메뉴 건너뛰기




Volumn 181, Issue 13, 1999, Pages 3904-3911

Effects of ethyl and benzyl analogues of spermine on Escherichia coli peptidyltransferase activity, polyamine transport, and cellular growth

Author keywords

[No Author keywords available]

Indexed keywords

MAGNESIUM ION; N1 ETHYLSPERMINE; N1,N12 DIETHYLSPERMINE; N4,N9 BIS(ETHYL)SPERMINE; N4,N9 DIBENZYLSPERMINE; PEPTIDYLTRANSFERASE; POLYAMINE; PUTRESCINE; SPERMINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0032987320     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.13.3904-3911.1999     Document Type: Article
Times cited : (5)

References (40)
  • 1
    • 0024319054 scopus 로고
    • Role of the methylene backbone in the antiproliferative activity of polyamine analogues on L1210 cells
    • Bergeron, R. J., T. R. Hawthorne, J. R. T. Vinson, D. E. Beck, and M. J. Ingeno. 1989. Role of the methylene backbone in the antiproliferative activity of polyamine analogues on L1210 cells. Cancer Res. 49:2959-2964.
    • (1989) Cancer Res. , vol.49 , pp. 2959-2964
    • Bergeron, R.J.1    Hawthorne, T.R.2    Vinson, J.R.T.3    Beck, D.E.4    Ingeno, M.J.5
  • 2
    • 0025316418 scopus 로고
    • Bis(benzyl)-polyamine analogues are substrates for a mammalian cell-transport system which is distinct from the polyamine-transport system
    • Byers, T. L., A. J. Bitonti, and P. P. McCann. 1990. Bis(benzyl)-polyamine analogues are substrates for a mammalian cell-transport system which is distinct from the polyamine-transport system. Biochem. J. 269:35-40.
    • (1990) Biochem. J. , vol.269 , pp. 35-40
    • Byers, T.L.1    Bitonti, A.J.2    McCann, P.P.3
  • 3
    • 0028095624 scopus 로고
    • Bimodal action of spermine on ribosomal peptidyltransferase at low concentrations of magnesium ions
    • Drainas, D., and D. L. Kalpaxis. 1993. Bimodal action of spermine on ribosomal peptidyltransferase at low concentrations of magnesium ions. Biochim. Biophys. Acta 1208:55-64.
    • (1993) Biochim. Biophys. Acta , vol.1208 , pp. 55-64
    • Drainas, D.1    Kalpaxis, D.L.2
  • 7
    • 0028070407 scopus 로고
    • Properties and structure of spermidine acetyltransferase in Escherichia coli
    • Fukuchi, J., K. Kashiwagi, K. Takio, and K. Igarashi. 1994. Properties and structure of spermidine acetyltransferase in Escherichia coli. J. Biol. Chem. 269:22581-22585.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22581-22585
    • Fukuchi, J.1    Kashiwagi, K.2    Takio, K.3    Igarashi, K.4
  • 8
    • 0024820056 scopus 로고
    • Regulation of eukaryotic initiator factor-2B activity by polyamines and amino acid starvation in rabbit reticulocyte lysate
    • Grass, M., and M. S. Rubino. 1989. Regulation of eukaryotic initiator factor-2B activity by polyamines and amino acid starvation in rabbit reticulocyte lysate. J. Biol. Chem. 264:21879-21884.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21879-21884
    • Grass, M.1    Rubino, M.S.2
  • 9
    • 0027420797 scopus 로고
    • Correlation between the inhibition of cell growth by accumulated polyamines and the decrease of magnesium and ATP
    • He, Y., K. Kashiwagi, J. Fukuchi, K. Terao, A. Shirahata, and K. Igarashi. 1993. Correlation between the inhibition of cell growth by accumulated polyamines and the decrease of magnesium and ATP. Eur. J. Biochem. 217:89-96.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 89-96
    • He, Y.1    Kashiwagi, K.2    Fukuchi, J.3    Terao, K.4    Shirahata, A.5    Igarashi, K.6
  • 10
    • 0028288228 scopus 로고
    • Correlation between the inhibition of cell growth by bis-(ethyl) polyamine analogues and the decrease in the function of mitochondria
    • He, Y., T. Suzuki, K. Kashiwagi, K. Kusama-Eguchi, A. Shirahata, and K. Igarashi. 1994. Correlation between the inhibition of cell growth by bis-(ethyl) polyamine analogues and the decrease in the function of mitochondria. Eur. J. Biochem. 221:391-398.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 391-398
    • He, Y.1    Suzuki, T.2    Kashiwagi, K.3    Kusama-Eguchi, K.4    Shirahata, A.5    Igarashi, K.6
  • 11
    • 0019334383 scopus 로고
    • Effect of polypeptide initiation factors on the spermidine stimulation of initiation complex formation
    • Igarashi, K., Y. Matsuo, K. Mitsui, and S. Hirose. 1980. Effect of polypeptide initiation factors on the spermidine stimulation of initiation complex formation. Biochem. Biophys. Res. Commun. 93:360-368.
    • (1980) Biochem. Biophys. Res. Commun. , vol.93 , pp. 360-368
    • Igarashi, K.1    Matsuo, Y.2    Mitsui, K.3    Hirose, S.4
  • 13
    • 0030049649 scopus 로고    scopus 로고
    • Polyamine transport in Escherichia coli
    • Igarashi, K., and K. Kashiwagi. 1996. Polyamine transport in Escherichia coli. Amino Acids 10:83-97.
    • (1996) Amino Acids , vol.10 , pp. 83-97
    • Igarashi, K.1    Kashiwagi, K.2
  • 14
    • 0031047822 scopus 로고    scopus 로고
    • Molecular mechanism of polyamine stimulation of the synthesis of oligopeptide-binding protein
    • Igarashi, K., T. Saisho, M. Yuguchi, and K. Kashiwagi. 1997. Molecular mechanism of polyamine stimulation of the synthesis of oligopeptide-binding protein. J. Biol. Chem. 272:4058-4064.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4058-4064
    • Igarashi, K.1    Saisho, T.2    Yuguchi, M.3    Kashiwagi, K.4
  • 15
    • 0022444341 scopus 로고
    • Kinetic studies on ribosomal peptidyltransferase. The behaviour of the inhibitor blasticidin S
    • Kalpaxis, D. L., D. Theocharis, and C. Coutsogeorgopoulos. 1986. Kinetic studies on ribosomal peptidyltransferase. The behaviour of the inhibitor blasticidin S. Eur. J. Biochem. 154:267-271.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 267-271
    • Kalpaxis, D.L.1    Theocharis, D.2    Coutsogeorgopoulos, C.3
  • 16
    • 0026630137 scopus 로고
    • Effect of spermine on peptide-bond formation, catalyzed by ribosomal peptidyltransferase
    • Kalpaxis, D. L., and D. Drainas. 1992. Effect of spermine on peptide-bond formation, catalyzed by ribosomal peptidyltransferase. Mol. Cell. Biochem. 115:19-26.
    • (1992) Mol. Cell. Biochem. , vol.115 , pp. 19-26
    • Kalpaxis, D.L.1    Drainas, D.2
  • 17
    • 0032005114 scopus 로고    scopus 로고
    • The effect of acylated polyamine derivatives on polyamine uptake mechanism, cell growth, and polyamine pools in Escherichia coli, and the pursuit of structure/activity relationships
    • Karahalios, P., P. Mamos, D. H. Vynios, D. Papaioannou, and D. L. Kalpaxis. 1998. The effect of acylated polyamine derivatives on polyamine uptake mechanism, cell growth, and polyamine pools in Escherichia coli, and the pursuit of structure/activity relationships. Eur. J. Biochem. 251:998-1004.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 998-1004
    • Karahalios, P.1    Mamos, P.2    Vynios, D.H.3    Papaioannou, D.4    Kalpaxis, D.L.5
  • 18
    • 0032402804 scopus 로고    scopus 로고
    • Structure/function correlation of spermine-analogue-induced modulation of peptidyltransferase activity
    • Karahalios, P., P. Mamos, G. Karigiannis, and D. L. Kalpaxis. 1998. Structure/function correlation of spermine-analogue-induced modulation of peptidyltransferase activity. Eur. J. Biochem. 258:437-444.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 437-444
    • Karahalios, P.1    Mamos, P.2    Karigiannis, G.3    Kalpaxis, D.L.4
  • 19
    • 0025687503 scopus 로고
    • Isolation of polyamine transport-deficient mutants of Escherichia coli and cloning of the genes for polyamine transport proteins
    • Kashiwagi, K., N. Hosokawa, T. Furuchi, H. Kobayashi, C. Sasakawa, M. Yoshikawa, and K. Igarashi. 1990. Isolation of polyamine transport-deficient mutants of Escherichia coli and cloning of the genes for polyamine transport proteins. J. Biol. Chem. 265:20893-20897.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20893-20897
    • Kashiwagi, K.1    Hosokawa, N.2    Furuchi, T.3    Kobayashi, H.4    Sasakawa, C.5    Yoshikawa, M.6    Igarashi, K.7
  • 23
    • 0028956729 scopus 로고
    • Polyamines as targets for therapeutic intervention
    • Marton, L. J., and A. E. Pegg. 1995. Polyamines as targets for therapeutic intervention. Annu. Rev. Pharmacol. Toxicol. 35:55-91.
    • (1995) Annu. Rev. Pharmacol. Toxicol. , vol.35 , pp. 55-91
    • Marton, L.J.1    Pegg, A.E.2
  • 24
    • 0031983566 scopus 로고    scopus 로고
    • Human prostatic carcinoma cell lines display altered regulation of polyamine transport in response to polyamine analogs and inhibitors
    • Mi, Z., D. L. Kramer, J. T. Miller, R. J. Bergeron, R. Bernacki, and C. W. Porter. 1998. Human prostatic carcinoma cell lines display altered regulation of polyamine transport in response to polyamine analogs and inhibitors. Prostate 34:51-60.
    • (1998) Prostate , vol.34 , pp. 51-60
    • Mi, Z.1    Kramer, D.L.2    Miller, J.T.3    Bergeron, R.J.4    Bernacki, R.5    Porter, C.W.6
  • 25
    • 0028232328 scopus 로고
    • Role of polyamines in the binding of initiator tRNA to the 70S ribosomes of extreme thermophilic bacterium Calderobacterium hydrogenophilum
    • Mikulik, K., and M. Anderova. 1994. Role of polyamines in the binding of initiator tRNA to the 70S ribosomes of extreme thermophilic bacterium Calderobacterium hydrogenophilum. Arch. Microbiol. 161:508-513.
    • (1994) Arch. Microbiol. , vol.161 , pp. 508-513
    • Mikulik, K.1    Anderova, M.2
  • 26
    • 0027265852 scopus 로고
    • Estimation of polyamine distribution and polyamine stimulation of protein synthesis in Escherichia coli
    • Mijamoto, S., K. Kashiwagi, K. Ito, S. Watanabe, and K. Igarashi. 1993. Estimation of polyamine distribution and polyamine stimulation of protein synthesis in Escherichia coli. Arch. Biochem. Biophys. 300:63-68.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 63-68
    • Mijamoto, S.1    Kashiwagi, K.2    Ito, K.3    Watanabe, S.4    Igarashi, K.5
  • 27
    • 0024312594 scopus 로고
    • Effect of spermine on the efficiency and fidelity of the codon-specific binding of tRNA to the ribosomes
    • Naranda, T., and Z. Kucan. 1989. Effect of spermine on the efficiency and fidelity of the codon-specific binding of tRNA to the ribosomes. Eur. J. Biochem. 182:291-297.
    • (1989) Eur. J. Biochem. , vol.182 , pp. 291-297
    • Naranda, T.1    Kucan, Z.2
  • 28
    • 0029039284 scopus 로고
    • Optimization of the HPLC analysis of biogenic amines in Peucedanum palustre plants and cell culture lines
    • Outinen, K., P. Vuoreta, R. Hinkkanen, R. Hiltunen, and H. Vuorela. 1995. Optimization of the HPLC analysis of biogenic amines in Peucedanum palustre plants and cell culture lines. Planta Med. 61:259-263.
    • (1995) Planta Med. , vol.61 , pp. 259-263
    • Outinen, K.1    Vuoreta, P.2    Hinkkanen, R.3    Hiltunen, R.4    Vuorela, H.5
  • 29
    • 0023881236 scopus 로고
    • Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy
    • Pegg, A. E. 1988. Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy. Cancer Res. 48:759-774.
    • (1988) Cancer Res. , vol.48 , pp. 759-774
    • Pegg, A.E.1
  • 30
    • 0029024723 scopus 로고
    • Use of aminopropyl-transferase inhibitors and of non-metabolizable analogs to study polyamine regulation and function
    • Pegg, A. E., R. Poulin, and J. K. Coward. 1995. Use of aminopropyl-transferase inhibitors and of non-metabolizable analogs to study polyamine regulation and function. Int. J. Biochem. Cell. Biol. 27:425-442.
    • (1995) Int. J. Biochem. Cell. Biol. , vol.27 , pp. 425-442
    • Pegg, A.E.1    Poulin, R.2    Coward, J.K.3
  • 31
    • 0023223138 scopus 로고
    • Relative abilities of bis(ethyl) derivatives of putrescine, spermidine, and spermine to regulate polyamine biosynthesis and inhibit L1210 leukemia cell growth
    • Porter, C. W., J. S. McManis, R. A. Casero, and R. J. Bergeron. 1987. Relative abilities of bis(ethyl) derivatives of putrescine, spermidine, and spermine to regulate polyamine biosynthesis and inhibit L1210 leukemia cell growth. Cancer Res, 47:2821-2825.
    • (1987) Cancer Res , vol.47 , pp. 2821-2825
    • Porter, C.W.1    McManis, J.S.2    Casero, R.A.3    Bergeron, R.J.4
  • 34
    • 0003518480 scopus 로고
    • John Wiley & Sons, New York, N.Y.
    • Segel, I. H. 1993. Enzyme kinetics, p. 166-169. John Wiley & Sons, New York, N.Y.
    • (1993) Enzyme Kinetics , pp. 166-169
    • Segel, I.H.1
  • 36
    • 0025785606 scopus 로고
    • Effects of polyamine analogs on the extent and fidelity of in vitro polypeptide synthesis
    • Synder, R. D., and M. L. Edwards. 1991. Effects of polyamine analogs on the extent and fidelity of in vitro polypeptide synthesis. Biochim. Biophys. Res. Commun. 176:1383-1392.
    • (1991) Biochim. Biophys. Res. Commun. , vol.176 , pp. 1383-1392
    • Synder, R.D.1    Edwards, M.L.2
  • 37
    • 0029658872 scopus 로고    scopus 로고
    • The 1.8-Å x-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding
    • Sugiyama, S., Y. Matsuo, K. Maenaka, D. G. Vassylyev, M. Matsusima, K. Kashiwagi, K. Igarashi, and K. Morikawa. 1996. The 1.8-Å x-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding. Protein Sci. 5:1984-1990.
    • (1996) Protein Sci. , vol.5 , pp. 1984-1990
    • Sugiyama, S.1    Matsuo, Y.2    Maenaka, K.3    Vassylyev, D.G.4    Matsusima, M.5    Kashiwagi, K.6    Igarashi, K.7    Morikawa, K.8
  • 38
    • 0023100740 scopus 로고
    • Studies on the catalytic rate constant of ribosomal peptidyltransferase
    • Synetos, D., and C. Coutsogeorgopoulos. 1987. Studies on the catalytic rate constant of ribosomal peptidyltransferase. Biochim. Biophys. Acta 923:275-285.
    • (1987) Biochim. Biophys. Acta , vol.923 , pp. 275-285
    • Synetos, D.1    Coutsogeorgopoulos, C.2
  • 40
    • 0032504154 scopus 로고    scopus 로고
    • Crystal structure and mutational analysis of the Escherichia coli putrescine receptor
    • Vassylyev, D. G., H. Tomitori, K. Kashiwagi, K. Morikawa, and K. Igarashi. 1998. Crystal structure and mutational analysis of the Escherichia coli putrescine receptor. J. Biol. Chem. 273:17604-17609.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17604-17609
    • Vassylyev, D.G.1    Tomitori, H.2    Kashiwagi, K.3    Morikawa, K.4    Igarashi, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.