메뉴 건너뛰기




Volumn 55, Issue 7, 1998, Pages 1119-1123

Induction of spermidine/spermine N1-acetyltransferase in human cancer cells in response to increased production of reactive oxygen species

Author keywords

Acetylation; Cancer cells; Polyamines; Reactive oxygen; Species

Indexed keywords

ACYLTRANSFERASE; REACTIVE OXYGEN METABOLITE; SPERMIDINE; SPERMINE;

EID: 0032055631     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(97)00601-1     Document Type: Article
Times cited : (76)

References (29)
  • 1
    • 0018088697 scopus 로고
    • Polyamines in rapid growth and cancer
    • Janne J., Poso H., Raina A. Polyamines in rapid growth and cancer. Biochim Biophys Acta. 473:1978;241-293.
    • (1978) Biochim Biophys Acta , vol.473 , pp. 241-293
    • Janne, J.1    Poso, H.2    Raina, A.3
  • 2
    • 0019469747 scopus 로고
    • Role of polyamines in the control of cell proliferation and differentiation
    • Heby O. Role of polyamines in the control of cell proliferation and differentiation. Differentiation. 19:1981;1-20.
    • (1981) Differentiation , vol.19 , pp. 1-20
    • Heby, O.1
  • 3
    • 0023881236 scopus 로고
    • Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy
    • Pegg A.E. Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy. Cancer Res. 48:1988;759-774.
    • (1988) Cancer Res. , vol.48 , pp. 759-774
    • Pegg, A.E.1
  • 4
    • 0025325255 scopus 로고
    • Molecular genetics of polyamine synthesis in eukaryotic cells
    • Heby O., Persson L. Molecular genetics of polyamine synthesis in eukaryotic cells. TIBS. 15:1990;153-158.
    • (1990) TIBS , vol.15 , pp. 153-158
    • Heby, O.1    Persson, L.2
  • 5
    • 0021921407 scopus 로고
    • Comparison of ornithine decarboxylase from rat liver, rat hepatoma and mouse kidney
    • Seely J.E., Persson L., Sertich G.J., Pegg A.E. Comparison of ornithine decarboxylase from rat liver, rat hepatoma and mouse kidney. Biochem J. 226:1985;577-586.
    • (1985) Biochem J. , vol.226 , pp. 577-586
    • Seely, J.E.1    Persson, L.2    Sertich, G.J.3    Pegg, A.E.4
  • 6
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded sequences: The PEST hypothesis
    • Rogers S., Wells R., Rechsteiner M. Amino acid sequences common to rapidly degraded sequences: The PEST hypothesis. Science. 234:1986;364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 7
    • 0021750983 scopus 로고
    • 1-acetyltransferase using a specific antiserum
    • 1-acetyltransferase using a specific antiserum. J Biol Chem. 259:1984;12364-12367.
    • (1984) J Biol Chem. , vol.259 , pp. 12364-12367
    • Persson, L.1    Pegg, A.E.2
  • 8
    • 0027238083 scopus 로고
    • 1-acetyltransferase: The turning point in polyamine metabolism
    • 1-acetyltransferase: the turning point in polyamine metabolism. FASEB J. 7:1993;653-689.
    • (1993) FASEB J , vol.7 , pp. 653-689
    • Casero R.A., Jr.1    Pegg, A.E.2
  • 9
    • 0020001510 scopus 로고
    • 1-acetyltransferase by dialkylnitrosoamines
    • 1-acetyltransferase by dialkylnitrosoamines. Cancer Res. 42:1982;2990-2995.
    • (1982) Cancer Res. , vol.42 , pp. 2990-2995
    • Matsui, I.1    Pegg, A.E.2
  • 10
    • 0023906738 scopus 로고
    • Elevation of acetylpolyamine levels in mouse tissues, serum and urine after treatment with radical producing drugs and lipopolysaccharide
    • Sugimoto H., Yamada S., Arai T., Kobayashi S., Hamana K., Matsuzaki S. Elevation of acetylpolyamine levels in mouse tissues, serum and urine after treatment with radical producing drugs and lipopolysaccharide. Hepatology. 8:1988;267-271.
    • (1988) Hepatology , vol.8 , pp. 267-271
    • Sugimoto, H.1    Yamada, S.2    Arai, T.3    Kobayashi, S.4    Hamana, K.5    Matsuzaki, S.6
  • 12
    • 0344312176 scopus 로고
    • Regulation of polyamine acetylation by doxorubicin in human breast cancer cells
    • Quick D.M., Wallace H.M. Regulation of polyamine acetylation by doxorubicin in human breast cancer cells. Br J Cancer. 68:1993;444.
    • (1993) Br J Cancer , vol.68 , pp. 444
    • Quick, D.M.1    Wallace, H.M.2
  • 13
    • 0025608363 scopus 로고
    • Changes in polyamine acetylation in human cancer cells
    • Wallace H.M., Coleman C.S. Changes in polyamine acetylation in human cancer cells. Biochem Soc Trans. 18:1990;1091-1094.
    • (1990) Biochem Soc Trans. , vol.18 , pp. 1091-1094
    • Wallace, H.M.1    Coleman, C.S.2
  • 14
    • 0027184078 scopus 로고
    • 1-acetyltransferase in human breast carcinoma cells - A possible role for calcium
    • 1-acetyltransferase in human breast carcinoma cells - a possible role for calcium. Biochem Pharmacol. 46:1993;969-974.
    • (1993) Biochem Pharmacol. , vol.46 , pp. 969-974
    • Quick, D.M.1    Wallace, H.M.2
  • 15
    • 0017064979 scopus 로고
    • A fluorimetric method for the determination of oxidised and reduced glutathione in tissues
    • Hissin P.J., Hilf R. A fluorimetric method for the determination of oxidised and reduced glutathione in tissues. Anal Biochem. 74:1976;214-226.
    • (1976) Anal Biochem. , vol.74 , pp. 214-226
    • Hissin, P.J.1    Hilf, R.2
  • 18
    • 0023633270 scopus 로고
    • Polyamine catabolism in mammalian cells: Excretion and acetylation
    • Wallace H.M. Polyamine catabolism in mammalian cells: excretion and acetylation. Med Sci Res. 15:1987;1437-1440.
    • (1987) Med Sci Res. , vol.15 , pp. 1437-1440
    • Wallace, H.M.1
  • 19
    • 0019876646 scopus 로고
    • Properties of spermidine N-acetyltransferase from livers of rats treated with carbon tetrachloride and its role in the conversion of spermidine into putrescine
    • Matsui I., Wiegand L., Pegg A.E. Properties of spermidine N-acetyltransferase from livers of rats treated with carbon tetrachloride and its role in the conversion of spermidine into putrescine. J Biol Chem. 256:1981;2454-2459.
    • (1981) J Biol Chem. , vol.256 , pp. 2454-2459
    • Matsui, I.1    Wiegand, L.2    Pegg, A.E.3
  • 20
    • 0003147690 scopus 로고
    • 8-spermidine acetyltransferase in human colonic carcinoma cells
    • H.R. Dowling, L.R. Folsch, & C. Loser. United Kingdom: Kluwer Academic Press
    • 8-spermidine acetyltransferase in human colonic carcinoma cells. Dowling H.R., Folsch L.R., Loser C. Polyamines and the Gastrointestinal Tract. 1992;87-93 Kluwer Academic Press, United Kingdom.
    • (1992) Polyamines and the Gastrointestinal Tract. , pp. 87-93
    • Wallace, H.M.1    Ball, D.E.2    Coleman, C.S.3
  • 21
    • 0025833516 scopus 로고
    • 1-acetyltransferase activity, polyamine pool depletion and growth inhibition in human melanoma cell lines
    • 1-acetyltransferase activity, polyamine pool depletion and growth inhibition in human melanoma cell lines. Cancer Res. 51:1991;3715-3720.
    • (1991) Cancer Res. , vol.51 , pp. 3715-3720
    • Porter, C.W.1    Ganis, B.2    Libby, P.R.3    Bergeron, R.J.4
  • 22
    • 0029081697 scopus 로고
    • Induction of programmed cell death in human breast cancer cells by an unsymmetrically alkylated polyamine analogue
    • McCloskey D.E., Casero R.A. Jr, Woster P.M., Davisdson N.E. Induction of programmed cell death in human breast cancer cells by an unsymmetrically alkylated polyamine analogue. Cancer Res. 55:1995;3233-3236.
    • (1995) Cancer Res. , vol.55 , pp. 3233-3236
    • McCloskey, D.E.1    Casero R.A., Jr.2    Woster, P.M.3    Davisdson, N.E.4
  • 24
    • 0027503178 scopus 로고
    • The permissive role of oxygen derived free radicals in the development of colonic cancer in the rat. A new theory for carcinogenesis
    • Salim A.S. The permissive role of oxygen derived free radicals in the development of colonic cancer in the rat. A new theory for carcinogenesis. Int J Cancer. 53:1993;1031-1035.
    • (1993) Int J Cancer , vol.53 , pp. 1031-1035
    • Salim, A.S.1
  • 25
    • 0016246294 scopus 로고
    • Role of superoxide radical in mitochondrial dehydrogenase reactions
    • Foreman H.J., Kennedy J.A. Role of superoxide radical in mitochondrial dehydrogenase reactions. Biochem Biophys Res Commun. 60:1974;1044-1050.
    • (1974) Biochem Biophys Res Commun. , vol.60 , pp. 1044-1050
    • Foreman, H.J.1    Kennedy, J.A.2
  • 26
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens J.F., Alexandre A., Lehninger A.L. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch Biochem Biophys. 237:1985;408-414.
    • (1985) Arch Biochem Biophys , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 27
    • 0027252891 scopus 로고
    • The implications of a unified theory of programmed cell death, polyamines, oxyradicals and histogenesis in the embryo
    • Parchment R. The implications of a unified theory of programmed cell death, polyamines, oxyradicals and histogenesis in the embryo. Int J Dev Biol. 37:1993;75-83.
    • (1993) Int J Dev Biol. , vol.37 , pp. 75-83
    • Parchment, R.1
  • 28
    • 0026076137 scopus 로고
    • Mechanisms of spermine toxicity in baby hamster kidney (BHK) cells: The role of amine oxidases and oxidative stress
    • Brunton V.G., Grant M.H., Wallace H.M. Mechanisms of spermine toxicity in baby hamster kidney (BHK) cells: the role of amine oxidases and oxidative stress. Biochem J. 280:1991;193-198.
    • (1991) Biochem J , vol.280 , pp. 193-198
    • Brunton, V.G.1    Grant, M.H.2    Wallace, H.M.3
  • 29
    • 0023692753 scopus 로고
    • Acetylation of spermidine and methylglyoxal bis(guanylhydrazone) in baby hamster kidney cells (BHK-21/C13)
    • Wallace H.M., Nuttall M.E., Robinson F.C. Acetylation of spermidine and methylglyoxal bis(guanylhydrazone) in baby hamster kidney cells (BHK-21/C13). Biochem J. 253:1988;223-227.
    • (1988) Biochem J , vol.253 , pp. 223-227
    • Wallace, H.M.1    Nuttall, M.E.2    Robinson, F.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.