메뉴 건너뛰기




Volumn 348, Issue 4, 2006, Pages 1302-1309

Scallop lens Ω-crystallin (ALDH1A9): A novel tetrameric aldehyde dehydrogenase

Author keywords

crystallin; Aldehyde dehydrogenase; Lens crystallin; Mitochondria; Molecular mass; Multi angle laser light scattering; Scallop

Indexed keywords

ALDEHYDE DEHYDROGENASE; OMEGA CRYSTALLIN; TETRAMER;

EID: 33747887926     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.07.197     Document Type: Article
Times cited : (10)

References (47)
  • 2
    • 0023917935 scopus 로고
    • Lens crystallins: the evolution and expression of proteins for a highly specialized tissue
    • Wistow G.J., and Piatigorsky J. Lens crystallins: the evolution and expression of proteins for a highly specialized tissue. Annu. Rev. Biochem. 57 (1988) 479-504
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 479-504
    • Wistow, G.J.1    Piatigorsky, J.2
  • 3
    • 0024520027 scopus 로고
    • Enzyme/crystallins: gene sharing as an evolutionary strategy
    • Piatigorsky J., and Wistow G.J. Enzyme/crystallins: gene sharing as an evolutionary strategy. Cell 57 (1989) 197-199
    • (1989) Cell , vol.57 , pp. 197-199
    • Piatigorsky, J.1    Wistow, G.J.2
  • 6
    • 0024279563 scopus 로고
    • A novel crystallin from octopus lens
    • Chiou S.H. A novel crystallin from octopus lens. FEBS Lett. 241 (1988) 261-264
    • (1988) FEBS Lett. , vol.241 , pp. 261-264
    • Chiou, S.H.1
  • 7
    • 0026354479 scopus 로고
    • Crystallins of the octopus lens. Recruitment from detoxification enzymes
    • Tomarev S.I., Zinovieva R.D., and Piatigorsky J. Crystallins of the octopus lens. Recruitment from detoxification enzymes. J. Biol. Chem. 266 (1991) 24226-24231
    • (1991) J. Biol. Chem. , vol.266 , pp. 24226-24231
    • Tomarev, S.I.1    Zinovieva, R.D.2    Piatigorsky, J.3
  • 8
    • 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. Aldehyde dehydrogenase-derived omega-crystallins of squid and octopus. Specialization for lens expression. J. Biol. Chem. 268 (1993) 11449-11455
    • (1993) J. Biol. Chem. , vol.268 , pp. 11449-11455
    • Zinovieva, R.D.1    Tomarev, S.I.2    Piatigorsky, J.3
  • 9
    • 0026705801 scopus 로고
    • The muscle-derived lens of a squid bioluminescent organ is biochemically convergent with the ocular lens. Evidence for recruitment of aldehyde dehydrogenase as a predominant structural protein
    • Montgomery M.K., and McFall-Ngai M.J. The muscle-derived lens of a squid bioluminescent organ is biochemically convergent with the ocular lens. Evidence for recruitment of aldehyde dehydrogenase as a predominant structural protein. J. Biol. Chem. 267 (1992) 20999-21003
    • (1992) J. Biol. Chem. , vol.267 , pp. 20999-21003
    • Montgomery, M.K.1    McFall-Ngai, M.J.2
  • 10
    • 0025890262 scopus 로고
    • Lens protein expression in mammals: taxon-specificity and the recruitment of crystallins
    • Wistow G., and Kim H. Lens protein expression in mammals: taxon-specificity and the recruitment of crystallins. J. Mol. Evol. 32 (1991) 262-269
    • (1991) J. Mol. Evol. , vol.32 , pp. 262-269
    • Wistow, G.1    Kim, H.2
  • 11
    • 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. A retinaldehyde dehydrogenase as a structural protein in a mammalian eye lens. Gene recruitment of eta-crystallin. J. Biol. Chem. 271 (1996) 15623-15628
    • (1996) J. Biol. Chem. , vol.271 , pp. 15623-15628
    • Graham, C.1    Hodin, J.2    Wistow, G.3
  • 12
    • 0037461267 scopus 로고    scopus 로고
    • Crystal structure of eta-crystallin: adaptation of a class 1 aldehyde dehydrogenase for a new role in the eye lens
    • Bateman O.A., Purkiss A.G., van Montfort R., Slingsby C., Graham C., and Wistow G. Crystal structure of eta-crystallin: adaptation of a class 1 aldehyde dehydrogenase for a new role in the eye lens. Biochemistry 42 (2003) 4349-4356
    • (2003) Biochemistry , vol.42 , pp. 4349-4356
    • Bateman, O.A.1    Purkiss, A.G.2    van Montfort, R.3    Slingsby, C.4    Graham, C.5    Wistow, G.6
  • 13
    • 17744419979 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase gene superfamily: the 2002 update
    • Sophos N.A., and Vasiliou V. Aldehyde dehydrogenase gene superfamily: the 2002 update. Chem. Biol. Interact. 143-144 (2003) 5-22
    • (2003) Chem. Biol. Interact. , vol.143-144 , pp. 5-22
    • Sophos, N.A.1    Vasiliou, V.2
  • 14
    • 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. Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases. Structure 6 (1998) 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
  • 15
    • 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. Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion. Structure 5 (1997) 701-711
    • (1997) Structure , vol.5 , pp. 701-711
    • Steinmetz, C.G.1    Xie, P.2    Weiner, H.3    Hurley, T.D.4
  • 16
    • 0015022316 scopus 로고
    • Theory of transparency of the eye
    • Benedek G.B. Theory of transparency of the eye. Applied Optics 10 (1971) 459-473
    • (1971) Applied Optics , vol.10 , pp. 459-473
    • Benedek, G.B.1
  • 17
    • 0038312706 scopus 로고
    • Biological-physical basis of lens transparency
    • McDevitt D.S. (Ed), Academic Press, New York
    • Bettelheim F.A., and Siew E.L. Biological-physical basis of lens transparency. In: McDevitt D.S. (Ed). Cell Biology of the Eye (1982), Academic Press, New York 243-297
    • (1982) Cell Biology of the Eye , pp. 243-297
    • Bettelheim, F.A.1    Siew, E.L.2
  • 18
    • 0020678719 scopus 로고
    • Short-range order of crystallin proteins accounts for eye lens transparency
    • Delaye M., and Tardieu A. Short-range order of crystallin proteins accounts for eye lens transparency. Nature 302 (1983) 415-417
    • (1983) Nature , vol.302 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 19
    • 3843153030 scopus 로고    scopus 로고
    • Are molecular weights of proteins determined by superose 12 column chromatography correct?
    • Lee S.C., and Whitaker J.R. Are molecular weights of proteins determined by superose 12 column chromatography correct?. J. Agric. Food Chem. 52 (2004) 4948-4952
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 4948-4952
    • Lee, S.C.1    Whitaker, J.R.2
  • 20
    • 0033433951 scopus 로고    scopus 로고
    • Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms
    • Ni L., Zhou J., Hurley T.D., and Weiner H. Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Sci. 8 (1999) 2784-2790
    • (1999) Protein Sci. , vol.8 , pp. 2784-2790
    • Ni, L.1    Zhou, J.2    Hurley, T.D.3    Weiner, H.4
  • 21
    • 0030571043 scopus 로고    scopus 로고
    • Size-exclusion chromatography with on-line light-scattering, absorbance, refractive index detectors for studying proteins and their interactions
    • Wen J., Arakawa T., and Philo J.S. Size-exclusion chromatography with on-line light-scattering, absorbance, refractive index detectors for studying proteins and their interactions. Anal. Biochem. 240 (1996) 155-166
    • (1996) Anal. Biochem. , vol.240 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 22
    • 4444243454 scopus 로고    scopus 로고
    • Determination of molecular masses of proteins in solution: implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory
    • Folta-Stogniew E., and Williams K. Determination of molecular masses of proteins in solution: implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory. J. Biolmol. Tech. 10 (1999) 51-63
    • (1999) J. Biolmol. Tech. , vol.10 , pp. 51-63
    • Folta-Stogniew, E.1    Williams, K.2
  • 23
    • 0346724680 scopus 로고    scopus 로고
    • Human aldehyde dehydrogenase 3A1 (ALDH3A1): biochemical characterization and immunohistochemical localization in the cornea
    • Pappa A., Estey T., Manzer R., Brown D., and Vasiliou V. Human aldehyde dehydrogenase 3A1 (ALDH3A1): biochemical characterization and immunohistochemical localization in the cornea. Biochem. J. 376 (2003) 615-623
    • (2003) Biochem. J. , vol.376 , pp. 615-623
    • Pappa, A.1    Estey, T.2    Manzer, R.3    Brown, D.4    Vasiliou, V.5
  • 24
    • 0012869069 scopus 로고    scopus 로고
    • Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA
    • Manzer R., Qamar L., Estey T., Pappa A., Petersen D.R., and Vasiliou V. Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA. DNA Cell Biol. 22 (2003) 329-338
    • (2003) DNA Cell Biol. , vol.22 , pp. 329-338
    • Manzer, R.1    Qamar, L.2    Estey, T.3    Pappa, A.4    Petersen, D.R.5    Vasiliou, V.6
  • 25
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 27
  • 28
    • 33747875674 scopus 로고    scopus 로고
    • J. Felsentein, Phylogeny Inference Package, Version 3.5c, Department of Genetics, University of Washington, Seattle, Washington, 1993.
  • 30
    • 0025217478 scopus 로고
    • Sequence of the precursor of bovine liver mitochondrial aldehyde dehydrogenase as determined from its cDNA, its gene, its functionality
    • Guan K.L., and Weiner H. Sequence of the precursor of bovine liver mitochondrial aldehyde dehydrogenase as determined from its cDNA, its gene, its functionality. Arch. Biochem. Biophys. 277 (1990) 351-360
    • (1990) Arch. Biochem. Biophys. , vol.277 , pp. 351-360
    • Guan, K.L.1    Weiner, H.2
  • 31
    • 0029788381 scopus 로고    scopus 로고
    • The role of positive charges and structural segments in the presequence of rat liver aldehyde dehydrogenase in import into mitochondria
    • Hammen P.K., Waltner M., Hahnemann B., Heard T.S., and Weiner H. The role of positive charges and structural segments in the presequence of rat liver aldehyde dehydrogenase in import into mitochondria. J. Biol. Chem. 271 (1996) 21041-21048
    • (1996) J. Biol. Chem. , vol.271 , pp. 21041-21048
    • Hammen, P.K.1    Waltner, M.2    Hahnemann, B.3    Heard, T.S.4    Weiner, H.5
  • 32
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros M.G., and Vincens P. Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur. J. Biochem. 241 (1996) 779-786
    • (1996) Eur. J. Biochem. , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 34
    • 0023691542 scopus 로고
    • Squid major lens polypeptides are homologous to glutathione S-transferases subunits
    • Tomarev S.I., and Zinovieva R.D. Squid major lens polypeptides are homologous to glutathione S-transferases subunits. Nature 336 (1988) 86-88
    • (1988) Nature , vol.336 , pp. 86-88
    • Tomarev, S.I.1    Zinovieva, R.D.2
  • 35
    • 0030032495 scopus 로고    scopus 로고
    • Lens crystallins of invertebrates-diversity and recruitment from detoxification enzymes and novel proteins
    • Tomarev S.I., and Piatigorsky J. Lens crystallins of invertebrates-diversity and recruitment from detoxification enzymes and novel proteins. Eur. J. Biochem. 235 (1996) 449-465
    • (1996) Eur. J. Biochem. , vol.235 , pp. 449-465
    • Tomarev, S.I.1    Piatigorsky, J.2
  • 36
    • 0018136162 scopus 로고
    • Ellipsosomes: organelles containing a cytochrome-like pigment in the retinal cones of certain fishes
    • MacNichol Jr. E.F., Kunz Y.W., Levine J.S., Harosi F.I., and Collins B.A. Ellipsosomes: organelles containing a cytochrome-like pigment in the retinal cones of certain fishes. Science 200 (1978) 549-552
    • (1978) Science , vol.200 , pp. 549-552
    • MacNichol Jr., E.F.1    Kunz, Y.W.2    Levine, J.S.3    Harosi, F.I.4    Collins, B.A.5
  • 37
    • 0028942423 scopus 로고
    • Retinal ellipsosomes: morphology, development, identification, and comparison with oil droplets
    • Nag T.C., and Bhattacharjee J. Retinal ellipsosomes: morphology, development, identification, and comparison with oil droplets. Cell Tissue Res. 279 (1995) 633-637
    • (1995) Cell Tissue Res. , vol.279 , pp. 633-637
    • Nag, T.C.1    Bhattacharjee, J.2
  • 38
    • 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. Human aldehyde dehydrogenase 3A1 inhibits proliferation and promotes survival of human corneal epithelial cells. J. Biol. Chem. 280 (2005) 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
  • 39
    • 0032553123 scopus 로고    scopus 로고
    • The molecular chaperone alphaA-crystallin enhances lens epithelial cell growth and resistance to UVA stress
    • Andley U.P., Song Z., Wawrousek E.F., and Bassnett S. The molecular chaperone alphaA-crystallin enhances lens epithelial cell growth and resistance to UVA stress. J. Biol. Chem. 273 (1998) 31252-31261
    • (1998) J. Biol. Chem. , vol.273 , pp. 31252-31261
    • Andley, U.P.1    Song, Z.2    Wawrousek, E.F.3    Bassnett, S.4
  • 40
    • 2442681777 scopus 로고    scopus 로고
    • Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis
    • Mao Y.W., Liu J.P., Xiang H., and Li D.W. Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis. Cell Death Differ. 11 (2004) 512-526
    • (2004) Cell Death Differ. , vol.11 , pp. 512-526
    • Mao, Y.W.1    Liu, J.P.2    Xiang, H.3    Li, D.W.4
  • 41
    • 33645538666 scopus 로고    scopus 로고
    • Caspase-dependent secondary lens fiber cell disintegration in {alpha}A-/{alpha}B-crystallin double-knockout mice
    • Morozov V., and Wawrousek E.F. Caspase-dependent secondary lens fiber cell disintegration in {alpha}A-/{alpha}B-crystallin double-knockout mice. Development 133 (2006) 813-821
    • (2006) Development , vol.133 , pp. 813-821
    • Morozov, V.1    Wawrousek, E.F.2
  • 42
    • 0037325497 scopus 로고    scopus 로고
    • Alpha-crystallin
    • Horwitz J. Alpha-crystallin. Exp. Eye Res. 76 (2003) 145-153
    • (2003) Exp. Eye Res. , vol.76 , pp. 145-153
    • Horwitz, J.1
  • 43
    • 0024095133 scopus 로고
    • Duck lens epsilon-crystallin and lactate dehydrogenase B4 are identical: a single-copy gene product with two distinct functions
    • Hendriks W., Mulders J.W., Bibby M.A., Slingsby C., Bloemendal H., and de Jong W.W. Duck lens epsilon-crystallin and lactate dehydrogenase B4 are identical: a single-copy gene product with two distinct functions. Proc. Natl. Acad. Sci. USA 85 (1988) 7114-7118
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7114-7118
    • Hendriks, W.1    Mulders, J.W.2    Bibby, M.A.3    Slingsby, C.4    Bloemendal, H.5    de Jong, W.W.6
  • 45
    • 0034764149 scopus 로고    scopus 로고
    • Enigma of the abundant water-soluble cytoplasmic proteins of the cornea: the "refracton" hypothesis
    • Piatigorsky J. Enigma of the abundant water-soluble cytoplasmic proteins of the cornea: the "refracton" hypothesis. Cornea 20 (2001) 853-858
    • (2001) Cornea , vol.20 , pp. 853-858
    • Piatigorsky, J.1
  • 46
    • 0026754720 scopus 로고
    • Lens crystallins. Innovation associated with changes in gene regulation
    • Piatigorsky J. Lens crystallins. Innovation associated with changes in gene regulation. J. Biol. Chem. 267 (1992) 4277-4280
    • (1992) J. Biol. Chem. , vol.267 , pp. 4277-4280
    • Piatigorsky, J.1
  • 47
    • 17844382395 scopus 로고    scopus 로고
    • Molecular cloning, baculovirus expression, tissue distribution of the zebrafish aldehyde dehydrogenase 2
    • Lassen N., Estey T., Tanguay R.L., Pappa A., Reimers M.J., and Vasiliou V. Molecular cloning, baculovirus expression, tissue distribution of the zebrafish aldehyde dehydrogenase 2. Drug Metab. Dispos. 33 (2005) 649-656
    • (2005) Drug Metab. Dispos. , vol.33 , pp. 649-656
    • Lassen, N.1    Estey, T.2    Tanguay, R.L.3    Pappa, A.4    Reimers, M.J.5    Vasiliou, V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.