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Volumn 63, Issue 24, 2006, Pages 2881-2885

Antiquitin, a relatively unexplored member in the superfamily of aldehyde dehydrogenases with diversified physiological functions

Author keywords

Aldehyde dehydrogenase; Alpha aminoadipic semialdehyde; Antiquitin; Detoxification; Osmoregulation

Indexed keywords

ALDEHYDE DEHYDROGENASE; ANTIQUITIN; UNCLASSIFIED DRUG;

EID: 33846106324     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-006-6089-4     Document Type: Short Survey
Times cited : (25)

References (35)
  • 1
    • 3042551383 scopus 로고    scopus 로고
    • Role of human aldehyde dehydrogenases in endobiotic and xenobiotic metabolism
    • Vasiliou, V., Pappa, A. and Estey, T. (2004) Role of human aldehyde dehydrogenases in endobiotic and xenobiotic metabolism. Drug Metab. Rev. 36, 279-299
    • (2004) Drug Metab. Rev , vol.36 , pp. 279-299
    • Vasiliou, V.1    Pappa, A.2    Estey, T.3
  • 2
    • 0029110729 scopus 로고
    • Expression of the betaine aldehyde dehydrogenase gene in barley in response to osmotic stress and abscisic acid
    • Ishitani, M., Nakamura, T., Han, S. Y. and Takabe, T. (1995) Expression of the betaine aldehyde dehydrogenase gene in barley in response to osmotic stress and abscisic acid. Plant Mol. Biol. 27, 307-315
    • (1995) Plant Mol. Biol , vol.27 , pp. 307-315
    • Ishitani, M.1    Nakamura, T.2    Han, S.Y.3    Takabe, T.4
  • 3
    • 0006196934 scopus 로고
    • A mechanism of the indirect transfer of photosynthetically reduced nicotinamide adenine diuncleotide phosphate from the chloroplast to the cytoplasm
    • Kelly, G. J. and Gibb, M. (1973) A mechanism of the indirect transfer of photosynthetically reduced nicotinamide adenine diuncleotide phosphate from the chloroplast to the cytoplasm. Plant Physiol. 52, 674-676
    • (1973) Plant Physiol , vol.52 , pp. 674-676
    • Kelly, G.J.1    Gibb, M.2
  • 4
    • 0027302398 scopus 로고
    • Aldehyde dehydrogenase-derived omega-crystallins of squid and octopus. Specialization for lens expression
    • Zinovieva, R. D., Tomarev, S. I. and Piatigorsky, J. (1993) Aldehyde dehydrogenase-derived omega-crystallins of squid and octopus. Specialization for lens expression. J. Biol. Chem. 268, 11449-11455
    • (1993) J. Biol. Chem , vol.268 , pp. 11449-11455
    • Zinovieva, R.D.1    Tomarev, S.I.2    Piatigorsky, J.3
  • 5
    • 0029984181 scopus 로고    scopus 로고
    • A retinaldehyde dehydrogenase as a structural protein in a mammalian eye lens. Gene recruitment of eta-crystallin
    • Graham, C., Hodin, J. and Wistow, G. (1996) A retinaldehyde dehydrogenase as a structural protein in a mammalian eye lens. Gene recruitment of eta-crystallin. J. Biol. Chem. 271, 15623-15628
    • (1996) J. Biol. Chem , vol.271 , pp. 15623-15628
    • Graham, C.1    Hodin, J.2    Wistow, G.3
  • 6
    • 33846035569 scopus 로고    scopus 로고
    • An update of the ALDH gene family
    • Weiner, H, Plapp, B, Lindahl, R. and Maser, E, eds, Purdue University Press, Indiana
    • Sophos, N. A., Black, W. J. and Vasiliou, V. (2006) An update of the ALDH gene family. In: Enzymology and Molecular Biology of Carbonyl Metabolism, Vol. 12, pp. 3-7, Weiner, H., Plapp, B., Lindahl, R. and Maser, E. (eds.), Purdue University Press, Indiana
    • (2006) Enzymology and Molecular Biology of Carbonyl Metabolism , vol.12 , pp. 3-7
    • Sophos, N.A.1    Black, W.J.2    Vasiliou, V.3
  • 7
    • 0032534764 scopus 로고    scopus 로고
    • Sheep liver cytosolic aldehyde dehydrogenase: The structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases
    • Moore, S. A., Baker, H. M., Blythe, T. J., Kitson, K. E., Kitson, T. M. and Baker, E. N. (1998) Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases. Structure 6, 1541-1551
    • (1998) Structure , vol.6 , pp. 1541-1551
    • Moore, S.A.1    Baker, H.M.2    Blythe, T.J.3    Kitson, K.E.4    Kitson, T.M.5    Baker, E.N.6
  • 8
    • 0031570328 scopus 로고    scopus 로고
    • Structure of mitochondrial aldehyde dehydrogenase: The genetic component of ethanol aversion
    • Steinmetz, C. G., Xie, P., Weiner, H. and Hurley, T. D. (1997) Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion. Structure 5, 701-711
    • (1997) Structure , vol.5 , pp. 701-711
    • Steinmetz, C.G.1    Xie, P.2    Weiner, H.3    Hurley, T.D.4
  • 11
    • 33644750108 scopus 로고    scopus 로고
    • The first crystal structure of a thioacylenzyme intermediate in the ALDH family: New coenzyme conformation and relevance to catalysis
    • D'Ambrosio, K., Pailot, A., Talfournier, F., Didierjean, C., Benedetti, E., Aubry, A., Branlant, G. and Corbier, C. (2006) The first crystal structure of a thioacylenzyme intermediate in the ALDH family: new coenzyme conformation and relevance to catalysis. Biochemistry 45, 2978-2986
    • (2006) Biochemistry , vol.45 , pp. 2978-2986
    • D'Ambrosio, K.1    Pailot, A.2    Talfournier, F.3    Didierjean, C.4    Benedetti, E.5    Aubry, A.6    Branlant, G.7    Corbier, C.8
  • 12
    • 0032859206 scopus 로고    scopus 로고
    • Eukaryotic aldehyde dehydrogenase (ALDH) genes: Human polymorphisms, and recommended nomenclature based on divergent evolution and chromosomal mapping
    • Vasiliou, V., Bairoch, A., Tipton, K. F. and Nebert, D. W. (1999) Eukaryotic aldehyde dehydrogenase (ALDH) genes: human polymorphisms, and recommended nomenclature based on divergent evolution and chromosomal mapping. Pharmacogenetics 9, 421-434
    • (1999) Pharmacogenetics , vol.9 , pp. 421-434
    • Vasiliou, V.1    Bairoch, A.2    Tipton, K.F.3    Nebert, D.W.4
  • 13
    • 0028357270 scopus 로고
    • Homology between a human protein and a protein of the green garden pea
    • Lee, P., Kuhl, W., Gelbart, T., Kamimura, T., West, C. and Beutler, E. (1994) Homology between a human protein and a protein of the green garden pea. Genomics 21, 371-378
    • (1994) Genomics , vol.21 , pp. 371-378
    • Lee, P.1    Kuhl, W.2    Gelbart, T.3    Kamimura, T.4    West, C.5    Beutler, E.6
  • 15
    • 0031467111 scopus 로고    scopus 로고
    • An ancient conserved gene expressed in the human inner ear: Identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1)
    • Skvorak, A. B., Robertson, N. G., Yin, Y., Weremowicz, S., Her, H., Bieber, F. R., Beisel, K. W., Lynch, E. D., Beier, D. R. and Morton, C. C. (1997) An ancient conserved gene expressed in the human inner ear: identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1). Genomics 46, 191-199
    • (1997) Genomics , vol.46 , pp. 191-199
    • Skvorak, A.B.1    Robertson, N.G.2    Yin, Y.3    Weremowicz, S.4    Her, H.5    Bieber, F.R.6    Beisel, K.W.7    Lynch, E.D.8    Beier, D.R.9    Morton, C.C.10
  • 16
    • 0037051878 scopus 로고    scopus 로고
    • First purification of the antiquitin protein and demonstration of its enzymatic activity
    • Tang, W. K., Cheng, C. H. K. and Fong, W. P. (2002) First purification of the antiquitin protein and demonstration of its enzymatic activity. FEBS Lett. 516, 183-186
    • (2002) FEBS Lett , vol.516 , pp. 183-186
    • Tang, W.K.1    Cheng, C.H.K.2    Fong, W.P.3
  • 17
    • 21244500981 scopus 로고    scopus 로고
    • Seabream antiquitin: Molecular cloning, tissue distribution, subcellular localization and functional expression
    • Tang, W. K., Chan, C. B., Cheng, C. H. K. and Fong, W. P. (2005) Seabream antiquitin: molecular cloning, tissue distribution, subcellular localization and functional expression. FEBS Lett. 579, 3759-3764
    • (2005) FEBS Lett , vol.579 , pp. 3759-3764
    • Tang, W.K.1    Chan, C.B.2    Cheng, C.H.K.3    Fong, W.P.4
  • 18
    • 0242365646 scopus 로고    scopus 로고
    • Purification, N-terminal sequence determination and enzymatic characterization of antiquitin from the liver of grass carp
    • Chan, W. M., Tang, W. K., Cheng, C. H. K. and Fong, W. P. (2003) Purification, N-terminal sequence determination and enzymatic characterization of antiquitin from the liver of grass carp. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 136, 443-450
    • (2003) Comp. Biochem. Physiol. B Biochem. Mol. Biol , vol.136 , pp. 443-450
    • Chan, W.M.1    Tang, W.K.2    Cheng, C.H.K.3    Fong, W.P.4
  • 19
    • 0025463350 scopus 로고
    • Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted. Sequence and expression of three inducible genes
    • Guerrero, F. D., Jones, J. T. and Mullet, J. E. (1990) Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted. Sequence and expression of three inducible genes. Plant Mol. Biol. 15, 11-26
    • (1990) Plant Mol. Biol , vol.15 , pp. 11-26
    • Guerrero, F.D.1    Jones, J.T.2    Mullet, J.E.3
  • 21
    • 0029240389 scopus 로고
    • Molecular cloning and expression of a turgor-responsive gene in Brassica napus
    • Stroeher, V. L., Boothe, J. G. and Good, A. G. (1995) Molecular cloning and expression of a turgor-responsive gene in Brassica napus. Plant Mol. Biol. 27, 541-551
    • (1995) Plant Mol. Biol , vol.27 , pp. 541-551
    • Stroeher, V.L.1    Boothe, J.G.2    Good, A.G.3
  • 22
    • 17744381836 scopus 로고    scopus 로고
    • Detailed expression analysis of selected genes of the aldehyde dehydrogenase (ALDH) gene superfamily in Arabidopsis thaliana
    • Kirch, H. H., Schlingensiepen, S., Kotchoni, S., Sunkar, R. and Bartels, D. (2005) Detailed expression analysis of selected genes of the aldehyde dehydrogenase (ALDH) gene superfamily in Arabidopsis thaliana. Plant Mol. Biol. 57, 315-332
    • (2005) Plant Mol. Biol , vol.57 , pp. 315-332
    • Kirch, H.H.1    Schlingensiepen, S.2    Kotchoni, S.3    Sunkar, R.4    Bartels, D.5
  • 23
    • 0033083703 scopus 로고    scopus 로고
    • Identification and cDNA cloning of a protein abundantly expressed during apple fruit development
    • Yamada, K., Mori, H. and Yamaki, S. (1999) Identification and cDNA cloning of a protein abundantly expressed during apple fruit development. Plant Cell Physiol. 40, 198-204
    • (1999) Plant Cell Physiol , vol.40 , pp. 198-204
    • Yamada, K.1    Mori, H.2    Yamaki, S.3
  • 24
    • 0036095577 scopus 로고    scopus 로고
    • Aldh7B6 encodes a turgor-responsive aldehyde dehydrogenase homologue that is constitutively expressed in Tortula ruralis gametophytes
    • Chen, X., Zeng, Q. and Wood, A. J. (2002) Aldh7B6 encodes a turgor-responsive aldehyde dehydrogenase homologue that is constitutively expressed in Tortula ruralis gametophytes. Bryologist 105, 177-184
    • (2002) Bryologist , vol.105 , pp. 177-184
    • Chen, X.1    Zeng, Q.2    Wood, A.J.3
  • 25
    • 0030467846 scopus 로고    scopus 로고
    • Osmotic regulation of gene expression
    • Burg, M. B., Kwon, E. D. and Kultz, D. (1996) Osmotic regulation of gene expression. FASEB J. 10, 1598-1606
    • (1996) FASEB J , vol.10 , pp. 1598-1606
    • Burg, M.B.1    Kwon, E.D.2    Kultz, D.3
  • 26
    • 0036011086 scopus 로고    scopus 로고
    • Enhancement of tolerance of abiotic stress by metabolic engineering of betaines and other compatible solutes
    • Chen, T. H. and Murata, N. (2002) Enhancement of tolerance of abiotic stress by metabolic engineering of betaines and other compatible solutes. Curr. Opin. Plant Biol. 5, 250-257
    • (2002) Curr. Opin. Plant Biol , vol.5 , pp. 250-257
    • Chen, T.H.1    Murata, N.2
  • 27
    • 0025270591 scopus 로고
    • Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought
    • Weretilnyk, E. A. and Hanson, A. D. (1990) Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought. Proc. Natl. Acad. Sci. USA 87, 2745-2749
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2745-2749
    • Weretilnyk, E.A.1    Hanson, A.D.2
  • 28
    • 33745593025 scopus 로고    scopus 로고
    • Arabidopsis and tobacco plants ectopically expressing the soybean antiquitin-like ALDH7 gene display enhanced tolerance to drought, salinity, and oxidative stress
    • in press
    • Rodrigues, S. M., Andrade, M. O., Gomes, A. P., Damatta, F. M., Baracat-Pereira, M. C. and Fontes, E. P. (2006) Arabidopsis and tobacco plants ectopically expressing the soybean antiquitin-like ALDH7 gene display enhanced tolerance to drought, salinity, and oxidative stress. J. Exp. Bot. (in press)
    • (2006) J. Exp. Bot
    • Rodrigues, S.M.1    Andrade, M.O.2    Gomes, A.P.3    Damatta, F.M.4    Baracat-Pereira, M.C.5    Fontes, E.P.6
  • 29
    • 0033729510 scopus 로고    scopus 로고
    • The translational apparatus of Tortula ruralis: Polysomal retention of transcripts encoding the ribosomal proteins RPS14, RPS16 and RPL23 in desiccated and rehydrated gametophytes
    • Wood, A. J., Joel Duff, R. and Oliver, M. J. (2000) The translational apparatus of Tortula ruralis: polysomal retention of transcripts encoding the ribosomal proteins RPS14, RPS16 and RPL23 in desiccated and rehydrated gametophytes. J. Exp. Bot. 51, 1655-1662
    • (2000) J. Exp. Bot , vol.51 , pp. 1655-1662
    • Wood, A.J.1    Joel Duff, R.2    Oliver, M.J.3
  • 31
    • 33846089150 scopus 로고    scopus 로고
    • Lack of inducibility of antiquitin (ALDH7A1) in cultured human embryonic kidney (HEK293) cell under osmotic or oxidative stress
    • Weiner, H, Plapp, B, Lindahl, R. and Maser, E, eds, Purdue University Press, Indiana
    • Wong, W. Y., Cheng, C. H. K. and Fong, W. P. (2006) Lack of inducibility of antiquitin (ALDH7A1) in cultured human embryonic kidney (HEK293) cell under osmotic or oxidative stress. In: Enzymology and Molecular Biology of Carbonyl Metabolism, Vol. 12, pp. 96-103, Weiner, H., Plapp, B., Lindahl, R. and Maser, E. (eds.), Purdue University Press, Indiana
    • (2006) Enzymology and Molecular Biology of Carbonyl Metabolism , vol.12 , pp. 96-103
    • Wong, W.Y.1    Cheng, C.H.K.2    Fong, W.P.3
  • 33
    • 0032839335 scopus 로고    scopus 로고
    • Paroxysmal nocturnal hemoglobinuria: Analysis of the effects of mutant PIG-A on gene expression
    • Kanai, N., Vreeke, T. M. and Parker, C. J. (1999) Paroxysmal nocturnal hemoglobinuria: analysis of the effects of mutant PIG-A on gene expression. Am. J. Hematol. 61, 221-231
    • (1999) Am. J. Hematol , vol.61 , pp. 221-231
    • Kanai, N.1    Vreeke, T.M.2    Parker, C.J.3
  • 34
    • 0036999615 scopus 로고    scopus 로고
    • Salt and drought stress signal transduction in plants
    • Zhu, J. K. (2002) Salt and drought stress signal transduction in plants. Annu. Rev. Plant Biol. 53, 247-273
    • (2002) Annu. Rev. Plant Biol , vol.53 , pp. 247-273
    • Zhu, J.K.1
  • 35
    • 23044469902 scopus 로고    scopus 로고
    • Human aldehyde dehydrogenase 3A1 inhibits proliferation and promotes survival of human corneal epithelial cells
    • Pappa, A., Brown, D., Koutalos, Y., DeGregori, J., White, C. and Vasiliou, V. (2005) Human aldehyde dehydrogenase 3A1 inhibits proliferation and promotes survival of human corneal epithelial cells. J. Biol. Chem. 280, 27998-28006
    • (2005) J. Biol. Chem , vol.280 , pp. 27998-28006
    • Pappa, A.1    Brown, D.2    Koutalos, Y.3    DeGregori, J.4    White, C.5    Vasiliou, V.6


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