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Volumn 2, Issue 4, 1997, Pages 124-130

Recent advances in polyamine research

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS;

EID: 0031127577     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1360-1385(97)01013-3     Document Type: Review
Times cited : (348)

References (53)
  • 2
    • 84941114293 scopus 로고
    • Polyamine metabolism
    • The Biochemistry of Plants (Miflin, B.J. and Lea, P.J., eds), Academic Press
    • 2 Tiburcio, A.F., Kaur-Sawhney, R. and Galston, A.W. (1990) Polyamine metabolism, in Intermedatory Nitrogen Metabolism (Vol. 16, The Biochemistry of Plants) (Miflin, B.J. and Lea, P.J., eds), pp. 283-325, Academic Press
    • (1990) Intermedatory Nitrogen Metabolism , vol.16 , pp. 283-325
    • Tiburcio, A.F.1    Kaur-Sawhney, R.2    Galston, A.W.3
  • 3
    • 0002040306 scopus 로고
    • Tissue and subcellular localisation of polyamines and enzymes of polyamine metabolism
    • (Slocum, R.D. and Flores, H.E., eds), CRC Press
    • 3 Slocum, R.D. (1991) Tissue and subcellular localisation of polyamines and enzymes of polyamine metabolism, in The Biochemistry and Physiology of Polyamines in Plants (Slocum, R.D. and Flores, H.E., eds), pp. 93-103, CRC Press
    • (1991) The Biochemistry and Physiology of Polyamines in Plants , pp. 93-103
    • Slocum, R.D.1
  • 4
    • 0025325255 scopus 로고
    • Molecular genetics of polyamine synthesis in eukaryotic cells
    • 4 Heby, O. and Persson, L. (1990) Molecular genetics of polyamine synthesis in eukaryotic cells, Trends Biochem. Sci. 15, 153-158
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 153-158
    • Heby, O.1    Persson, L.2
  • 5
    • 0029968417 scopus 로고    scopus 로고
    • Phosphorylation of Okazaki-like DNA fragments in mammalian cells and role of polyamines in the processing of this DNA
    • 5 Pohjanpelto, P. and Höltta, E. (1996) Phosphorylation of Okazaki-like DNA fragments in mammalian cells and role of polyamines in the processing of this DNA, EMBO J. 15, 1193-1200
    • (1996) EMBO J. , vol.15 , pp. 1193-1200
    • Pohjanpelto, P.1    Höltta, E.2
  • 6
    • 0000454546 scopus 로고
    • Do polyamines have roles in plant development?
    • 6 Evans, P.T. and Malmberg, R.L. (1989) Do polyamines have roles in plant development? Annu. Rev. Plant Physiol. 40, 235-269
    • (1989) Annu. Rev. Plant Physiol. , vol.40 , pp. 235-269
    • Evans, P.T.1    Malmberg, R.L.2
  • 8
    • 0028269271 scopus 로고
    • Agmatine - An endogenous clonidine-displacing substances in the brain
    • 8 Li, G.M. et al. (1994) Agmatine - an endogenous clonidine-displacing substances in the brain, Science 263, 966-969
    • (1994) Science , vol.263 , pp. 966-969
    • Li, G.M.1
  • 9
    • 0028799607 scopus 로고
    • Rapid and regulated degradation of ornithine decarboxylase
    • 9 Hayashi, S. and Murakami, Y. (1995) Rapid and regulated degradation of ornithine decarboxylase, Biochem. J. 306, 221-230
    • (1995) Biochem. J. , vol.306 , pp. 221-230
    • Hayashi, S.1    Murakami, Y.2
  • 10
    • 0028985119 scopus 로고
    • cDNAs from Catharanthus roseus, heterologous expression, identification of the proenzyme-processing site, evidence for the presence of both subunits in the active enzyme, and a conserved region in the 5′-mRNA leader
    • 10 Schröder, G. and Schröder, J. (1995) cDNAs from Catharanthus roseus, heterologous expression, identification of the proenzyme-processing site, evidence for the presence of both subunits in the active enzyme, and a conserved region in the 5′-mRNA leader, Eur. J. Biochem. 228, 74-78
    • (1995) Eur. J. Biochem. , vol.228 , pp. 74-78
    • Schröder, G.1    Schröder, J.2
  • 11
    • 0028101319 scopus 로고
    • Arginine decarboxylase of oats is activated by enzymatic cleavage into two polypeptides
    • 11 Malmberg, R.L. and Cellino, M.L. (1994) Arginine decarboxylase of oats is activated by enzymatic cleavage into two polypeptides, J. Biol. Chem. 28, 2703-2706
    • (1994) J. Biol. Chem. , vol.28 , pp. 2703-2706
    • Malmberg, R.L.1    Cellino, M.L.2
  • 12
    • 0030499122 scopus 로고    scopus 로고
    • Regulation of arginine decarboxylase by spermine in osmotically-stressed oat leaves
    • 12 Borrell, A. et al. (1996) Regulation of arginine decarboxylase by spermine in osmotically-stressed oat leaves, Physiol. Plant. 98, 105-110
    • (1996) Physiol. Plant. , vol.98 , pp. 105-110
    • Borrell, A.1
  • 13
    • 0030221359 scopus 로고    scopus 로고
    • Regulation of Arabidopsis thaliana (L.) Heynh arginine decarboxylase by potassium deficiency stress
    • 13 Watson, M.B. and Malmberg, R.L. (1996) Regulation of Arabidopsis thaliana (L.) Heynh arginine decarboxylase by potassium deficiency stress, Plant Physiol 111, 1077-1083
    • (1996) Plant Physiol , vol.111 , pp. 1077-1083
    • Watson, M.B.1    Malmberg, R.L.2
  • 14
    • 0027145724 scopus 로고
    • Polyamines in the photosynthetic apparatus. Photosystem II highly resolved subcomplexes are enriched in spermine
    • 14 Kotzabasis, K. et al. (1993) Polyamines in the photosynthetic apparatus. Photosystem II highly resolved subcomplexes are enriched in spermine, Photosynth. Res. 38, 83-88
    • (1993) Photosynth. Res. , vol.38 , pp. 83-88
    • Kotzabasis, K.1
  • 15
    • 0028042505 scopus 로고
    • Identification of chlorophyll-a/b proteins as substrates of transglutaminase activity in isolated chloroplasts of Helianthus tuberosus (L.)
    • 15 Del Duca, S. et al. (1994) Identification of chlorophyll-a/b proteins as substrates of transglutaminase activity in isolated chloroplasts of Helianthus tuberosus (L.), Planta 193, 283-289
    • (1994) Planta , vol.193 , pp. 283-289
    • Del Duca, S.1
  • 16
    • 0000427023 scopus 로고
    • Effect of polyamines on stabilization of molecular complexes in thylakoid membranes of osmotically-stressed oat leaves
    • 16 Besford, R. et al. (1993) Effect of polyamines on stabilization of molecular complexes in thylakoid membranes of osmotically-stressed oat leaves, Planta 189, 201-206
    • (1993) Planta , vol.189 , pp. 201-206
    • Besford, R.1
  • 17
    • 0029012387 scopus 로고
    • Influence of polyamine inhibitors on light independent and light dependent chlorophyll biosynthesis and on the photosynthetic rate
    • 17 Beigbeder, A. et al. (1995) Influence of polyamine inhibitors on light independent and light dependent chlorophyll biosynthesis and on the photosynthetic rate, J. Photochem. Photobiol. 28, 235-242
    • (1995) J. Photochem. Photobiol. , vol.28 , pp. 235-242
    • Beigbeder, A.1
  • 18
    • 0029176066 scopus 로고
    • Arginine decarboxylase is localized in chloroplasts
    • 18 Borrell, A.F. et al. (1995) Arginine decarboxylase is localized in chloroplasts, Plant Physiol. 109, 771-776
    • (1995) Plant Physiol. , vol.109 , pp. 771-776
    • Borrell, A.F.1
  • 19
    • 0001569460 scopus 로고
    • The possible involvement of polyamines in the development of tomato fruits in vitro
    • 19 Teitel, D.C. et al. (1985) The possible involvement of polyamines in the development of tomato fruits in vitro, Plant Growth Regul. 3, 309-317
    • (1985) Plant Growth Regul. , vol.3 , pp. 309-317
    • Teitel, D.C.1
  • 20
    • 0002142630 scopus 로고
    • Cytological events induced by inhibition of polyamine biosynthesis in thin cell layers of tobacco
    • 20 Altamura, M.M. et al (1993) Cytological events induced by inhibition of polyamine biosynthesis in thin cell layers of tobacco, Protoplasma 175, 9-16
    • (1993) Protoplasma , vol.175 , pp. 9-16
    • Altamura, M.M.1
  • 21
    • 0028874035 scopus 로고
    • Efficient plant regeneration from long-term callus cultures of rice by spermidine
    • 21 Bajaj, S. and Rajam, M.V. (1995) Efficient plant regeneration from long-term callus cultures of rice by spermidine, Plant Cell Rep. 14, 717-720
    • (1995) Plant Cell Rep. , vol.14 , pp. 717-720
    • Bajaj, S.1    Rajam, M.V.2
  • 23
    • 0011197593 scopus 로고
    • Regulatory functions of polyamines during in vitro plant development
    • 23 Tiburcio, A.F. et al. (1993) Regulatory functions of polyamines during in vitro plant development, Curr. Top. Plant Physiol. 1, 41-63
    • (1993) Curr. Top. Plant Physiol. , vol.1 , pp. 41-63
    • Tiburcio, A.F.1
  • 24
    • 0001847716 scopus 로고
    • Changes in polyamine content of Arabidopsis thaliana after UV-C irradiation
    • (Galston, A.W. and Tiburcio, A.F., eds), Fundación Juan March
    • 24 Campos, J.L. et al (1991) Changes in polyamine content of Arabidopsis thaliana after UV-C irradiation, Lecture Course on Polyamines as Modulators of Plant Development (Galston, A.W. and Tiburcio, A.F., eds), pp. 78-80, Fundación Juan March
    • (1991) Lecture Course on Polyamines As Modulators of Plant Development , pp. 78-80
    • Campos, J.L.1
  • 25
    • 0028900859 scopus 로고
    • Stable amplification of the S-adenosylmethionine decarboxylase gene in Chinese hamster ovary cells
    • 25 Kramer, D. et al (1995) Stable amplification of the S-adenosylmethionine decarboxylase gene in Chinese hamster ovary cells, J. Biol. Chem. 270, 2124-2132
    • (1995) J. Biol. Chem. , vol.270 , pp. 2124-2132
    • Kramer, D.1
  • 26
    • 0001777654 scopus 로고
    • Biochemical genetics of resistance to MGBG in tobacco: Mutants that alter SAM-decarboxylase or polyamine ratios, and flower morphology
    • 26 Malmberg, R.L. and Rose, D.G. (1987) Biochemical genetics of resistance to MGBG in tobacco: mutants that alter SAM-decarboxylase or polyamine ratios, and flower morphology, Mol. Gen. Genet. 207, 9-14
    • (1987) Mol. Gen. Genet. , vol.207 , pp. 9-14
    • Malmberg, R.L.1    Rose, D.G.2
  • 27
    • 0029152442 scopus 로고
    • T-DNA tagging of genes influencing polyamine metabolism: Isolation of mutant plant lines and rescue of DNA promoting growth in the presence of a polyamine biosynthetic inhibitor
    • 27 Fritze, K., Czaja, I. and Walden, R. (1995) T-DNA tagging of genes influencing polyamine metabolism: isolation of mutant plant lines and rescue of DNA promoting growth in the presence of a polyamine biosynthetic inhibitor, Plant J. 7, 261-271
    • (1995) Plant J. , vol.7 , pp. 261-271
    • Fritze, K.1    Czaja, I.2    Walden, R.3
  • 29
    • 0024301133 scopus 로고
    • Strong cellular preference in the expression of a housekeeping gene of Arabidopsis thaliana encoding S-adenosylmethionine synthetase
    • 29 Peleman, J. et al. (1989) Strong cellular preference in the expression of a housekeeping gene of Arabidopsis thaliana encoding S-adenosylmethionine synthetase, Plant Cell 1, 81-93
    • (1989) Plant Cell , vol.1 , pp. 81-93
    • Peleman, J.1
  • 30
    • 0000083666 scopus 로고
    • Cloning and nucleotide sequence of an S-adenosylmethionine synthetase cDNA from carnation
    • 30 Larsen, R.B. and Woodson, W.R. (1991) Cloning and nucleotide sequence of an S-adenosylmethionine synthetase cDNA from carnation, Plant Physiol. 96, 997-999
    • (1991) Plant Physiol. , vol.96 , pp. 997-999
    • Larsen, R.B.1    Woodson, W.R.2
  • 31
    • 0026587102 scopus 로고
    • Induction by fungal elicitor of S-adenosyl-L-methionine synthetase and S-adenosyl-L-homocysteine hydrolase mRNA in cultured cells and leaves of Petroselium crispum
    • 31 Kawalleck, P. et al. (1992) Induction by fungal elicitor of S-adenosyl-L-methionine synthetase and S-adenosyl-L-homocysteine hydrolase mRNA in cultured cells and leaves of Petroselium crispum, Proc. Natl. Acad. Sci. U. S, A. 89, 4713-4717
    • (1992) Proc. Natl. Acad. Sci. U. S, A. , vol.89 , pp. 4713-4717
    • Kawalleck, P.1
  • 32
    • 0027639576 scopus 로고
    • A cDNA encoding S-adenosyl-L-methionine synthetase from poplar
    • 32 Doorsselaere, J.V. et al. (1993) A cDNA encoding S-adenosyl-L-methionine synthetase from poplar, Plant Physiol. 102, 1365-1366
    • (1993) Plant Physiol. , vol.102 , pp. 1365-1366
    • Doorsselaere, J.V.1
  • 33
    • 0028426943 scopus 로고
    • Differential accumulation of S-adenosylmethionine synthetase transcripts in response to salt stress
    • 33 Espartero, J., Pintor-Toro, J.A. and Pardo, J.M. (1994) Differential accumulation of S-adenosylmethionine synthetase transcripts in response to salt stress, Plant Mol. Biol. 25, 217-227
    • (1994) Plant Mol. Biol. , vol.25 , pp. 217-227
    • Espartero, J.1    Pintor-Toro, J.A.2    Pardo, J.M.3
  • 34
    • 0025616156 scopus 로고
    • Analysis of cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing
    • 34 Bell, E. and Malmberg, R.L. (1990) Analysis of 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
  • 35
    • 0027689369 scopus 로고
    • Cloning of tomato (Lycopersicon esculentum Mill.) arginine decarboxylase (ADC) gene and its expression during fruit ripening
    • 35 Rastogi, R., Dulson, J. and Rothstein, S. (1993) Cloning of tomato (Lycopersicon esculentum Mill.) arginine decarboxylase (ADC) gene and its expression during fruit ripening, Plant Physiol. 103, 829-834
    • (1993) Plant Physiol. , vol.103 , pp. 829-834
    • Rastogi, R.1    Dulson, J.2    Rothstein, S.3
  • 36
    • 0029360766 scopus 로고
    • Expression of arginine decarboxylase is induced during early fruit development and in young tissues of Pisum sativum (L.)
    • 36 Perez-Amador, M.A., Carbonell, J. and Granell, A. (1995) Expression of arginine decarboxylase is induced during early fruit development and in young tissues of Pisum sativum (L.), Plant Mol. Biol. 28, 997-1009
    • (1995) Plant Mol. Biol. , vol.28 , pp. 997-1009
    • Perez-Amador, M.A.1    Carbonell, J.2    Granell, A.3
  • 37
    • 0030019664 scopus 로고    scopus 로고
    • Molecular cloning and functional identification of a plant ornithine decarboxylase cDNA
    • 37 Michael, A.J. et al. (1996) Molecular cloning and functional identification of a plant ornithine decarboxylase cDNA, Biochem. J. 314, 241-248
    • (1996) Biochem. J. , vol.314 , pp. 241-248
    • Michael, A.J.1
  • 38
    • 0026949144 scopus 로고
    • Expression and sequence analysis of cDNAs induced during the early stages of tuberisation in different organs of potato plant (Solanum tuberosum)
    • 38 Taylor, M.A. et al. (1992) Expression and sequence analysis of cDNAs induced during the early stages of tuberisation in different organs of potato plant (Solanum tuberosum), Plant Mol. Biol. 20, 641-651
    • (1992) Plant Mol. Biol. , vol.20 , pp. 641-651
    • Taylor, M.A.1
  • 39
    • 0028519277 scopus 로고
    • Characterisation of the S-adenosylmethionine decarboxylase (SAMDC) gene of potato
    • 39 Mad Arif, S.A. et al. (1994) Characterisation of the S-adenosylmethionine decarboxylase (SAMDC) gene of potato, Plant Mol. Biol. 26, 327-338
    • (1994) Plant Mol. Biol. , vol.26 , pp. 327-338
    • Mad Arif, S.A.1
  • 40
    • 0029285357 scopus 로고
    • A spinach cDNA with homology to S-adenosylmethionine decarboxylase
    • 40 Bolle, C., Hermann, R.G. and Oelmuller, R. (1995) A spinach cDNA with homology to S-adenosylmethionine decarboxylase, Plant Physiol. 107, 1461-1462
    • (1995) Plant Physiol. , vol.107 , pp. 1461-1462
    • Bolle, C.1    Hermann, R.G.2    Oelmuller, R.3
  • 41
    • 0030095799 scopus 로고    scopus 로고
    • Isolation and characterisation of a Tritordeum cDNA encoding S-adenosylmethionine decarboxylase that is circadian-clock-regulated
    • 41 Dresselhaus, T. et al. (1996) Isolation and characterisation of a Tritordeum cDNA encoding S-adenosylmethionine decarboxylase that is circadian-clock-regulated, Plant Mol. Biol. 30, 1021-1033
    • (1996) Plant Mol. Biol. , vol.30 , pp. 1021-1033
    • Dresselhaus, T.1
  • 42
    • 0024845611 scopus 로고
    • Site of pyruvate formation and processing of mammalian S-adenosylmethionine decarboxylase proenzyme
    • 42 Stanley, B.A., Pegg, A.E. and Holm, I. (1989). Site of pyruvate formation and processing of mammalian S-adenosylmethionine decarboxylase proenzyme, J. Biol. Chem. 264, 21073-21079
    • (1989) J. Biol. Chem. , vol.264 , pp. 21073-21079
    • Stanley, B.A.1    Pegg, A.E.2    Holm, I.3
  • 43
    • 0026629831 scopus 로고
    • Structure and organisation of human S-adenosylmethionine decarboxylase
    • 43 Marie, S.C., Crozat, A. and Jänne, O.A. (1992) Structure and organisation of human S-adenosylmethionine decarboxylase, J. Biol. Chem. 267, 18915-18923
    • (1992) J. Biol. Chem. , vol.267 , pp. 18915-18923
    • Marie, S.C.1    Crozat, A.2    Jänne, O.A.3
  • 45
    • 0030596836 scopus 로고    scopus 로고
    • Spatial distribution and temporal accumulation of mRNA encoding diamine oxidase during lentil (Lens culinaris Medicus) seedling development
    • 45 Angelini, R. et al. (1996) Spatial distribution and temporal accumulation of mRNA encoding diamine oxidase during lentil (Lens culinaris Medicus) seedling development, Plant Sci. 119, 103-113
    • (1996) Plant Sci. , vol.119 , pp. 103-113
    • Angelini, R.1
  • 46
    • 0028798027 scopus 로고
    • Increased putrescine biosynthesis through transfer of mouse ornithine decarboxylase cDNA in carrot promotes somatic embryogenesis
    • 46 Bastola, D.R. and Minocha, S.C. (1995) Increased putrescine biosynthesis through transfer of mouse ornithine decarboxylase cDNA in carrot promotes somatic embryogenesis, Plant Physiol. 109, 63-71
    • (1995) Plant Physiol. , vol.109 , pp. 63-71
    • Bastola, D.R.1    Minocha, S.C.2
  • 47
    • 0028086622 scopus 로고
    • Expression of a human S-adenosylmethionine decarboxylase in transgenic tobacco and its effects on polyamine biosynthesis
    • 47 Woon Noh, E. and Minocha, S. (1994) Expression of a human S-adenosylmethionine decarboxylase in transgenic tobacco and its effects on polyamine biosynthesis, Transgenic Res. 3, 26-35
    • (1994) Transgenic Res. , vol.3 , pp. 26-35
    • Woon Noh, E.1    Minocha, S.2
  • 48
    • 0030037936 scopus 로고    scopus 로고
    • Potato plants expressing antisense and sense S-adenosylmethionine decarboxylase (SAMDC) transgenes show altered levels of polyamines and ethylene: Antisense plants display abnormal phenotypes
    • 48 Kumar, A. et al. (1996) Potato plants expressing antisense and sense S-adenosylmethionine decarboxylase (SAMDC) transgenes show altered levels of polyamines and ethylene: antisense plants display abnormal phenotypes, Plant J. 9, 147-158
    • (1996) Plant J. , vol.9 , pp. 147-158
    • Kumar, A.1
  • 49
    • 0000528668 scopus 로고
    • Inverse relationship between polyamine levels and the degree of phenotypic alteration induced by Ri-TL-DNA from Agrobacterium rhizogenes
    • 49 Martin-Tanguy, J. et al (1990) Inverse relationship between polyamine levels and the degree of phenotypic alteration induced by Ri-TL-DNA from Agrobacterium rhizogenes, Plant Physiol. 92, 912-918
    • (1990) Plant Physiol. , vol.92 , pp. 912-918
    • Martin-Tanguy, J.1
  • 50
    • 85030294635 scopus 로고    scopus 로고
    • Inducible overexpression of oat ADC in transgenic tobacco
    • in press
    • 50 Masgrau, C. et al. Inducible overexpression of oat ADC in transgenic tobacco, Plant J. (in press)
    • Plant J.
    • Masgrau, C.1
  • 51
    • 0000931399 scopus 로고
    • The ethylene signal transduction pathways in plants
    • 51 Ecker, J.R. (1994). The ethylene signal transduction pathways in plants, Science 268, 327-338
    • (1994) Science , vol.268 , pp. 327-338
    • Ecker, J.R.1
  • 53
    • 0027454149 scopus 로고
    • The role of dietary polyamines
    • 53 Bardoz, S. (1993) The role of dietary polyamines, Eur. J. Nutr. 47, 683-690
    • (1993) Eur. J. Nutr. , vol.47 , pp. 683-690
    • Bardoz, S.1


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