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Volumn 145, Issue 2, 2006, Pages 147-157

Cloning and characterization of angiotensin converting enzyme related dipeptidylcarboxypeptidase from Leishmania donovani

Author keywords

Dipeptidylcarboxypeptidase; Drug target; Exopeptidases; Kala azar; Leishmania donovani

Indexed keywords

ALANINE; ANGIOTENSIN I; CAPTOPRIL; DIPEPTIDYL CARBOXYPEPTIDASE; GLUTAMIC ACID; HISTIDINE; HYPERTENSIVE AGENT;

EID: 30544442263     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2005.09.014     Document Type: Article
Times cited : (23)

References (54)
  • 1
    • 0035067363 scopus 로고    scopus 로고
    • Leishmaniasis current status of vaccine development
    • E. Handman Leishmaniasis current status of vaccine development Clin Microbiol Rev 14 2001 229 243
    • (2001) Clin Microbiol Rev , vol.14 , pp. 229-243
    • Handman, E.1
  • 2
    • 0026592139 scopus 로고
    • Human Leishmniasis: Epidemiology and public health aspects
    • P. Desjeux Human Leishmniasis: epidemiology and public health aspects World Health Stat Quart 45 1992 267 275
    • (1992) World Health Stat Quart , vol.45 , pp. 267-275
    • Desjeux, P.1
  • 3
    • 0000969567 scopus 로고
    • Morphology, ultrastructure and lifecycles
    • W. Peters R. Killick-Kendrick Academic Press
    • D. Molyneux, and R. Killick-Kendrick Morphology, ultrastructure and lifecycles W. Peters R. Killick-Kendrick The leishmaniasis in biology and Medicine vol. 1 1987 Academic Press 121 176
    • (1987) The Leishmaniasis in Biology and Medicine , vol.1 , pp. 121-176
    • Molyneux, D.1    Killick-Kendrick, R.2
  • 4
    • 0026533657 scopus 로고
    • The interaction of Leishamania species with macrophages
    • J. Alexander, and D.G. Russel The interaction of Leishamania species with macrophages Adv Parasitol 32 1992 175 254
    • (1992) Adv Parasitol , vol.32 , pp. 175-254
    • Alexander, J.1    Russel, D.G.2
  • 5
    • 0028061958 scopus 로고
    • The role of pH and temperature on the development of Leishmania parasites
    • D. Zilberstein, and M. Shapira The role of pH and temperature on the development of Leishmania parasites Annu Rev Microbiol 48 1994 449 470
    • (1994) Annu Rev Microbiol , vol.48 , pp. 449-470
    • Zilberstein, D.1    Shapira, M.2
  • 6
    • 0032967680 scopus 로고    scopus 로고
    • Effect of acidic pH on heat shock gene expression in Leishmania
    • S. Garlapati, E. Dahan, and M. Shapira Effect of acidic pH on heat shock gene expression in Leishmania Mol Biochem Parasitol 100 1999 95 101
    • (1999) Mol Biochem Parasitol , vol.100 , pp. 95-101
    • Garlapati, S.1    Dahan, E.2    Shapira, M.3
  • 7
    • 0030841734 scopus 로고    scopus 로고
    • Loss of virulence in Leishmania donovani deficient in an amastigote specific protein A2
    • W.W. Zang, and G. Matlashewski Loss of virulence in Leishmania donovani deficient in an amastigote specific protein A2 Proc Natl Acad Sci USA 94 1997 8807 8811
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8807-8811
    • Zang, W.W.1    Matlashewski, G.2
  • 8
    • 0033727540 scopus 로고    scopus 로고
    • A new developmentally regulated gene family in Leishmania amastigotes encoding a homology of amastin surface protein
    • F.Y. Wu El, D. Sereno, S. Tamar, and B. Papadopulou A new developmentally regulated gene family in Leishmania amastigotes encoding a homology of amastin surface protein Mol Biochem Parasitol 110 2000 345 357
    • (2000) Mol Biochem Parasitol , vol.110 , pp. 345-357
    • Wu El, F.Y.1    Sereno, D.2    Tamar, S.3    Papadopulou, B.4
  • 9
    • 0035203992 scopus 로고    scopus 로고
    • Heat shock Protein 90 homeostatic controls stage differentiation in Leishmania donovani
    • M. Wiesgigl, and J. Clos Heat shock Protein 90 homeostatic controls stage differentiation in Leishmania donovani Mol Biol Cell 12 2001 3307 3316
    • (2001) Mol Biol Cell , vol.12 , pp. 3307-3316
    • Wiesgigl, M.1    Clos, J.2
  • 10
    • 2942535893 scopus 로고    scopus 로고
    • Centrin gene disruption impairs stage specific basal body duplication and cell cycle progression in Leishmania
    • A. Selvapandiyan, A. Debrabant, and R. Duncan Centrin gene disruption impairs stage specific basal body duplication and cell cycle progression in Leishmania J Biol Chem 279 2004 25703 25710
    • (2004) J Biol Chem , vol.279 , pp. 25703-25710
    • Selvapandiyan, A.1    Debrabant, A.2    Duncan, R.3
  • 11
    • 0033042010 scopus 로고    scopus 로고
    • Proteases of protozoan parasites
    • F.J. Rosenthal Proteases of protozoan parasites Adv Parasitol 43 1999 105 159
    • (1999) Adv Parasitol , vol.43 , pp. 105-159
    • Rosenthal, F.J.1
  • 12
  • 13
    • 0029038660 scopus 로고
    • Leishmanolysin: Surface metalloproteinase of Leishmania
    • J. Bouvier, P. Schneider, and R. Etges Leishmanolysin: surface metalloproteinase of Leishmania Meth Enzymol 248 1995 614 633
    • (1995) Meth Enzymol , vol.248 , pp. 614-633
    • Bouvier, J.1    Schneider, P.2    Etges, R.3
  • 14
    • 0344625412 scopus 로고    scopus 로고
    • Leishmania (Leishmania) amazonensis: Purification and enzymatic characterization of soluble serine oligopeptidase
    • A.S. Andrade Ribeirode, M.M. Santero, M.N. de Melo, and M. Mares-Guia Leishmania (Leishmania) amazonensis: purification and enzymatic characterization of soluble serine oligopeptidase Exp Parasitol 89 1998 153 160
    • (1998) Exp Parasitol , vol.89 , pp. 153-160
    • Andrade Ribeirode, A.S.1    Santero, M.M.2    De Melo, M.N.3    Mares-Guia, M.4
  • 15
    • 0037135520 scopus 로고    scopus 로고
    • Cloning and characterization of leucylaminopeptidase from three pathogenic Leishmania species
    • R.E. Morty, and J. Morehead Cloning and characterization of leucylaminopeptidase from three pathogenic Leishmania species J Biol Chem 277 2002 26057 26065
    • (2002) J Biol Chem , vol.277 , pp. 26057-26065
    • Morty, R.E.1    Morehead, J.2
  • 16
    • 0027761911 scopus 로고
    • Characterization of two soluble metalloprotease in protozoan parasite Leishmania major
    • P. Schneider, and T.A. Glaser Characterization of two soluble metalloprotease in protozoan parasite Leishmania major Mol Biochem Parasitol 62 1993 223 231
    • (1993) Mol Biochem Parasitol , vol.62 , pp. 223-231
    • Schneider, P.1    Glaser, T.A.2
  • 17
    • 0027745973 scopus 로고
    • Cathepsin B like cysteine protease of Leishmania mexicana
    • C.D. Robertson, and G.H. Coombs Cathepsin B like cysteine protease of Leishmania mexicana Mol Biochem Parasitol 62 1993 271 279
    • (1993) Mol Biochem Parasitol , vol.62 , pp. 271-279
    • Robertson, C.D.1    Coombs, G.H.2
  • 19
    • 1542374556 scopus 로고    scopus 로고
    • Carboxy dipeptidase activities of recombinant cysteine peptidase cruzain of Trypanosoma cruzi and CPB of Leishmania mexicana
    • W.A.S. Judice, L. Puzer, and S.S. Cortin Carboxy dipeptidase activities of recombinant cysteine peptidase cruzain of Trypanosoma cruzi and CPB of Leishmania mexicana Eur J Biochem 271 2004 1046 1053
    • (2004) Eur J Biochem , vol.271 , pp. 1046-1053
    • Judice, W.A.S.1    Puzer, L.2    Cortin, S.S.3
  • 20
  • 21
    • 84961004518 scopus 로고
    • The purification of hypertension II
    • L.T. Skeggs, J.R. Kahn, and N.P. Shumway The purification of hypertension II J Exp Med 103 1956 301 307
    • (1956) J Exp Med , vol.103 , pp. 301-307
    • Skeggs, L.T.1    Kahn, J.R.2    Shumway, N.P.3
  • 22
    • 0017102431 scopus 로고
    • Angiotensin converting enzyme and the regulation of vasoactive peptides
    • R.L. Soffer Angiotensin converting enzyme and the regulation of vasoactive peptides Annu Rev Biochem 45 1976 73 94
    • (1976) Annu Rev Biochem , vol.45 , pp. 73-94
    • Soffer, R.L.1
  • 23
    • 0018237538 scopus 로고
    • Escherichia coli mutant defective in dipeptidyl carboxypeptidase
    • C.E. Deutch, and R.L. Soffer Escherichia coli mutant defective in dipeptidyl carboxypeptidase Pro Natl Acad Sci USA 75 1978 5998 6001
    • (1978) Pro Natl Acad Sci USA , vol.75 , pp. 5998-6001
    • Deutch, C.E.1    Soffer, R.L.2
  • 24
    • 0029046178 scopus 로고
    • Isolation and characterization of gene encoding the surface membrane 3′-nucleotidase/nuclease of Leishmania donovani
    • A. Debrabant, M. Gottilieb, and D.M. Dwyer Isolation and characterization of gene encoding the surface membrane 3′-nucleotidase/nuclease of Leishmania donovani Mol Biochem Parasitol 71 1995 51 63
    • (1995) Mol Biochem Parasitol , vol.71 , pp. 51-63
    • Debrabant, A.1    Gottilieb, M.2    Dwyer, D.M.3
  • 25
    • 1242294372 scopus 로고    scopus 로고
    • Generation of Leishmania amastigotes, their growth and biological characteristics
    • A. Debrabant, M.B. Joshi, P.F. Pimenta, and D.M. Dwyer Generation of Leishmania amastigotes, their growth and biological characteristics Int J Parasitol 34 2004 205 217
    • (2004) Int J Parasitol , vol.34 , pp. 205-217
    • Debrabant, A.1    Joshi, M.B.2    Pimenta, P.F.3    Dwyer, D.M.4
  • 26
    • 0035815347 scopus 로고    scopus 로고
    • A survey of Leishmania major Friedlin strain VI genome by short gun sequencing: A resource of DNA microarray and expression profiling
    • N.S. Akyopyants, S.W. Clifton, and J. Martin A survey of Leishmania major Friedlin strain VI genome by short gun sequencing: a resource of DNA microarray and expression profiling Mol Biochem Parasitol 113 2001 337 340
    • (2001) Mol Biochem Parasitol , vol.113 , pp. 337-340
    • Akyopyants, N.S.1    Clifton, S.W.2    Martin, J.3
  • 27
  • 28
    • 0026049349 scopus 로고
    • Nucleotide sequence of Leishmania donovani medRNA gene
    • K. Wilson, S. Hanson, S. Landfear, and B. Ulman Nucleotide sequence of Leishmania donovani medRNA gene Nucl Acid Res 19 1991 5787
    • (1991) Nucl Acid Res , vol.19 , pp. 5787
    • Wilson, K.1    Hanson, S.2    Landfear, S.3    Ulman, B.4
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structrural proteins during the assembly of the head of bacteriphage T4
    • U.K. Lammeli Cleavage of structrural proteins during the assembly of the head of bacteriphage T4 Nature 227 1970 678 685
    • (1970) Nature , vol.227 , pp. 678-685
    • Lammeli, U.K.1
  • 31
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some application
    • H. Towbin, T. Staehelin, and B. Falgout Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some application Proc Natl Acad Sci USA 76 1979 4350 4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Falgout, B.3
  • 33
    • 0037449810 scopus 로고    scopus 로고
    • An atypical protein disulfide isomerase from protozoan parasite Leishmania containing a single thirodoxin like domain
    • A. Padilla, R. Noiva, N. Lee, K.V. Krishna Mohan, H.L. Nakhasi, and A. Debrabant An atypical protein disulfide isomerase from protozoan parasite Leishmania containing a single thirodoxin like domain J Biol Chem 278 2003 1872 1878
    • (2003) J Biol Chem , vol.278 , pp. 1872-1878
    • Padilla, A.1    Noiva, R.2    Lee, N.3    Krishna Mohan, K.V.4    Nakhasi, H.L.5    Debrabant, A.6
  • 34
    • 0015083353 scopus 로고
    • Spectrophotometric assay for angiotensin converting enzyme
    • D.W. Cushman, and H.S. Cheung Spectrophotometric assay for angiotensin converting enzyme Biochem Pharmacol 20 1971 1637 1648
    • (1971) Biochem Pharmacol , vol.20 , pp. 1637-1648
    • Cushman, D.W.1    Cheung, H.S.2
  • 35
    • 0018398672 scopus 로고
    • A continous spectrophotometric assay for angiotensin converting enzyme
    • B. Holmquist, P. Burnning, and J.F. Riordan A continous spectrophotometric assay for angiotensin converting enzyme Anal Biochem 95 1979 540 548
    • (1979) Anal Biochem , vol.95 , pp. 540-548
    • Holmquist, B.1    Burnning, P.2    Riordan, J.F.3
  • 36
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding Anal Biochem 72 1976 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 37
    • 0028215740 scopus 로고
    • Use of water soluble formazan complex to quantitate the cell number and mitochondrial function of Leishmania major promastigotes
    • K. Berg, L. Zhai, A. Chen, A. Kharazmi, and T.C. Owen Use of water soluble formazan complex to quantitate the cell number and mitochondrial function of Leishmania major promastigotes Parasitol Res 80 1994 235 239
    • (1994) Parasitol Res , vol.80 , pp. 235-239
    • Berg, K.1    Zhai, L.2    Chen, A.3    Kharazmi, A.4    Owen, T.C.5
  • 38
    • 0030926411 scopus 로고    scopus 로고
    • Distruption of trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages
    • C. Dumas, M. Ouellette, and J. Tovar Distruption of trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages EMBO J 1 1997 2590 2598
    • (1997) EMBO J , vol.1 , pp. 2590-2598
    • Dumas, C.1    Ouellette, M.2    Tovar, J.3
  • 39
    • 0027425738 scopus 로고
    • Dcp Gene of Escherichia coli: Cloning, sequencing, transcript mapping and characterization of the gene product
    • B. Henrich, S. Becker, U. Schroeder, and R. Plapp dcp Gene of Escherichia coli: cloning, sequencing, transcript mapping and characterization of the gene product J Bacteriol 175 1993 7290 7300
    • (1993) J Bacteriol , vol.175 , pp. 7290-7300
    • Henrich, B.1    Becker, S.2    Schroeder, U.3    Plapp, R.4
  • 40
    • 0141888314 scopus 로고    scopus 로고
    • The major surface protease (MSP or GP63) of Leishmania species: Biosynthesis, regulation of expression and function
    • C. Yao, J.E. Donelson, and M.E. Wilson The major surface protease (MSP or GP63) of Leishmania species: biosynthesis, regulation of expression and function Mol Biochem Parasitol 132 2003 1 16
    • (2003) Mol Biochem Parasitol , vol.132 , pp. 1-16
    • Yao, C.1    Donelson, J.E.2    Wilson, M.E.3
  • 41
    • 0029898541 scopus 로고    scopus 로고
    • Evidence from disruption of the Lmcpb gene array of Leishmania mexicana that cysteine proteinases are virulence factors
    • J.C. Mottram, A.E. Souza, J.E. Hutchinson, R. Carter, M.J. Frame, and G.H. Coombs Evidence from disruption of the Lmcpb gene array of Leishmania mexicana that cysteine proteinases are virulence factors Proc Natl Acad Sci USA 93 1996 6008 6013
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6008-6013
    • Mottram, J.C.1    Souza, A.E.2    Hutchinson, J.E.3    Carter, R.4    Frame, M.J.5    Coombs, G.H.6
  • 42
    • 13044256387 scopus 로고    scopus 로고
    • Cysteine proteinase inhibitors as chemotherapy: Lessons from parasite target
    • P.M. Selzer, S. Pingel, and I. Hseih Cysteine proteinase inhibitors as chemotherapy: lessons from parasite target Proc Natl Acad Sci USA 96 1999 11015 11022
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11015-11022
    • Selzer, P.M.1    Pingel, S.2    Hseih, I.3
  • 43
    • 0035858106 scopus 로고    scopus 로고
    • A protective cocktail vaccine against murine cutaneous leishmaniasis with DNA encoding cysteine proteinases of Leishmania major
    • S. Rafati, A.H. Salmanian, T. Tahei, M. Vafa, and N. Fasel A protective cocktail vaccine against murine cutaneous leishmaniasis with DNA encoding cysteine proteinases of Leishmania major Vaccine 19 2001 3369 3375
    • (2001) Vaccine , vol.19 , pp. 3369-3375
    • Rafati, S.1    Salmanian, A.H.2    Tahei, T.3    Vafa, M.4    Fasel, N.5
  • 44
    • 0035946347 scopus 로고    scopus 로고
    • In vitro cytocidal effect on Trypanosoma brucei and inhibition of Leishmania major GP 63 by peptidomimetic metalloprotease inhibitor
    • J.D. Bang, D.A. Ransom, D.A. Nimik, G. Christie, and N.M. Hooper In vitro cytocidal effect on Trypanosoma brucei and inhibition of Leishmania major GP 63 by peptidomimetic metalloprotease inhibitor Mol Biochem Parasitol 114 2001 111 117
    • (2001) Mol Biochem Parasitol , vol.114 , pp. 111-117
    • Bang, J.D.1    Ransom, D.A.2    Nimik, D.A.3    Christie, G.4    Hooper, N.M.5
  • 46
    • 0025007049 scopus 로고
    • Molecular cloning and primary structure of rat testes metalloendopeptidase E.C.3.4.24.15
    • A. Pierotti, K.W. Dong, M.J. Glucksman, M. Orlowski, and J.L. Robert Molecular cloning and primary structure of rat testes metalloendopeptidase E.C.3.4.24.15 Biochemistry 29 1990 10323 10329
    • (1990) Biochemistry , vol.29 , pp. 10323-10329
    • Pierotti, A.1    Dong, K.W.2    Glucksman, M.J.3    Orlowski, M.4    Robert, J.L.5
  • 47
    • 0026830327 scopus 로고
    • Cloning and nucleotide sequence of opdA, the gene encoding oligopeptidaseA in Salmonella typhimurium
    • C.A. Colin, and C.G. Miller Cloning and nucleotide sequence of opdA, the gene encoding oligopeptidaseA in Salmonella typhimurium J Bacteriol 174 1992 1631 1640
    • (1992) J Bacteriol , vol.174 , pp. 1631-1640
    • Colin, C.A.1    Miller, C.G.2
  • 48
    • 0026596421 scopus 로고
    • Yeast sequencing reports: The complete sequence of K3b, a 7.9 kb fragment between PKG1on chromosome 11 reveals the presence of seven open reading frames
    • P.A. Bolle, V. Gilliquet, G. Berben, J. Dumont, and F. Hilger Yeast sequencing reports: the complete sequence of K3b, a 7.9 kb fragment between PKG1on chromosome 11 reveals the presence of seven open reading frames Yeast 8 1992 205 213
    • (1992) Yeast , vol.8 , pp. 205-213
    • Bolle, P.A.1    Gilliquet, V.2    Berben, G.3    Dumont, J.4    Hilger, F.5
  • 49
    • 0026825857 scopus 로고
    • Cloning and nucleotide sequence of Salmonella typhimurium dcp gene encoding dipeptidyl carboxypaptidase
    • S. Hamilton, and C.G. Miller Cloning and nucleotide sequence of Salmonella typhimurium dcp gene encoding dipeptidyl carboxypaptidase J Bacteriol 174 1992 1626 1630
    • (1992) J Bacteriol , vol.174 , pp. 1626-1630
    • Hamilton, S.1    Miller, C.G.2
  • 50
    • 0019206260 scopus 로고
    • Degradation of intracellular proteins in Salmonella typhimurium peptidase mutants
    • C. Yen, L. Green, and C.G. Miller Degradation of intracellular proteins in Salmonella typhimurium peptidase mutants J Mol Biol 143 1980 21 23
    • (1980) J Mol Biol , vol.143 , pp. 21-23
    • Yen, C.1    Green, L.2    Miller, C.G.3
  • 51
    • 0019788287 scopus 로고
    • Degradation of abnormal proteins in peptidase deficient mutants of Salmonella typhimurium
    • C.G. Miller, and L. Green Degradation of abnormal proteins in peptidase deficient mutants of Salmonella typhimurium J Bacteriol 147 1981 925 930
    • (1981) J Bacteriol , vol.147 , pp. 925-930
    • Miller, C.G.1    Green, L.2
  • 52
    • 0025941521 scopus 로고
    • Biochemical and Molecular characterization of L. pifanoi amastigotes in continous axenic culture
    • P.M. Rainey, T.W. Spithill, D. McMahon-Pratt, and A.A. Pan Biochemical and Molecular characterization of L. pifanoi amastigotes in continous axenic culture Mol Biochem Parasitol 49 1991 111 118
    • (1991) Mol Biochem Parasitol , vol.49 , pp. 111-118
    • Rainey, P.M.1    Spithill, T.W.2    McMahon-Pratt, D.3    Pan, A.A.4
  • 53
    • 0017584729 scopus 로고
    • Design of potent competitive inhibitors of angiotensin converting enzymes: Carboxyalkanoyl and mercaptoalkanoyl amino acids
    • D.W. Cushman, H.S. Cheung, E.F. Sabo, and M.P. Ondetti Design of potent competitive inhibitors of angiotensin converting enzymes: carboxyalkanoyl and mercaptoalkanoyl amino acids Biochemistry 16 1977 5484 5491
    • (1977) Biochemistry , vol.16 , pp. 5484-5491
    • Cushman, D.W.1    Cheung, H.S.2    Sabo, E.F.3    Ondetti, M.P.4
  • 54
    • 0020586871 scopus 로고
    • Dipeptidylcarboxypaptidase deficient mutants of Salmonella typhimurium
    • E.R. Vimr, and C.C. Miller Dipeptidylcarboxypaptidase deficient mutants of Salmonella typhimurium J Bacteriol 153 1983 1252 1258
    • (1983) J Bacteriol , vol.153 , pp. 1252-1258
    • Vimr, E.R.1    Miller, C.C.2


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