메뉴 건너뛰기




Volumn 343, Issue 2, 2006, Pages 443-449

An endosymbiont positively modulates ornithine decarboxylase in host trypanosomatids

Author keywords

Cell growth; Endosymbiotic bacterium; Ornithine decarboxylase; Polyamine metabolism; Symbiotic relationship; Trypanosomatid protozoa

Indexed keywords

ORNITHINE DECARBOXYLASE;

EID: 33645129478     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.02.168     Document Type: Article
Times cited : (17)

References (47)
  • 1
    • 0016119295 scopus 로고
    • Simple nutrition of Crithidia deanei, a reduviid trypanosomatid with an endosymbiont
    • M.H. Mundim, I. Roitman, M.A. Hermans, and E.W. Kitajima Simple nutrition of Crithidia deanei, a reduviid trypanosomatid with an endosymbiont J. Protozool. 21 1974 518 521
    • (1974) J. Protozool. , vol.21 , pp. 518-521
    • Mundim, M.H.1    Roitman, I.2    Hermans, M.A.3    Kitajima, E.W.4
  • 2
    • 0344955809 scopus 로고
    • Nutritional requirements and biosynthetic capabilities of the parasitic flagellates Strigomonas oncopelti
    • B.A. Newton Nutritional requirements and biosynthetic capabilities of the parasitic flagellates Strigomonas oncopelti J. Gen. Microbiol. 17 1957 708 717
    • (1957) J. Gen. Microbiol. , vol.17 , pp. 708-717
    • Newton, B.A.1
  • 3
    • 0015947565 scopus 로고
    • Nutritional significance of symbiotic bacteria in two species of hemoflagellates
    • K.P. Chang, and W. Trager Nutritional significance of symbiotic bacteria in two species of hemoflagellates Science 183 1974 531 532
    • (1974) Science , vol.183 , pp. 531-532
    • Chang, K.P.1    Trager, W.2
  • 7
    • 0016810319 scopus 로고
    • Reduced growth in Blastocrithidia culicis and Crithidia oncopelti freed of intracellular symbiotes by chloramphenicol
    • K.P. Chang Reduced growth in Blastocrithidia culicis and Crithidia oncopelti freed of intracellular symbiotes by chloramphenicol J. Protozool. 22 1975 271 276
    • (1975) J. Protozool. , vol.22 , pp. 271-276
    • Chang, K.P.1
  • 8
    • 0018248345 scopus 로고
    • Trypanosomatid protozoa: Survey of acetylornithinase and ornithine acetyltransferase
    • S. Galinari, and E.P. Camargo Trypanosomatid protozoa: survey of acetylornithinase and ornithine acetyltransferase Exp. Parasitol. 46 1978 277 282
    • (1978) Exp. Parasitol. , vol.46 , pp. 277-282
    • Galinari, S.1    Camargo, E.P.2
  • 9
    • 33645116658 scopus 로고
    • Urea cycle enzymes in wild and aposymbiotic strain of Blastocrithidia culicis
    • S. Galinari, and E.P. Camargo Urea cycle enzymes in wild and aposymbiotic strain of Blastocrithidia culicis J. Parasitol. 65 1979 88
    • (1979) J. Parasitol. , vol.65 , pp. 88
    • Galinari, S.1    Camargo, E.P.2
  • 10
    • 0018252473 scopus 로고
    • Ureotelism and ammonotelism in trypanosomatids
    • N. Yoshida, and E.P. Camargo Ureotelism and ammonotelism in trypanosomatids J. Bacteriol. 136 1978 1184 1186
    • (1978) J. Bacteriol. , vol.136 , pp. 1184-1186
    • Yoshida, N.1    Camargo, E.P.2
  • 11
    • 0017763292 scopus 로고
    • Endosymbiont as supplier of ornithine carbamoyl transferase in trypanosomatids
    • E.P. Camargo, and E. Freymuller Endosymbiont as supplier of ornithine carbamoyl transferase in trypanosomatids Nature 270 1977 52 53
    • (1977) Nature , vol.270 , pp. 52-53
    • Camargo, E.P.1    Freymuller, E.2
  • 12
    • 0025325255 scopus 로고
    • Molecular genetics of polyamine synthesis in eukaryotic cells
    • O. Heby, and L. Persson Molecular genetics of polyamine synthesis in eukaryotic cells Trends Biochem. Sci. 15 1990 153 158
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 153-158
    • Heby, O.1    Persson, L.2
  • 13
    • 0029455991 scopus 로고
    • Ornithine decarboxylase as a target for chemoprevention
    • A.E. Pegg, L.M. Shantz, and C.S. Coleman Ornithine decarboxylase as a target for chemoprevention J. Cell. Biochem. 58 Suppl. 1995 132 138
    • (1995) J. Cell. Biochem. , vol.58 , Issue.SUPPL. , pp. 132-138
    • Pegg, A.E.1    Shantz, L.M.2    Coleman, C.S.3
  • 14
    • 0028799607 scopus 로고
    • Rapid and regulated degradation of ornithine decarboxylase
    • S. Hayashi, and Y. Murakami Rapid and regulated degradation of ornithine decarboxylase Biochem. J. 306 1995 1 10
    • (1995) Biochem. J. , vol.306 , pp. 1-10
    • Hayashi, S.1    Murakami, Y.2
  • 15
    • 0030052923 scopus 로고    scopus 로고
    • Ornithine decarboxylase antizyme: A novel type of regulatory protein
    • S. Hayashi, Y. Murakami, and S. Matsufuji Ornithine decarboxylase antizyme: a novel type of regulatory protein Trends Biochem. Sci. 21 1996 27 30
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 27-30
    • Hayashi, S.1    Murakami, Y.2    Matsufuji, S.3
  • 16
    • 0035291218 scopus 로고    scopus 로고
    • Regulation of cellular polyamines by antizyme
    • P. Coffino Regulation of cellular polyamines by antizyme Nat. Rev. Mol. Cell Biol. 2 2001 188 194
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 188-194
    • Coffino, P.1
  • 17
    • 0022971952 scopus 로고
    • Aminoacid sequences common to rapidly degraded proteins: The PEST hypothesis
    • S. Rogers, R. Wells, and M. Rechsteiner Aminoacid sequences common to rapidly degraded proteins: the PEST hypothesis Science 234 1986 364 368
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 20
    • 0019194217 scopus 로고
    • Polyamine metabolism: A potential therapeutic target in trypanosomes
    • C.J. Bacchi, H.C. Nathan, S.H. Hutner, P.P. McCann, and A. Sjoerdsman Polyamine metabolism: a potential therapeutic target in trypanosomes Science 210 1980 332 334
    • (1980) Science , vol.210 , pp. 332-334
    • Bacchi, C.J.1    Nathan, H.C.2    Hutner, S.H.3    McCann, P.P.4    Sjoerdsman, A.5
  • 21
    • 0022194481 scopus 로고
    • Treatment of gambiense sleeping sickness in the Sudan with oral DFMO, an inhibitor of ornithine decarboxylase: First field trial
    • S. Van Nieuwenhove, P.J. Schechter, J. Declereq, G. Bone, J. Burke, and A. Sjoerdsma Treatment of gambiense sleeping sickness in the Sudan with oral DFMO, an inhibitor of ornithine decarboxylase: first field trial Trans. R. Soc. Trop. Med. Hyg. 79 1985 692 698
    • (1985) Trans. R. Soc. Trop. Med. Hyg. , vol.79 , pp. 692-698
    • Van Nieuwenhove, S.1    Schechter, P.J.2    Declereq, J.3    Bone, G.4    Burke, J.5    Sjoerdsma, A.6
  • 22
    • 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
    • F. Svensson, C. Ceriani, E.L. Wallström, I. Kockum, I.D. Algranati, O. Heby, and L. Persson 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 74 1997 397 402
    • (1997) Proc. Natl. Acad. Sci. USA , vol.74 , 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
  • 23
    • 0026603431 scopus 로고
    • Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation
    • C. Ceriani, N.S. González, and I.D. Algranati Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation FEBS Lett. 301 1992 261 264
    • (1992) FEBS Lett. , vol.301 , pp. 261-264
    • Ceriani, C.1    González, N.S.2    Algranati, I.D.3
  • 24
    • 70449538030 scopus 로고
    • Metabolism of Schizotrypanum cruzi, Chagas. 1. Effect of culture age and substrate concentration on respiratory rate
    • L.G. Warren Metabolism of Schizotrypanum cruzi, Chagas. 1. Effect of culture age and substrate concentration on respiratory rate J. Parasitol. 46 1960 529 539
    • (1960) J. Parasitol. , vol.46 , pp. 529-539
    • Warren, L.G.1
  • 25
    • 0020145791 scopus 로고
    • Trypanosomatidae: Isoleucine requirement and threonine deaminase in species with and without endosymbionts
    • S.C. Alfieri, and E.P. Camargo Trypanosomatidae: isoleucine requirement and threonine deaminase in species with and without endosymbionts Exp. Parasitol. 53 1982 371 380
    • (1982) Exp. Parasitol. , vol.53 , pp. 371-380
    • Alfieri, S.C.1    Camargo, E.P.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications
    • H. Towbin, T. Staehlin, and J. Bordon Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedures and some applications Proc. Natl. Acad. Sci. USA 76 1979 4350 4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehlin, T.2    Bordon, J.3
  • 28
    • 0017202399 scopus 로고
    • Ornithine and glutamic acid decarboxylase activities in the developing chick retina
    • F.G. De Mello, U. Bachrach, and M. Nirenberg Ornithine and glutamic acid decarboxylase activities in the developing chick retina J. Neurochem. 27 1976 847 851
    • (1976) J. Neurochem. , vol.27 , pp. 847-851
    • De Mello, F.G.1    Bachrach, U.2    Nirenberg, M.3
  • 30
    • 0020266408 scopus 로고
    • Adenine nucleoside and lysine transport in Chlamydia psittaci
    • T.P. Hatch, E. Al-Hossainy, and J.A. Silverman Adenine nucleoside and lysine transport in Chlamydia psittaci J. Bacteriol. 150 1982 662 670
    • (1982) J. Bacteriol. , vol.150 , pp. 662-670
    • Hatch, T.P.1    Al-Hossainy, E.2    Silverman, J.A.3
  • 31
    • 0015887291 scopus 로고
    • Growth and physiology of Rickettsiae
    • E. Weiss Growth and physiology of Rickettsiae Bacteriol. Rev. 37 1973 259 289
    • (1973) Bacteriol. Rev. , vol.37 , pp. 259-289
    • Weiss, E.1
  • 32
    • 0017230491 scopus 로고
    • Rickettsial permeability, An ADP-ATP transport system
    • H.H. Winkler Rickettsial permeability, An ADP-ATP transport system J. Biol. Chem. 251 1976 389 396
    • (1976) J. Biol. Chem. , vol.251 , pp. 389-396
    • Winkler, H.H.1
  • 34
    • 0026532729 scopus 로고
    • Deficiencies in DNA replication and cell-cycle progression in polyamine-starved HeLa cells
    • R.A. Koza, and E.J. Herbst Deficiencies in DNA replication and cell-cycle progression in polyamine-starved HeLa cells Biochem. J. 281 1992 87 93
    • (1992) Biochem. J. , vol.281 , pp. 87-93
    • Koza, R.A.1    Herbst, E.J.2
  • 35
    • 0027518126 scopus 로고
    • Features of the spermidin-binding site of deoxyhyposine synthase as derived from inhibition studies: Effective inhibition by bis- and mono-guanylated diamines and polyamines
    • J. Jakus, E.C. Wolff, M.H. Park, and E.J. Folk Features of the spermidin-binding site of deoxyhyposine synthase as derived from inhibition studies: effective inhibition by bis- and mono-guanylated diamines and polyamines J. Biol. Chem. 268 1993 13151 13159
    • (1993) J. Biol. Chem. , vol.268 , pp. 13151-13159
    • Jakus, J.1    Wolff, E.C.2    Park, M.H.3    Folk, E.J.4
  • 36
    • 0028985470 scopus 로고
    • Ornithine decarboxylase and S-adenosylmethionine decarboxylase expression during the cell cycle of chines hamster ovary cells
    • J.O. Fredlund, M.C. Johansson, E. Dahlberg, and S.M. Oredson Ornithine decarboxylase and S-adenosylmethionine decarboxylase expression during the cell cycle of chines hamster ovary cells Exp. Cell Res. 216 1995 86 92
    • (1995) Exp. Cell Res. , vol.216 , pp. 86-92
    • Fredlund, J.O.1    Johansson, M.C.2    Dahlberg, E.3    Oredson, S.M.4
  • 37
    • 0028386481 scopus 로고
    • Free, conjugated and bound polyamines during the cell cycle in synchronized cultures of Scenedesmus obliquus
    • K. Kotzabasis, and H. Senger Free, conjugated and bound polyamines during the cell cycle in synchronized cultures of Scenedesmus obliquus Z. Naturforsch. 49 1994 181 189
    • (1994) Z. Naturforsch. , vol.49 , pp. 181-189
    • Kotzabasis, K.1    Senger, H.2
  • 38
    • 0033671762 scopus 로고    scopus 로고
    • Ell-cycle dependent regulation of ornithine decarboxylase activity in the unicellular green alga Chlamydomonas reinhardtii
    • J. Voigt, and P. Bohley Ell-cycle dependent regulation of ornithine decarboxylase activity in the unicellular green alga Chlamydomonas reinhardtii Physiol. Plant 110 2000 419 425
    • (2000) Physiol. Plant , vol.110 , pp. 419-425
    • Voigt, J.1    Bohley, P.2
  • 39
    • 0025834130 scopus 로고
    • Insulin induction of ornithine decarboxylase. Importance of mRNA secondary structure and phosphorylation of eukaryotic initiation factors elF-4B and elF-4E
    • J.M. Manzella, W. Rychlik, R.E. Rhoads, J.W.B. Hershey, and P.J. Blackshear Insulin induction of ornithine decarboxylase. Importance of mRNA secondary structure and phosphorylation of eukaryotic initiation factors elF-4B and elF-4E J. Biol. Chem. 266 1991 2383 2389
    • (1991) J. Biol. Chem. , vol.266 , pp. 2383-2389
    • Manzella, J.M.1    Rychlik, W.2    Rhoads, R.E.3    Hershey, J.W.B.4    Blackshear, P.J.5
  • 40
    • 0025906211 scopus 로고
    • Effects of overexpression of ornithine decarboxylase (ODC) on growth control and oncogene-induced cell transformation
    • H. Hibshoosh, M. Johnson, and J.B. Weinstein Effects of overexpression of ornithine decarboxylase (ODC) on growth control and oncogene-induced cell transformation Oncogene 6 1991 739 743
    • (1991) Oncogene , vol.6 , pp. 739-743
    • Hibshoosh, H.1    Johnson, M.2    Weinstein, J.B.3
  • 41
    • 0026683752 scopus 로고
    • Ornithine decarboxylase is critical for cell transformation
    • M. Auvinen, A. Paasinen, L.A. Andersson, and E. Hölttä Ornithine decarboxylase is critical for cell transformation Nature 360 1992 355 358
    • (1992) Nature , vol.360 , pp. 355-358
    • Auvinen, M.1    Paasinen, A.2    Andersson, L.A.3    Hölttä, E.4
  • 42
    • 0028880977 scopus 로고
    • Relationship between ornithine decarboxylase and cytoskeletal organization in cultured human keratinocytes: Cellular responses to phorbol esters, cytochalasins, and α-difluoromethylornithine
    • M.M. Pomidor, K.R. Kimberley, P. Zheng, Y. Song, O.A. Janne, R.S. Tuan, and N.J. Hickok Relationship between ornithine decarboxylase and cytoskeletal organization in cultured human keratinocytes: cellular responses to phorbol esters, cytochalasins, and α-difluoromethylornithine Exp. Cell Res. 221 1995 426 437
    • (1995) Exp. Cell Res. , vol.221 , pp. 426-437
    • Pomidor, M.M.1    Kimberley, K.R.2    Zheng, P.3    Song, Y.4    Janne, O.A.5    Tuan, R.S.6    Hickok, N.J.7
  • 43
    • 0021718970 scopus 로고
    • Localization of ornithine decarboxylase in mutant CHO cells that overproduce the enzyme. Differences between the intracellular distribution of monospecific ornithine decarboxylase antibodies and radiolabeled alpha-difluoromethylornithine
    • S. Anehus, H. Emanuelsson, L. Persson, F. Sundler, I.E. Scheffler, and O. Heby Localization of ornithine decarboxylase in mutant CHO cells that overproduce the enzyme. Differences between the intracellular distribution of monospecific ornithine decarboxylase antibodies and radiolabeled alpha-difluoromethylornithine Eur. J. Cell Biol. 35 1984 264 272
    • (1984) Eur. J. Cell Biol. , vol.35 , pp. 264-272
    • Anehus, S.1    Emanuelsson, H.2    Persson, L.3    Sundler, F.4    Scheffler, I.E.5    Heby, O.6
  • 44
    • 0028950506 scopus 로고
    • Regulation of human ornithine decarboxylase expression following prolonged quiescence: Role for the c-Myc/Max protein complex
    • A. Pena, S. Wu, N.J. Hickok, D.R. Soprano, and K.J. Soprano Regulation of human ornithine decarboxylase expression following prolonged quiescence: role for the c-Myc/Max protein complex J. Cell. Physiol. 162 1995 234 245
    • (1995) J. Cell. Physiol. , vol.162 , pp. 234-245
    • Pena, A.1    Wu, S.2    Hickok, N.J.3    Soprano, D.R.4    Soprano, K.J.5
  • 45
    • 0033855363 scopus 로고    scopus 로고
    • Polyamine composition and expression of genes related to polyamine biosynthesis in a aphid endosymbiont, Buchnera
    • A. Nakabachi, and H. Ishikawa Polyamine composition and expression of genes related to polyamine biosynthesis in a aphid endosymbiont, Buchnera Appl. Environ. Microbiol. 6 2000 3305 3309
    • (2000) Appl. Environ. Microbiol. , vol.6 , pp. 3305-3309
    • Nakabachi, A.1    Ishikawa, H.2
  • 46
    • 0024805783 scopus 로고
    • On the subcellular localization of the polyamines
    • S. Sarhan, and N. Seiler On the subcellular localization of the polyamines Biol. Chem. Hoppe Seyler 370 1989 1279 1284
    • (1989) Biol. Chem. Hoppe Seyler , vol.370 , pp. 1279-1284
    • Sarhan, S.1    Seiler, N.2
  • 47
    • 0036010676 scopus 로고    scopus 로고
    • Regulation by polyamines of ornithine decarboxylase activity and cell division in the unicellular green alga Chlamydomonas reinhardtii
    • C. Theiss, P. Bohley, and J. Voigt Regulation by polyamines of ornithine decarboxylase activity and cell division in the unicellular green alga Chlamydomonas reinhardtii Plant Physiol. 128 2002 1470 1479
    • (2002) Plant Physiol. , vol.128 , pp. 1470-1479
    • Theiss, C.1    Bohley, P.2    Voigt, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.