메뉴 건너뛰기




Volumn 87, Issue 3, 1997, Pages 171-184

Haemonchus contortus: Cloning and functional expression of a cDNA encoding ornithine decarboxylase and development of a screen for inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; EFLORNITHINE; ORNITHINE DECARBOXYLASE;

EID: 0031282538     PISSN: 00144894     EISSN: None     Source Type: Journal    
DOI: 10.1006/expr.1997.4213     Document Type: Article
Times cited : (19)

References (54)
  • 2
    • 0026683752 scopus 로고
    • Ornithine decarboyxlase activity is critical for cell transformation
    • Auvinen, M., Paasinen, A., Andersson, L. C., and Hölttä, E. 1992. Ornithine decarboyxlase activity is critical for cell transformation. Nature 360, 355-358.
    • (1992) Nature , vol.360 , pp. 355-358
    • Auvinen, M.1    Paasinen, A.2    Andersson, L.C.3    Hölttä, E.4
  • 3
    • 0002960266 scopus 로고
    • Parasitic protozoa and polyamines
    • P. P. McCann, A. E. Pegg, and A. Sjoerdsma, Eds. Academic Press, Inc., Orlando, FL
    • Bacchi, C. J., and McCann, P. P. 1987. Parasitic protozoa and polyamines. In "Inhibition of Polyamine Metabolism" (P. P. McCann, A. E. Pegg, and A. Sjoerdsma, Eds.), pp. 317-344. Academic Press, Inc., Orlando, FL.
    • (1987) Inhibition of Polyamine Metabolism , pp. 317-344
    • Bacchi, C.J.1    McCann, P.P.2
  • 6
    • 0028029974 scopus 로고
    • The presence of an active S-adenosylmethionine decarboxylase gene increases the growth defect observed in Saccharomyces cerevisiae mutants unable to synthesize putrescine, spremidine, and spermine
    • Balasundaram, D., Xie, Q-W., Tabor, C. W., and Tabor, H. 1994. The presence of an active S-adenosylmethionine decarboxylase gene increases the growth defect observed in Saccharomyces cerevisiae mutants unable to synthesize putrescine, spremidine, and spermine. Journal of Bacteriology 176, 6407-6409.
    • (1994) Journal of Bacteriology , vol.176 , pp. 6407-6409
    • Balasundaram, D.1    Xie, Q.-W.2    Tabor, C.W.3    Tabor, H.4
  • 7
    • 0022454288 scopus 로고
    • Characterization of Trypanosoma brucei brucei S-adenosyl-L-methionine decarboxylase and its inhibition by Berenil, pentamidine and methylglyoxal bis(guanyl-hydrazone)
    • Bitonti, A. J., Dumont, J. A., and McCann, P. P. 1986. Characterization of Trypanosoma brucei brucei S-adenosyl-L-methionine decarboxylase and its inhibition by Berenil, pentamidine and methylglyoxal bis(guanyl-hydrazone). Biochemical Journal 237, 685-689.
    • (1986) Biochemical Journal , vol.237 , pp. 685-689
    • Bitonti, A.J.1    Dumont, J.A.2    McCann, P.P.3
  • 8
    • 0020670098 scopus 로고
    • The accumulation of polyamines and paraquat by human peripheral lung
    • Brooke-Taylor, S., Smith, L. L., and Cohen, G. M. 1983. The accumulation of polyamines and paraquat by human peripheral lung. Biochemical Pharmacology 32, 717-720.
    • (1983) Biochemical Pharmacology , vol.32 , pp. 717-720
    • Brooke-Taylor, S.1    Smith, L.L.2    Cohen, G.M.3
  • 9
    • 0019119792 scopus 로고
    • Regulatory mutations affecting ornithine decarboxylase activity in Saccharomyces cerevisiae
    • Cohn, M. S., Tabor, C. W., and Tabor, H. 1980. Regulatory mutations affecting ornithine decarboxylase activity in Saccharomyces cerevisiae. Journal of Bacteriology 142, 791-799.
    • (1980) Journal of Bacteriology , vol.142 , pp. 791-799
    • Cohn, M.S.1    Tabor, C.W.2    Tabor, H.3
  • 10
    • 0027504342 scopus 로고
    • Effect of mutations at active site residues on the activity of ornithine decarboxylase and its inhibition by active site-directed irreversible inhibitors
    • Coleman, C. S., Stanley, B. A., and Pegg, A. E. 1993. Effect of mutations at active site residues on the activity of ornithine decarboxylase and its inhibition by active site-directed irreversible inhibitors. Journal of Biological Chemistry 268, 24572-24579.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 24572-24579
    • Coleman, C.S.1    Stanley, B.A.2    Pegg, A.E.3
  • 11
    • 0029853782 scopus 로고    scopus 로고
    • A novel trans-spliced mRNA from Onchocerca volvulus encodes a functional S-adenosylmethionine decarboxylase
    • Da' Dara, A. A., Henkle-Dührsen, K., and Walter, R. D. 1996. A novel trans-spliced mRNA from Onchocerca volvulus encodes a functional S-adenosylmethionine decarboxylase. Biochemical Journal 320, 519-530.
    • (1996) Biochemical Journal , vol.320 , pp. 519-530
    • Da' Dara, A.A.1    Henkle-Dührsen, K.2    Walter, R.D.3
  • 12
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereaux, J., Harberli, P., and Smithies, O. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Research 12, 387-394.
    • (1984) Nucleic Acids Research , vol.12 , pp. 387-394
    • Devereaux, J.1    Harberli, P.2    Smithies, O.3
  • 13
    • 0019985069 scopus 로고
    • Uptake of α-difluoromethylornithine by mouse fibroblasts
    • Erwin, B. G., and Pegg, A. E. 1982. Uptake of α-difluoromethylornithine by mouse fibroblasts. Biochemical Pharmacology 31, 2820-2823.
    • (1982) Biochemical Pharmacology , vol.31 , pp. 2820-2823
    • Erwin, B.G.1    Pegg, A.E.2
  • 14
    • 0023664659 scopus 로고
    • The gene and primary structure of ornithine decarboxylase from Saccharomyces cerevisiae
    • Fonzi, W. A., and Sypherd, P. S. 1987. The gene and primary structure of ornithine decarboxylase from Saccharomyces cerevisiae. Journal of Biological Chemistry 262, 10127-10133.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 10127-10133
    • Fonzi, W.A.1    Sypherd, P.S.2
  • 16
    • 0018633031 scopus 로고
    • Mutants of Escherichia coli that do not contain 1,4-diaminobutane (putrescine) or spermidine
    • Hafner, E. W., Tabor, C. W., and Tabor, H. 1979. Mutants of Escherichia coli that do not contain 1,4-diaminobutane (putrescine) or spermidine. Journal of Biological Chemistry 254, 419-426.
    • (1979) Journal of Biological Chemistry , vol.254 , pp. 419-426
    • Hafner, E.W.1    Tabor, C.W.2    Tabor, H.3
  • 17
    • 0000897560 scopus 로고
    • Transport interactions between paraquat and polyamines in roots of intact maize seedlings
    • Hart, J. J., DiTomaso, J. M., Linscott, D. L., and Kochian, L. V. 1992. Transport interactions between paraquat and polyamines in roots of intact maize seedlings. Plant Physiology 99, 1400-1405.
    • (1992) Plant Physiology , vol.99 , pp. 1400-1405
    • Hart, J.J.1    DiTomaso, J.M.2    Linscott, D.L.3    Kochian, L.V.4
  • 18
    • 0022400737 scopus 로고
    • Irreversible inhibition of putrescine-stimulated S-adenosyl-L-methionine decarboxylase by Berenil and Pentamidine
    • Karvonen, E., Kauppinen, L., Partanen, T., and Pösö, H. 1985. Irreversible inhibition of putrescine-stimulated S-adenosyl-L-methionine decarboxylase by Berenil and Pentamidine. Biochemical Journal 231, 165-169.
    • (1985) Biochemical Journal , vol.231 , pp. 165-169
    • Karvonen, E.1    Kauppinen, L.2    Partanen, T.3    Pösö, H.4
  • 21
    • 0002025886 scopus 로고    scopus 로고
    • Recombinant microorganisms as tools for high throughput screening for non-antibiotic compounds
    • Klein, R. D., and Geary, T. G. 1997. Recombinant microorganisms as tools for high throughput screening for non-antibiotic compounds. Journal of Biomolecular Screening 2, 41-49.
    • (1997) Journal of Biomolecular Screening , vol.2 , pp. 41-49
    • Klein, R.D.1    Geary, T.G.2
  • 22
    • 0023782502 scopus 로고
    • Isolation of a gene from Schwanniomyces occidentalis which complements a ura-3 mutation in Saccharomyces cerevisiae
    • Klein, R. D., and Roof, L. L. 1988. Isolation of a gene from Schwanniomyces occidentalis which complements a ura-3 mutation in Saccharomyces cerevisiae. Current Genetics 13, 29-35.
    • (1988) Current Genetics , vol.13 , pp. 29-35
    • Klein, R.D.1    Roof, L.L.2
  • 25
    • 0029044140 scopus 로고
    • The ornithine decarboxylase gene of Caenorhabditis elegans: Cloning, mapping and mutagenesis
    • Macrae, M., Plasterk, R. H., and Coffino, P. 1995. The ornithine decarboxylase gene of Caenorhabditis elegans: cloning, mapping and mutagenesis. Genetics 140, 517-525.
    • (1995) Genetics , vol.140 , pp. 517-525
    • Macrae, M.1    Plasterk, R.H.2    Coffino, P.3
  • 26
    • 0027976621 scopus 로고
    • The 20S proteasome mediates the degradation of mouse and yeast ornithine decarboxylase in yeast cells
    • Mamroud-Kidron, E., Rosenberg-Hasson, Y., Rom, E., and Kahana, C. 1994. The 20S proteasome mediates the degradation of mouse and yeast ornithine decarboxylase in yeast cells. FEBS Lett. 337, 239-242.
    • (1994) FEBS Lett. , vol.337 , pp. 239-242
    • Mamroud-Kidron, E.1    Rosenberg-Hasson, Y.2    Rom, E.3    Kahana, C.4
  • 27
    • 0025052130 scopus 로고
    • Inhibition of the dimorphic transition of Candida albicans by the ornithine decarboxylase inhibitor 1,4-diaminobutane: Alterations in the glycoprotein component of the cell wall
    • Martinez, J. P., Lopez-Ribot, J. L., Gil, M. L., Sentandreu, R., and Ruiz-Herrera, J. 1990. Inhibition of the dimorphic transition of Candida albicans by the ornithine decarboxylase inhibitor 1,4-diaminobutane: alterations in the glycoprotein component of the cell wall. Journal of General Microbiology 136, 1937-1943.
    • (1990) Journal of General Microbiology , vol.136 , pp. 1937-1943
    • Martinez, J.P.1    Lopez-Ribot, J.L.2    Gil, M.L.3    Sentandreu, R.4    Ruiz-Herrera, J.5
  • 29
    • 0025305215 scopus 로고
    • Paraquat toxicity is increased in Escherichia coli defective in the synthesis of polyamines
    • Minton, K. W., Tabor, H., and Tabor, C. W. 1990. Paraquat toxicity is increased in Escherichia coli defective in the synthesis of polyamines. Proceedings of the National Academy of Sciences USA 87, 2851-2855.
    • (1990) Proceedings of the National Academy of Sciences USA , vol.87 , pp. 2851-2855
    • Minton, K.W.1    Tabor, H.2    Tabor, C.W.3
  • 30
    • 0027263467 scopus 로고
    • Transformation of NIH/3T3 cells by ornithine decarboxylase overexpression
    • Moshier, J. A., Dosescu, J., Skunca, M., and Luk, G. D. 1993. Transformation of NIH/3T3 cells by ornithine decarboxylase overexpression. Cancer Research 53, 2618-2622.
    • (1993) Cancer Research , vol.53 , pp. 2618-2622
    • Moshier, J.A.1    Dosescu, J.2    Skunca, M.3    Luk, G.D.4
  • 32
    • 0029970148 scopus 로고    scopus 로고
    • Panagrellus redivivus ornithine decarboxylase: Structure of the gene, expression in Escherichia coli and characterization of the recombinant protein
    • Niemann, G., von Besser, H., and Walter, R. D. 1996. Panagrellus redivivus ornithine decarboxylase: structure of the gene, expression in Escherichia coli and characterization of the recombinant protein. Biochemical Journal 317, 135-140.
    • (1996) Biochemical Journal , vol.317 , pp. 135-140
    • Niemann, G.1    Von Besser, H.2    Walter, R.D.3
  • 33
    • 0029042171 scopus 로고
    • Acidic residues important for substrate binding and cofactor reactivity in eukaryotic ornithine decarboxylase identified by alanine scanning mutagenesis
    • Osterman, A. L., Kinch, L. N., Grishin, N. V., and Phillips, M. A. 1995. Acidic residues important for substrate binding and cofactor reactivity in eukaryotic ornithine decarboxylase identified by alanine scanning mutagenesis. Journal of Biological Chemistry 270, 11797-11802.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 11797-11802
    • Osterman, A.L.1    Kinch, L.N.2    Grishin, N.V.3    Phillips, M.A.4
  • 34
    • 0025844980 scopus 로고
    • Molecular features necessary for the uptake of diamines and related compounds by the polyamine receptor of rat lung slices
    • O'Sullivan, M. C., Golding, B. T., Smith, L. L., and Wyatt, I. 1991. Molecular features necessary for the uptake of diamines and related compounds by the polyamine receptor of rat lung slices. Biochemical Pharmacology 41, 1839-1848.
    • (1991) Biochemical Pharmacology , vol.41 , pp. 1839-1848
    • O'Sullivan, M.C.1    Golding, B.T.2    Smith, L.L.3    Wyatt, I.4
  • 35
    • 0028071986 scopus 로고
    • Ornithine decarboxylase: Structure, function and translational regulation
    • Pegg, A. E., Shantz, L. M., and Coleman, C. S. 1994. Ornithine decarboxylase: structure, function and translational regulation. Biochemical Society Transactions 22, 846-852.
    • (1994) Biochemical Society Transactions , vol.22 , pp. 846-852
    • Pegg, A.E.1    Shantz, L.M.2    Coleman, C.S.3
  • 36
    • 0024205515 scopus 로고
    • Trypanosoma brucei ornithine decarboxylase: Enzyme purification, characterization and expression in Escherichia coli
    • Phillips, M. A., Coffino, P., and Wang, C. C. 1988. Trypanosoma brucei ornithine decarboxylase: enzyme purification, characterization and expression in Escherichia coli. Journal of Biological Chemistry 263, 17933-17941.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 17933-17941
    • Phillips, M.A.1    Coffino, P.2    Wang, C.C.3
  • 37
    • 0026599430 scopus 로고
    • Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by α-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites
    • Poulin, R., Lu, L., Ackermann, B., Bey, P., and Pegg, A. E. 1992. Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by α-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites. Journal of Biological Chemistry 267, 150-158.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 150-158
    • Poulin, R.1    Lu, L.2    Ackermann, B.3    Bey, P.4    Pegg, A.E.5
  • 38
    • 0023908603 scopus 로고
    • Ascaris suum and Onchocerca volvulus: S-adenosylmethionine decarboxylase
    • Rathaur, S., Wittich, R. M., and Walter, R. D. 1988. Ascaris suum and Onchocerca volvulus: S-adenosylmethionine decarboxylase. Experimental Parasitology 65, 277-281.
    • (1988) Experimental Parasitology , vol.65 , pp. 277-281
    • Rathaur, S.1    Wittich, R.M.2    Walter, R.D.3
  • 40
    • 0025708397 scopus 로고
    • Characterization of a high-affinity membrane-associated ornithine decarboxylase from the free-living nematode Caenorhabditis elegans
    • Schaeffer, J. M., and Donatelli, M. R. 1990. Characterization of a high-affinity membrane-associated ornithine decarboxylase from the free-living nematode Caenorhabditis elegans. Biochemical Journal 270, 599-604.
    • (1990) Biochemical Journal , vol.270 , pp. 599-604
    • Schaeffer, J.M.1    Donatelli, M.R.2
  • 41
    • 0026040908 scopus 로고
    • Pharmacological properties of the natural polyamines and their depletion by biosynthesis inhibitors as a therapeutic approach
    • Seiler, N. 1991. Pharmacological properties of the natural polyamines and their depletion by biosynthesis inhibitors as a therapeutic approach. Progress in Drug Research 37, 107-159.
    • (1991) Progress in Drug Research , vol.37 , pp. 107-159
    • Seiler, N.1
  • 44
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Skorski, R. S., and Hieter, P. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Skorski, R.S.1    Hieter, P.2
  • 45
    • 0019969556 scopus 로고
    • An ornithine decarboxylase-deficient mutant of Chinese hamster ovary cells
    • Steglich, C., and Scheffler, I. E. 1982. An ornithine decarboxylase-deficient mutant of Chinese hamster ovary cells. Journal of Biological Chemistry 257, 4603-4609.
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 4603-4609
    • Steglich, C.1    Scheffler, I.E.2
  • 47
    • 0019521962 scopus 로고
    • Streptomycin resistance (rpsL) produces an absolute requirement for polyamines for growth of an Eschericia coli strain unable to synthesize putrescine and spermidine [Δ(speA-speB) ΔspeC]
    • Tabor, H., Tabor, C. W., Cohn, M. A., and Hafner, E. W. 1981. Streptomycin resistance (rpsL) produces an absolute requirement for polyamines for growth of an Eschericia coli strain unable to synthesize putrescine and spermidine [Δ(speA-speB) ΔspeC]. Journal of Bacteriology 147, 702-704.
    • (1981) Journal of Bacteriology , vol.147 , pp. 702-704
    • Tabor, H.1    Tabor, C.W.2    Cohn, M.A.3    Hafner, E.W.4
  • 48
    • 0020651442 scopus 로고
    • Ornithine decarboxylase (Saccharomyces cerevisiae)
    • Tyagi, A. K., Tabor, C. W., and Tabor, H. 1983. Ornithine decarboxylase (Saccharomyces cerevisiae). Methods in Enzymology 94, 135-154.
    • (1983) Methods in Enzymology , vol.94 , pp. 135-154
    • Tyagi, A.K.1    Tabor, C.W.2    Tabor, H.3
  • 49
    • 0029039938 scopus 로고
    • Molecular cloning and characterization of ornithine decarboxylase cDNA of the nematode Panagrellus redivivus
    • von Besser, H., Niemann, G., Domdey, B., and Walter, R. D. 1995. Molecular cloning and characterization of ornithine decarboxylase cDNA of the nematode Panagrellus redivivus. Biochemical Journal 308, 635-640.
    • (1995) Biochemical Journal , vol.308 , pp. 635-640
    • Von Besser, H.1    Niemann, G.2    Domdey, B.3    Walter, R.D.4
  • 50
    • 0023836459 scopus 로고
    • Polyamine metabolism of filarial and allied parasites
    • Walter, R. D. 1988. Polyamine metabolism of filarial and allied parasites. Parasitology Today 4, 18-20.
    • (1988) Parasitology Today , vol.4 , pp. 18-20
    • Walter, R.D.1
  • 52
    • 0025517678 scopus 로고
    • Ornithine decarboxylase in Saccharomyces cerevisiae: Chromosomal assignment and genetic mapping of the SPE1 gene
    • Xie, Q-W., Tabor, C. W., and Tabor, H. 1990. Ornithine decarboxylase in Saccharomyces cerevisiae: chromosomal assignment and genetic mapping of the SPE1 gene. Yeast 6, 455-460.
    • (1990) Yeast , vol.6 , pp. 455-460
    • Xie, Q.-W.1    Tabor, C.W.2    Tabor, H.3
  • 53
    • 0026740472 scopus 로고
    • Inhibition of Trichomonas vaginalis ornithine decarboxylase by amino acid analogs
    • Yarlett, N., Goldberg, B., Moharrami, M. A., and Bacchi, C. J. 1992. Inhibition of Trichomonas vaginalis ornithine decarboxylase by amino acid analogs. Biochemical Pharmacology 44, 243-250.
    • (1992) Biochemical Pharmacology , vol.44 , pp. 243-250
    • Yarlett, N.1    Goldberg, B.2    Moharrami, M.A.3    Bacchi, C.J.4
  • 54
    • 0021710272 scopus 로고
    • Use of lacZ fusions to delimit regulatory elements of the inducible divergent GAL1-GAL10 promoter in Saccharomyces cerevisiae
    • Yocum, R. R., Hanley, S., West, R. Jr., and Ptashne, M. 1984. Use of lacZ fusions to delimit regulatory elements of the inducible divergent GAL1-GAL10 promoter in Saccharomyces cerevisiae. Molecular and Cellular Biology 4, 1985-1998.
    • (1984) Molecular and Cellular Biology , vol.4 , pp. 1985-1998
    • Yocum, R.R.1    Hanley, S.2    West R., Jr.3    Ptashne, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.