메뉴 건너뛰기




Volumn 17, Issue 5, 2001, Pages 242-249

Targeting polyamines of parasitic protozoa in chemotherapy

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMALARIAL AGENT; ANTITRYPANOSOMAL AGENT; PENTAMIDINE; POLYAMINE;

EID: 0035017334     PISSN: 14714922     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1471-4922(01)01908-0     Document Type: Review
Times cited : (130)

References (61)
  • 1
  • 2
    • 0034146546 scopus 로고    scopus 로고
    • Population pharmacokinetics/toxicodynamics (PK/TD) relationship of SAM486A in phase I studies in patients with advanced cancers
    • (2000) J. Clin. Pharmacol. , vol.40 , pp. 275-283
    • Zhou, H.1
  • 7
    • 0001054364 scopus 로고
    • Clinical aspects of inhibition of ornithine decarboxylase with emphasis on therapeutic trials of eflornithine (DFMO) in cancer and protozoan diseases
    • McCann P.P., et al. (Eds.), Inhibition of Polyamine Metabolism. Biological Significance and Basis for New Therapies, Academic Press
    • (1987) , pp. 345-364
    • Schechter, P.J.1
  • 8
    • 0020413932 scopus 로고
    • Measurement of the number of ornithine decarboxylase molecules in rat and mouse tissues under various physiological conditions by binding of radiolabelled α-difluoromethylornithine
    • (1982) Biochem J. , vol.206 , pp. 311-318
    • Seely, J.E.1
  • 9
    • 0033117817 scopus 로고    scopus 로고
    • Kinetics of S-adenosylmethionine cellular transport and protein methylation in T. brucei brucei and T. brucei rhodesiense
    • (1999) Arch. Biochem. Biophys. , vol.364 , pp. 13-18
    • Goldberg, B.1
  • 10
    • 0002486260 scopus 로고    scopus 로고
    • Polyamine metabolism in trypanosomes
    • Hide G., et al. (Eds.), Trypanosomiasis and Leishmaniasis, CAB International
    • (1997) , pp. 149-161
    • Fairlamb, A.H.1    LeQuesne, S.A.2
  • 11
    • 0023219692 scopus 로고
    • Cloning and sequencing of the ornithine decarboxylase gene from T. brucei. Implications for enzyme turnover and selective difluoromethylornithine inhibition
    • (1987) J. Biol. Chem. , vol.262 , pp. 8721-8727
    • Phillips, M.A.1
  • 12
    • 0025282471 scopus 로고
    • Trypanosome ornithine decarboxylase is stable because it lacks sequences found in the carboxyl terminus of the mouse enzyme which target the latter for intracellular degradation
    • (1990) J. Biol. Chem. , vol.265 , pp. 11823-11826
    • Ghoda, L.1
  • 13
    • 0026803049 scopus 로고
    • Amplification and molecular cloning of the ornithine decarboxylase gene of Leishmania donovani
    • (1992) J. Biol. Chem. , vol.267 , pp. 2350-2359
    • Hanson, S.1
  • 14
    • 0026685057 scopus 로고
    • Structural elements of ornithine decarboxylase required for intracellular degradation and polyamine-dependent regulation
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2178-2185
    • Ghoda, L.1
  • 16
    • 0031035013 scopus 로고    scopus 로고
    • Cloning of a trypanosomatid gene coding for an ornithine decarboxylase that is metabolically unstable even though it lacks the C-terminal degradation domain
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 397-402
    • Svensson, F.1
  • 17
    • 0033525089 scopus 로고    scopus 로고
    • Ornithine decarboxylase gene deletion mutants of Leishmania donovani
    • (1999) J. Biol. Chem. , vol.274 , pp. 3781-3788
    • Jiang, Y.1
  • 19
    • 0026842163 scopus 로고
    • Biochemical evidence for the presence of arginine decarboxylase activity in Trypanosoma cruzi
    • (1992) J. Parasitol. , vol.78 , pp. 371-374
    • Majumder, S.1
  • 22
    • 0032143330 scopus 로고    scopus 로고
    • Trypanosoma cruzi has not lost its S-adenosylmethionine decarboxylase: characterization of the gene and the encoded enzyme
    • (1998) Biochem. J. , vol.333 , pp. 527-537
    • Persson, K.1
  • 23
    • 0033049344 scopus 로고    scopus 로고
    • Trypanosoma cruzi epimastigotes lack ornithine decarboxylase but can express a foreign gene encoding this enzyme
    • (1999) FEBS Lett. , vol.454 , pp. 192-196
    • Carrillo, C.1
  • 24
    • 0034642522 scopus 로고    scopus 로고
    • Uptake of apoptotic cells drives the growth of a pathogenic trypanosome in macrophages
    • (2000) Nature , vol.403 , pp. 199-203
    • Freire-de-Lima, G.C.1
  • 26
    • 0021063774 scopus 로고
    • Plasmodium berghei: Inhibition of the sporogonous cycle by α-difluoromethylornithine
    • (1983) Exp. Parasitol. , vol.56 , pp. 190-193
    • Gillet, J.M.1
  • 28
  • 29
    • 0023433861 scopus 로고
    • Plasmodium falciparum and Plasmodium berghei: Effects of ornithine decarboxylase inhibitors on erythrocytic schizogony
    • (1987) Exp. Parasitol. , vol.64 , pp. 237-243
    • Bitonti, A.J.1
  • 30
    • 0039765384 scopus 로고    scopus 로고
    • In the human malaria parasite Plasmodium falciparum, polyamines are synthesized by a bifunctional ornithine decarboxylase, S-adenosylmethionine decarboxylase
    • (2000) J. Biol. Chem. , vol.275 , pp. 8097-8102
    • Müller, S.1
  • 31
    • 0034534695 scopus 로고    scopus 로고
    • The ornithine decarboxylase domain of the bifunctional ornithine decarboxylase/S-adenosylmethionine decarboxylase of Plasmodium falciparum: Recombinant expression and catalytic properties of two different constructs
    • (2000) Biochem. J. , vol.352 , pp. 287-292
    • Krause, T.1
  • 33
    • 0033533601 scopus 로고    scopus 로고
    • Lysine-69 plays a key role in catalysis by ornithine decarboxylase through acceleration of the Schiff base formation, decarboxylation, and product release steps
    • (1999) Biochemistry , vol.38 , pp. 11814-11826
    • Osterman, A.L.1
  • 34
    • 0033576286 scopus 로고    scopus 로고
    • X-ray structure of ornithine decarboxylase from T. brucei: the native structure and the structure in complex with α-difluoromethylornithine
    • (1999) Biochemistry , vol.38 , pp. 15174-15184
    • Grishin, N.V.1
  • 35
    • 0034614359 scopus 로고    scopus 로고
    • Crystal structure of human ornithine decarboxylase at 2.1 Å resolution: structural insights to antizyme binding
    • (2000) J. Mol. Biol. , vol.295 , pp. 7-16
    • Almrud, J.J.1
  • 36
    • 0021989464 scopus 로고
    • Catalytic irreversible inhibition of Trypanosoma brucei brucei ornithine decarboxylase by substrate and product analogs and their effects on murine trypanosomiasis
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 1773-1777
    • Bitonti, A.J.1
  • 37
    • 0023134509 scopus 로고
    • Effects of the ornithine decarboxylase inhibitors dl-α-difluoromethylornithine and α-monofluoromethyldehydroornithine methyl ester alone and in combination with suramin against Trypanosoma brucei brucei central nervous system models
    • (1987) Am J. Trop. Med. Hyg. , vol.36 , pp. 46-52
    • Bacchi, C.J.1
  • 38
    • 0033134691 scopus 로고    scopus 로고
    • The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 Å resolution reveals a novel fold
    • (1999) Structure Fold. Des. , vol.7 , pp. 583-595
    • Ekstrom, J.L.1
  • 39
    • 0033591757 scopus 로고    scopus 로고
    • Synthesis of spermidine and norspermidine dimers as high affinity polyamine transport inhibitors
    • (1999) Bioorg. Med. Chem. , vol.9 , pp. 1709-1714
    • Covassin, L.1
  • 42
    • 0023125604 scopus 로고
    • Effect of polyamine depletion on macromolecular synthesis of the malarial parasite, Plasmodium falciparum, cultured in human erythrocytes
    • (1987) Biochem. J. , vol.242 , pp. 221-226
    • Assaraf, Y.G.1
  • 44
    • 0004930356 scopus 로고
    • Arginine uptake by mouse erythrocytes infected with Plasmodium yoelii nigeriensis
    • (1995) J. Parasitic Dis. , vol.19 , pp. 55-58
    • Mishra, M.1
  • 45
    • 0030985218 scopus 로고    scopus 로고
    • Characterization of simian malarial parasite (Plasmodium knowlesi)-induced putrescine transport in rhesus monkey erythrocytes. A novel putrescine conjugate arrests in vitro growth of simian malarial parasite (Plasmodium knowlesi) and cures multidrug resistant murine malaria (Plasmodium yoelii) infection in vivo
    • (1997) J. Biol. Chem. , vol.272 , pp. 13506-13511
    • Singh, S.1
  • 46
    • 0026740249 scopus 로고
    • 2-Substituted 3-(aminooxy)propanamines as inhibitors of ornithine decarboxylase. Synthesis and biological activity
    • (1992) J. Med. Chem. , vol.35 , pp. 1339-1344
    • Stanek, J.1
  • 48
    • 0004978232 scopus 로고    scopus 로고
    • Brun, R. et al. The story of CGP 40215: Studies on the efficacy and pharmacokinetics in the African green monkey model. Trop. Med. Int. Health (in press)
  • 50
    • 0033977079 scopus 로고    scopus 로고
    • Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress
    • (2000) Mol. Microbiol. , vol.35 , pp. 542-552
    • Krieger, S.1
  • 52
    • 0031854156 scopus 로고    scopus 로고
    • Evidence that trypanothione reductase is an essential enzyme in Leishmania by targeted replacement of the tyrA gene locus
    • (1998) Mol. Microbiol. , vol.29 , pp. 653-660
    • Tovar, J.1
  • 53
    • 0345035516 scopus 로고    scopus 로고
    • Nitrofuran drugs as common subversive substrates of Trypanosoma cruzi lipoamide dehydrogenase and trypanothione reductase
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 1791-1799
    • Blumenstiel, K.1
  • 54
    • 0034599953 scopus 로고    scopus 로고
    • Parallel synthesis of a library of 1,4-naphthoquinones and automated screening of potential inhibitors of trypanothione reductase from Trypanosoma cruzi
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 631-635
    • Salmon-Chemin, L.1
  • 55
    • 0030838722 scopus 로고    scopus 로고
    • New spermine and spermidine derivatives as potent inhibitors of Trypanosoma cruzi trypanothione reductase
    • (1997) Biorg. Med. Chem. , vol.5 , pp. 1249-1256
    • Bonnet, B.1
  • 56
    • 0034101748 scopus 로고    scopus 로고
    • Trypanothione reductase inhibition/trypanocidal activity relationships in a 1,4-bis(3-aminopropyl)piperazine series
    • (2000) Biorg. Med. Chem. , vol.8 , pp. 95-103
    • Bonnet, B.1
  • 57
    • 0029731341 scopus 로고    scopus 로고
    • Bis(7-amino-4-azaheptyl) dimethylsilane and bis(7-ethylamino-4-azaheptyl)dimethylsilane: inhibition of tumor cell growth in vitro and in vivo
    • (1996) Cancer Res. , vol.56 , pp. 5624-5630
    • Seiler, N.1
  • 58
  • 59
    • 0000731846 scopus 로고
    • Bis(benzyl)polyamine analogs inhibit the growth of chloroquine-resistant human malaria parasites (Plasmodium falciparum) in vitro and in combination with α-difluoromethylornithine cure murine malaria
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 651-655
    • Bitonti, A.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.