메뉴 건너뛰기




Volumn 38, Issue 2, 2010, Pages 645-651

Polyamine metabolism in Trypanosoma cruzi: Studies on the expression and regulation of heterologous genes involved in polyamine biosynthesis

Author keywords

DFMO resistance; Gene expression; Polyamine auxotrophy; Post translational processing; Transgenic parasites; Trypanosoma cruzi

Indexed keywords

ARGININE DECARBOXYLASE; EFLORNITHINE; GENOMIC DNA; MESSENGER RNA; ORNITHINE DECARBOXYLASE; POLYAMINE; PROTOZOAL PROTEIN;

EID: 77953064754     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-009-0425-6     Document Type: Conference Paper
Times cited : (18)

References (53)
  • 1
    • 0141734184 scopus 로고
    • Polyamines in Tripanosoma cruzi and Leishmania mexicana
    • Goldemberg SH, Algranati ID eds, Oxford University Press, Oxford
    • Algranati ID, Sánchez C, González NS (1990) Polyamines in Tripanosoma cruzi and Leishmania mexicana. In: Goldemberg SH, Algranati ID (eds) The biology and chemistry of polyamines. Oxford University Press, Oxford, pp 137-146
    • (1990) The Biology and Chemistry of Polyamines , pp. 137-146
    • Algranati, I.D.1    Sánchez, C.2    González, N.S.3
  • 2
    • 0031057528 scopus 로고    scopus 로고
    • Diamine auxotrophy may be a universal feature of Trypanosoma cruzi epimastigotes
    • Ariyanayagam MR, Fairlamb AH (1997) Diamine auxotrophy may be a universal feature of Trypanosoma cruzi epimastigotes. Mol Biochem Parasitol 84:111-121
    • (1997) Mol. Biochem. Parasitol. , vol.84 , pp. 111-121
    • Ariyanayagam, M.R.1    Fairlamb, A.H.2
  • 3
    • 0016207796 scopus 로고
    • Unsubstituted agarose as an affinity matrix for isolation of NAD-dependent alpha-glycerophosphate dehydrogenase from the trypanosomatid Crithidia fasciculate
    • Bacchi CJ, Marcus SL, Lambros C, Goldberg B, Messina L, Hutner SH (1974) Unsubstituted agarose as an affinity matrix for isolation of NAD-dependent alpha-glycerophosphate dehydrogenase from the trypanosomatid Crithidia fasciculate. Biochem Biophys Res Commun 58:778-786
    • (1974) Biochem. Biophys. Res. Commun. , vol.58 , pp. 778-786
    • Bacchi, C.J.1    Marcus, S.L.2    Lambros, C.3    Goldberg, B.4    Messina, L.5    Hutner, S.H.6
  • 5
    • 0025616156 scopus 로고
    • Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing
    • Bell E, Malmberg RL (1990) Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing. Mol Gen Genet 224:431-436
    • (1990) Mol. Gen. Genet. , vol.224 , pp. 431-436
    • Bell, E.1    Malmberg, R.L.2
  • 6
    • 0028822932 scopus 로고
    • New mechanisms of drug resistance in parasitic protozoa
    • Borst P, Ouellette M (1995) New mechanisms of drug resistance in parasitic protozoa. Annu Rev Microbiol 49:427-460
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 427-460
    • Borst, P.1    Ouellette, M.2
  • 7
    • 0033049344 scopus 로고    scopus 로고
    • Trypanosoma cruzi epimastigotes lack ornithine decarboxylase but can express a foreign gene encoding this enzyme
    • Carrillo C, Cejas S, González NS, Algranati ID (1999) Trypanosoma cruzi epimastigotes lack ornithine decarboxylase but can express a foreign gene encoding this enzyme. FEBS Lett 454:192-196
    • (1999) FEBS Lett. , vol.454 , pp. 192-196
    • Carrillo, C.1    Cejas, S.2    González, N.S.3    Algranati, I.D.4
  • 10
    • 33646484364 scopus 로고    scopus 로고
    • Molecular and functional characterization of a spermidine transporter (TcPAT12) from Trypanosoma cruzi
    • Carrillo C, Cánepa GE, Algranati ID, Pereira CA (2006) Molecular and functional characterization of a spermidine transporter (TcPAT12) from Trypanosoma cruzi. Biochem Biophys Res Común 344:936-940
    • (2006) Biochem. Biophys. Res. Común , vol.344 , pp. 936-940
    • Carrillo, C.1    Cánepa, G.E.2    Algranati, I.D.3    Pereira, C.A.4
  • 11
    • 35448955196 scopus 로고    scopus 로고
    • Tripanosoma cruzi as a model system to study the expression of exogenous genes coding for polyamine biosynthetic enzymes. Induction of DFMO resistance in transgenic parasites
    • Carrillo C, González NS, Algranati ID (2007) Tripanosoma cruzi as a model system to study the expression of exogenous genes coding for polyamine biosynthetic enzymes. Induction of DFMO resistance in transgenic parasites. Biochim Biophys Acta 1770:1605-1611
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 1605-1611
    • Carrillo, C.1    González, N.S.2    Algranati, I.D.3
  • 13
    • 0037090528 scopus 로고    scopus 로고
    • Life without transcriptional control? From fly to man and back again
    • Clayton CE (2002) Life without transcriptional control? From fly to man and back again. EMBO J 21:1881-1888
    • (2002) EMBO J. , vol.21 , pp. 1881-1888
    • Clayton, C.E.1
  • 14
    • 77956392108 scopus 로고    scopus 로고
    • Biosynthesis and metabolism of diamines in bacteria
    • Cohen SS ed, Oxford University Press, Oxford
    • Cohen SS (1998) Biosynthesis and metabolism of diamines in bacteria. In: Cohen SS (ed) A guide to the polyamines. Oxford University Press, Oxford, pp 122-141
    • (1998) A Guide to the Polyamines , pp. 122-141
    • Cohen, S.S.1
  • 16
    • 0024497978 scopus 로고
    • The enzymes of the classical pentose phosphate pathway display differential activities in procyclic and bloodstream forms of Trypanosoma brucei
    • Cronin CN, Nolan DP, Voorheis HP (1989) The enzymes of the classical pentose phosphate pathway display differential activities in procyclic and bloodstream forms of Trypanosoma brucei. FEBS Lett 244:26-30
    • (1989) FEBS Lett. , vol.244 , pp. 26-30
    • Cronin, C.N.1    Nolan, D.P.2    Voorheis, H.P.3
  • 17
    • 0024342966 scopus 로고
    • Novel biochemical pathways in parasitic protozoa
    • Fairlamb AH (1989) Novel biochemical pathways in parasitic protozoa. Parasitology 99: S93-S112
    • (1989) Parasitology , vol.99
    • Fairlamb, A.H.1
  • 18
    • 0037192115 scopus 로고    scopus 로고
    • Metabolic pathway analysis in trypanosomes and malaria parasites
    • Fairlamb AH (2002) Metabolic pathway analysis in trypanosomes and malaria parasites. Phil Trans R Soc Lond B 357:101-107
    • (2002) Phil. Trans. R Soc. Lond. B. , vol.357 , pp. 101-107
    • Fairlamb, A.H.1
  • 19
    • 0021933665 scopus 로고
    • Identification of a novel, thiolcontaining cofactor essential for glutathione reductase enzyme activity in trypanosomatids
    • Fairlamb AH, Cerami A (1985) Identification of a novel, thiolcontaining cofactor essential for glutathione reductase enzyme activity in trypanosomatids. Mol Biochem Parasitol 14:187-198
    • (1985) Mol. Biochem. Parasitol. , vol.14 , pp. 187-198
    • Fairlamb, A.H.1    Cerami, A.2
  • 20
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the kinetoplastida
    • Fairlamb AH, Cerami A (1992) Metabolism and functions of trypanothione in the kinetoplastida. Annu Rev Microbiol 46:695-729
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 21
    • 0022002912 scopus 로고
    • Tripanothione: A novel bis (glutathionyl) spermidine cofactor for glutathione reductase in trypanosomatids
    • Fairlamb AH, Blackburn P, Ulrich P, Chait BT, Cerami A (1985) Tripanothione: a novel bis (glutathionyl) spermidine cofactor for glutathione reductase in trypanosomatids. Science 227:1485-1487
    • (1985) Science , vol.227 , pp. 1485-1487
    • Fairlamb, A.H.1    Blackburn, P.2    Ulrich, P.3    Chait, B.T.4    Cerami, A.5
  • 22
    • 0026451048 scopus 로고
    • Differential regulation of putrescine uptake in Trypanosoma cruzi and other tripanosomatids
    • González NS, Ceriani C, Algranati ID (1992) Differential regulation of putrescine uptake in Trypanosoma cruzi and other tripanosomatids. Biochem Biophys Res Commun 188:120-128
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 120-128
    • González, N.S.1    Ceriani, C.2    Algranati, I.D.3
  • 24
    • 0035941059 scopus 로고    scopus 로고
    • Spermidine is essential for normal proliferation of trypanosomatid protozoa
    • González NS, Huber A, Algranati ID (2001) Spermidine is essential for normal proliferation of trypanosomatid protozoa. FEBS Lett 508:323-326
    • (2001) FEBS Lett. , vol.508 , pp. 323-326
    • González, N.S.1    Huber, A.2    Algranati, I.D.3
  • 25
    • 0034798209 scopus 로고    scopus 로고
    • Arabidopsis polyamine biosynthesis: Absence of ornithine decarboxylase and the mechanism of arginine decarboxylase activity
    • Hanfrey C, Sommer S, Mayer MJ, Burtin D, Michael AJ (2001) Arabidopsis polyamine biosynthesis: absence of ornithine decarboxylase and the mechanism of arginine decarboxylase activity. Plant J 27:551-560
    • (2001) Plant. J. , vol.27 , pp. 551-560
    • Hanfrey, C.1    Sommer, S.2    Mayer, M.J.3    Burtin, D.4    Michael, A.J.5
  • 26
    • 0019808002 scopus 로고
    • Role of the polyamines in germ cell differentiation and in early embryonic development
    • Heby O, Emanuelsson H (1981) Role of the polyamines in germ cell differentiation and in early embryonic development. Med Biol 59:417-422
    • (1981) Med. Biol. , vol.59 , pp. 417-422
    • Heby, O.1    Emanuelsson, H.2
  • 27
    • 34547654456 scopus 로고    scopus 로고
    • Targeting the polyamine biosynthetic enzymes: A promising approach to therapy of African sleeping sickness, Chagas' disease and Leishmaniasis
    • Heby O, Persson L, Rentala M (2007) Targeting the polyamine biosynthetic enzymes: a promising approach to therapy of African sleeping sickness, Chagas' disease and Leishmaniasis. Amino Acids 33:359-366
    • (2007) Amino Acids , vol.33 , pp. 359-366
    • Heby, O.1    Persson, L.2    Rentala, M.3
  • 28
    • 0033146548 scopus 로고    scopus 로고
    • Arginine decarboxylase in Trypanosoma cruzi. Characteristics and kinetic properties
    • Hernández S, Schwarcs de Tarlovsky M (1999) Arginine decarboxylase in Trypanosoma cruzi. Characteristics and kinetic properties. Cell Mol Biol 45:383-391
    • (1999) Cell. Mol. Biol. , vol.45 , pp. 383-391
    • Hernández, S.1    Schwarcs De Tarlovsky, S.M.2
  • 29
    • 34547671110 scopus 로고    scopus 로고
    • Ubiquitin dependent and independent protein degradation in the regulation of cellular polyamines
    • Kahana C (2007) Ubiquitin dependent and independent protein degradation in the regulation of cellular polyamines. Amino Acids 33:225-230
    • (2007) Amino Acids , vol.33 , pp. 225-230
    • Kahana, C.1
  • 30
    • 0026673614 scopus 로고
    • A shuttle vector which facilitates the expression of transfected genes in Trypanosoma cruzi and Leishmania
    • Kelly JM, Ward HM, Miles MA, Kendall G (1992) A shuttle vector which facilitates the expression of transfected genes in Trypanosoma cruzi and Leishmania. Nucleic Acids Res 20:3963-3969
    • (1992) Nucleic. Acids Res. , vol.20 , pp. 3963-3969
    • Kelly, J.M.1    Ward, H.M.2    Miles, M.A.3    Kendall, G.4
  • 31
    • 0011740954 scopus 로고
    • Arginine decarboxylase inhibitors reduce the capacity of Trypanosoma cruzi to infect and multiply in mammalian host cells
    • Kierszenbaum F, Wirth JJ, McCann PP, Sjoerdsma A (1987) Arginine decarboxylase inhibitors reduce the capacity of Trypanosoma cruzi to infect and multiply in mammalian host cells. Proc Natl Acad Sci USA 84:4278-4282
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4278-4282
    • Kierszenbaum, F.1    Wirth, J.J.2    McCann, P.P.3    Sjoerdsma, A.4
  • 33
    • 0142105416 scopus 로고    scopus 로고
    • Novel roles for the flagellum in cell morphogenesis and cytokinesis of trypanosomes
    • Kohl L, Robinson D, Bastin P (2003) Novel roles for the flagellum in cell morphogenesis and cytokinesis of trypanosomes. EMBO J 22:5336-5346
    • (2003) EMBO J. , vol.22 , pp. 5336-5346
    • Kohl, L.1    Robinson, D.2    Bastin, P.3
  • 34
    • 0026842163 scopus 로고
    • Biochemical evidence for the presence of arginine decarboxylase activity in Trypanosoma cruzi
    • Majunder S, Wirth JJ, Bitonti AJ, McCann PP, Kierszenbaum F (1992) Biochemical evidence for the presence of arginine decarboxylase activity in Trypanosoma cruzi. J Parasitol 78:371-374
    • (1992) J. Parasitol. , vol.78 , pp. 371-374
    • Majunder, S.1    Wirth, J.J.2    Bitonti, A.J.3    McCann, P.P.4    Kierszenbaum, F.5
  • 35
    • 0028101319 scopus 로고
    • Arginine decarboxylase of oats is activated by enzymatic cleavage into two polypeptides
    • Malmberg RL, Cellino ML (1994) Arginine decarboxylase of oats is activated by enzymatic cleavage into two polypeptides. J Biol Chem 269:2703-2706
    • (1994) J. Biol. Chem. , vol.269 , pp. 2703-2706
    • Malmberg, R.L.1    Cellino, M.L.2
  • 36
    • 0020620209 scopus 로고
    • Pyrazolopyrimidine metabolism in the pathogenic trypanosomatidae
    • Marr JJ, Berens RL (1983) Pyrazolopyrimidine metabolism in the pathogenic trypanosomatidae. Mol Biochem Parasitol 7:339-356
    • (1983) Mol. Biochem. Parasitol. , vol.7 , pp. 339-356
    • Marr, J.J.1    Berens, R.L.2
  • 37
    • 0343416375 scopus 로고    scopus 로고
    • PRIBOTEX expresión vector: A pTEX derivative for rapid selection of Tripanosoma cruzi transfectants
    • Martínez Calvillo S, López I, Hernández R (1997) pRIBOTEX expresión vector: a pTEX derivative for rapid selection of Tripanosoma cruzi transfectants. Gene 199:71-76
    • (1997) Gene , vol.199 , pp. 71-76
    • Calvillo, S.M.1    López, I.2    Hernández, R.3
  • 38
    • 0035017334 scopus 로고    scopus 로고
    • Targeting polyamines of parasitic protozoa in chemotherapy
    • Müller S, Coombs GH, Walter RD (2001) Targeting polyamines of parasitic protozoa in chemotherapy. Trends Parasitol 17:242-249
    • (2001) Trends Parasitol. , vol.17 , pp. 242-249
    • Müller, S.1    Coombs, G.H.2    Walter, R.D.3
  • 39
    • 33947221526 scopus 로고    scopus 로고
    • Metabolism of Leishmania; proven and predicted
    • Opperdoes FR, Coombs GH (2007) Metabolism of Leishmania; proven and predicted. Trends Parasitol 23:149-158
    • (2007) Trends Parasitol. , vol.23 , pp. 149-158
    • Opperdoes, F.R.1    Coombs, G.H.2
  • 40
    • 0035339822 scopus 로고    scopus 로고
    • Enzymes of carbohydrate metabolism as potential drug targets
    • Opperdoes FR, Michels PA (2001) Enzymes of carbohydrate metabolism as potential drug targets. Int J Parasitol 31:482-490
    • (2001) Int. J. Parasitol. , vol.31 , pp. 482-490
    • Opperdoes, F.R.1    Michels, P.A.2
  • 42
    • 0023881236 scopus 로고
    • Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy
    • Pegg AE (1988) Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy. Cancer Res 48:759-774
    • (1988) Cancer Res. , vol.48 , pp. 759-774
    • Pegg, A.E.1
  • 43
    • 33644940174 scopus 로고    scopus 로고
    • Modulation of oat arginine decarboxylase gene expression and genome organization in transgenic Trypanosoma cruzi epimastigotes
    • Serra MP, Carrillo C, González NS, Algranati ID (2006) Modulation of oat arginine decarboxylase gene expression and genome organization in transgenic Trypanosoma cruzi epimastigotes. FEBS J 273:628-637
    • (2006) FEBS J. , vol.273 , pp. 628-637
    • Serra, M.P.1    Carrillo, C.2    González, N.S.3    Algranati, I.D.4
  • 44
    • 67349162534 scopus 로고    scopus 로고
    • Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes
    • Serra MP, Senn A, Algranati ID (2009) Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes. Exp Parasitol 122:169-176
    • (2009) Exp. Parasitol. , vol.122 , pp. 169-176
    • Serra, M.P.1    Senn, A.2    Algranati, I.D.3
  • 45
    • 0005656365 scopus 로고
    • The oxidative decarboxylation of ornithine by extracts of higher plants
    • Smith TA, Marshall J H A (1988) The oxidative decarboxylation of ornithine by extracts of higher plants. Phytochemistry 27:710-793
    • (1988) Phytochemistry , vol.27 , pp. 710-793
    • Smith, T.A.1    Marshall, J.H.A.2
  • 46
    • 33645580051 scopus 로고    scopus 로고
    • The ornithine decarboxylase gene of Trypanosoma brucei: Evidence for horizontal gene transfer from a vertebrate source
    • Steglich C, Schaeffer SW (2006) The ornithine decarboxylase gene of Trypanosoma brucei: evidence for horizontal gene transfer from a vertebrate source. Infect Genet Evolut 6:205-219
    • (2006) Infect. Genet. Evolut , vol.6 , pp. 205-219
    • Steglich, C.1    Schaeffer, S.W.2
  • 47
    • 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
    • Svensson F, Ceriani C, Lövkvist Wallström E, Kockum I, Algranati ID, Heby O, Persson L (1997) Cloning of a trypanosomatid gene coding for an ornithine decarboxylase that is metabolically unstable even though it lacks the C-terminal degradation domain. Proc Natl Acad Sci USA 94:397-402
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 397-402
    • Svensson, F.1    Ceriani, C.2    Wallström, E.L.3    Kockum, I.4    Algranati, I.D.5    Heby, O.6    Persson, L.7
  • 48
    • 0035340990 scopus 로고    scopus 로고
    • The life cycle of Trypanosoma cruzi revisited
    • Tyler KM, Engman DM (2001) The life cycle of Trypanosoma cruzi revisited. Int J Parasitol 31:472-481
    • (2001) Int. J. Parasitol. , vol.31 , pp. 472-481
    • Tyler, K.M.1    Engman, D.M.2
  • 49
    • 0030975596 scopus 로고    scopus 로고
    • Inhibition of the respiratory chain results in a reversible metabolic arrest in Leishmania promastigotes
    • van Hellemond JJ, Tielens AG (1997) Inhibition of the respiratory chain results in a reversible metabolic arrest in Leishmania promastigotes. Mol Biochem Parasitol 85:135-138
    • (1997) Mol. Biochem. Parasitol. , vol.85 , pp. 135-138
    • Van Hellemond, J.J.1    Tielens, A.G.2
  • 50
    • 0021877040 scopus 로고
    • Developmental cycles and biology of pathogenic trypanosomes
    • Vickerman K (1985) Developmental cycles and biology of pathogenic trypanosomes. Br Med Bull 41:105-114
    • (1985) Br. Med. Bull. , vol.41 , pp. 105-114
    • Vickerman, K.1
  • 52
    • 0026729618 scopus 로고
    • DL-α difluoromethy-larginine inhibits intracellular Trypanosoma cruzi multiplication by affecting cell division but not trypomastigote- amastigote transformation
    • Yakubu MA, Basso B, Kierszenbaum F (1992) DL-α difluoromethy- larginine inhibits intracellular Trypanosoma cruzi multiplication by affecting cell division but not trypomastigote-amastigote transformation. J Parasitol 78:414-419
    • (1992) J. Parasitol. , vol.78 , pp. 414-419
    • Yakubu, M.A.1    Basso, B.2    Kierszenbaum, F.3
  • 53
    • 0018252473 scopus 로고
    • Ureotelism and ammonotelism in trypanosomatids
    • Yoshida N, Camargo EP (1978) Ureotelism and ammonotelism in trypanosomatids. J Bacteriol 136:1184-1186
    • (1978) J. Bacteriol. , vol.136 , pp. 1184-1186
    • Yoshida, N.1    Camargo, E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.