
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • 9396791 10.1093/nar/25.24.4876
    • The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. JD Thompson TJ Gibson F Plewniak F Jeanmougin DG Higgins, Nucleic Acids Res 1997 25 4876 4882 9396791 10.1093/nar/25.24.4876
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 55
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. TA Hall, Nucl Acids Symp Ser 1999 41 95 98
    • (1999) Nucl Acids Symp ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 56
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • 3447015
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees. N Saitou M Nei, Mol Biol Evol 1987 4 406 425 3447015
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 57
    • 0036139211 scopus 로고    scopus 로고
    • MEGA2: Molecular evolutionary genetics analysis software
    • 10.1093/bioinformatics/17.12.1244 11751241
    • MEGA2: molecular evolutionary genetics analysis software. S Kumar K Tamura IB Jakobsen M Nei, Bioinformatics 2001 17 1244 1255 10.1093/ bioinformatics/17.12.1244 11751241
    • (2001) Bioinformatics , vol.17 , pp. 1244-1255
    • Kumar, S.1    Tamura, K.2    Jakobsen, I.B.3    Nei, M.4
  • 58
    • 0037211912 scopus 로고    scopus 로고
    • Molecular cloning, expression and isolation of ferritins from two tick species-Ornithodoros moubata and Ixodes ricinus
    • 10.1016/S0965-1748(02)00181-9 12459205
    • Molecular cloning, expression and isolation of ferritins from two tick species-Ornithodoros moubata and Ixodes ricinus. P Kopáek J dychová T Yoshiga C Weise N Rudenko JH Law, Insect Biochem Mol Biol 2003 233 103 113 10.1016/S0965-1748(02)00181-9 12459205
    • (2003) Insect Biochem Mol Biol , vol.233 , pp. 103-113
    • Kopáek, P.1    Dychová, J.2    Yoshiga, T.3    Weise, C.4    Rudenko, N.5    Law, J.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.