메뉴 건너뛰기




Volumn 247, Issue 3, 1997, Pages 792-800

Further characterization of a rat hepatoma-derived aldose-reductase-like protein: Organ distribution and modulation in vitro

Author keywords

Aldose reductase like protein; Rat hepatoma; Two dimensional electrophoresis

Indexed keywords

ALDEHYDE REDUCTASE; FIBROBLAST GROWTH FACTOR 1; GLUCOSE; LENS PROTEIN; MARKER; METHYLNITROSOUREA;

EID: 0030750775     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00792.x     Document Type: Article
Times cited : (19)

References (70)
  • 1
    • 0016637146 scopus 로고
    • Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissue. A novel approach to testing for induced point mutations in mammals
    • Klose, J. (1975) Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissue. A novel approach to testing for induced point mutations in mammals, Humangenetik 26, 231-243.
    • (1975) Humangenetik , vol.26 , pp. 231-243
    • Klose, J.1
  • 2
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H. (1975) High resolution two-dimensional electrophoresis of proteins, J. Biol. Chem. 250, 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 3
    • 0029020259 scopus 로고
    • Two-dimensional electrophoresis of proteins: An updated protocol and implications for a functional analysis of the genome
    • Klose, J. & Kobalz, U. (1995) Two-dimensional electrophoresis of proteins: An updated protocol and implications for a functional analysis of the genome, Electrophoresis 16, 1034-1059.
    • (1995) Electrophoresis , vol.16 , pp. 1034-1059
    • Klose, J.1    Kobalz, U.2
  • 4
    • 0018648853 scopus 로고
    • Trace polypeptides in cellular extracts and human body fluids detected by two-dimensional elctrophoresis and a highly sensitive silver stain
    • Merril, C. R., Switzer, R. & Van Keuren, M. L. (1979) Trace polypeptides in cellular extracts and human body fluids detected by two-dimensional elctrophoresis and a highly sensitive silver stain, Proc. Natl Acad. Sci. USA 76, 4335-4339.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4335-4339
    • Merril, C.R.1    Switzer, R.2    Van Keuren, M.L.3
  • 5
    • 0025312701 scopus 로고
    • Analysis by high-resolution two-dimensional electrophoresis of differentiation-dependent alterations in cytosolic protein pattern of HL60 leukemic cells
    • Jungblut, P. R. & Seifert, F. (1990) Analysis by high-resolution two-dimensional electrophoresis of differentiation-dependent alterations in cytosolic protein pattern of HL60 leukemic cells, J. Biochem. Biophys. Methods 21, 47-58.
    • (1990) J. Biochem. Biophys. Methods , vol.21 , pp. 47-58
    • Jungblut, P.R.1    Seifert, F.2
  • 6
    • 0018350337 scopus 로고
    • Two-dimensional gel electrophoretic comparison of proteins of nuclear fractions of normal liver and Novikoff hepatoma
    • Takami, H. & Busch, H. (1979) Two-dimensional gel electrophoretic comparison of proteins of nuclear fractions of normal liver and Novikoff hepatoma, Cancer Res. 39, 507-518.
    • (1979) Cancer Res. , vol.39 , pp. 507-518
    • Takami, H.1    Busch, H.2
  • 7
    • 0018391857 scopus 로고
    • Two-dimensional gel electrophoresis of cytosol phosphoproteins of Novikoff hepatoma and regenerating liver
    • Wu, B. C., Spohn, W. H. & Busch, H. (1979) Two-dimensional gel electrophoresis of cytosol phosphoproteins of Novikoff hepatoma and regenerating liver, Cancer Res. 39, 116-122.
    • (1979) Cancer Res. , vol.39 , pp. 116-122
    • Wu, B.C.1    Spohn, W.H.2    Busch, H.3
  • 8
    • 0018747228 scopus 로고
    • Comparison of salt-extractable nuclear proteins of regenerating liver, fetal liver, and Morris hepatomas 9618 A and 3924 A
    • Takami, H., Busch, F. N., Morris, H. P. & Busch, H. (1979) Comparison of salt-extractable nuclear proteins of regenerating liver, fetal liver, and Morris hepatomas 9618 A and 3924 A, Cancer Res. 39, 2096-2105.
    • (1979) Cancer Res. , vol.39 , pp. 2096-2105
    • Takami, H.1    Busch, F.N.2    Morris, H.P.3    Busch, H.4
  • 9
    • 0022384909 scopus 로고
    • Detection of the changes in cellular proteins in regenerating rat liver by high-resolution two-dimensional gel electrophoresis
    • Kadofuku, T. & Sato, T. (1985) Detection of the changes in cellular proteins in regenerating rat liver by high-resolution two-dimensional gel electrophoresis, J. Chromatogr. 343, 51-58.
    • (1985) J. Chromatogr. , vol.343 , pp. 51-58
    • Kadofuku, T.1    Sato, T.2
  • 10
    • 0022655780 scopus 로고
    • Sequential analysis of chemically induced hepatoma development by two-dimensional gel electrophoresis
    • Wirth, P. J., Benjamin, T. Schwartz, D. M. & Thorgeirsson, S. S. (1986) Sequential analysis of chemically induced hepatoma development by two-dimensional gel electrophoresis, Cancer Res. 46, 400-413.
    • (1986) Cancer Res. , vol.46 , pp. 400-413
    • Wirth, P.J.1    Benjamin, T.2    Schwartz, D.M.3    Thorgeirsson, S.S.4
  • 11
    • 0026624920 scopus 로고
    • Variant protein patterns in hepatomas and transformed liver cell lines as determined by two-dimensional gel electrophoresis
    • Zeindl-Eberhart, E. & Rabes, H. M. (1992) Variant protein patterns in hepatomas and transformed liver cell lines as determined by two-dimensional gel electrophoresis, Carcinogenesis 13, 1177-1183.
    • (1992) Carcinogenesis , vol.13 , pp. 1177-1183
    • Zeindl-Eberhart, E.1    Rabes, H.M.2
  • 12
    • 0028287568 scopus 로고
    • Expression of tumor-associated protein variants in chemically induced rat hepatomas and transformed rat liver cell lines determined by two-dimensional gel electrophoresis
    • Zeindl-Eberhart, E., Jungblut, P. R. & Rabes, H. M. (1994) Expression of tumor-associated protein variants in chemically induced rat hepatomas and transformed rat liver cell lines determined by two-dimensional gel electrophoresis. Electrophoresis 15, 372-381.
    • (1994) Electrophoresis , vol.15 , pp. 372-381
    • Zeindl-Eberhart, E.1    Jungblut, P.R.2    Rabes, H.M.3
  • 13
    • 0028335907 scopus 로고
    • Identification of tumor-associated protein variants during rat hepatocarcinogenesis
    • Zeindl-Eberhart, E., Jungblut, P. R., Otto, A. & Rabes, H. M. (1994) Identification of tumor-associated protein variants during rat hepatocarcinogenesis, J. Biol. Chem. 269, 14 589-14 594.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14589-14594
    • Zeindl-Eberhart, E.1    Jungblut, P.R.2    Otto, A.3    Rabes, H.M.4
  • 14
    • 0028346373 scopus 로고
    • A delayed-early gene activated by fibroblast growth factor-1 encodes a protein related to aldose reductase
    • Donohue, P. J., Alberts, G. F., Hampton, B. S. & Winkles, J. A. (1994) A delayed-early gene activated by fibroblast growth factor-1 encodes a protein related to aldose reductase, J. Biol. Chem. 269, 8604-8609.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8604-8609
    • Donohue, P.J.1    Alberts, G.F.2    Hampton, B.S.3    Winkles, J.A.4
  • 15
    • 0022626415 scopus 로고
    • Cell cycle-dependent initiation of adenosine triphosphatase-deficient populations in adult rat liver by a single dose of N-methyl-N-nitrosourea
    • Rabes, H. M., Müller, L., Hartmann, A., Kerler, R. & Schuster, C. (1986) Cell cycle-dependent initiation of adenosine triphosphatase-deficient populations in adult rat liver by a single dose of N-methyl-N-nitrosourea, Cancer Res. 46, 645-650.
    • (1986) Cancer Res. , vol.46 , pp. 645-650
    • Rabes, H.M.1    Müller, L.2    Hartmann, A.3    Kerler, R.4    Schuster, C.5
  • 16
    • 0023848684 scopus 로고
    • Preneoplastic rat liver cells in vitro: Slow progression without promoters, hormones, or growth factors
    • Kerler, R. & Rabes, H. M. (1988) Preneoplastic rat liver cells in vitro: slow progression without promoters, hormones, or growth factors, J. Cancer Res. Clin. Oncol. 114, 113-123.
    • (1988) J. Cancer Res. Clin. Oncol. , vol.114 , pp. 113-123
    • Kerler, R.1    Rabes, H.M.2
  • 17
    • 0029986330 scopus 로고
    • Karyotype evolution of the clonal rat liver cell line CL 52 during progression in vitro and in vivo
    • Kerler, R. & Rabes, H. M. (1986) Karyotype evolution of the clonal rat liver cell line CL 52 during progression in vitro and in vivo, Cancer Genet. Cytogenet. 87, 140-147.
    • (1986) Cancer Genet. Cytogenet. , vol.87 , pp. 140-147
    • Kerler, R.1    Rabes, H.M.2
  • 19
    • 0027202755 scopus 로고
    • Altered aldose reductase gene regulation in cultured human retinal pigment epithelial cells
    • Henry, D. N., Del Monte, M., Greene, D. A. & Killen, P. D. (1993) Altered aldose reductase gene regulation in cultured human retinal pigment epithelial cells, J. Clin. Invest. 92, 617-623.
    • (1993) J. Clin. Invest. , vol.92 , pp. 617-623
    • Henry, D.N.1    Del Monte, M.2    Greene, D.A.3    Killen, P.D.4
  • 20
    • 0023575451 scopus 로고
    • Analysis of protein patterns from different organs and cell fractions of trisomy 19 mice
    • Zeindl-Eberhart, E., Grohé, G. & Klose, J. (1987) Analysis of protein patterns from different organs and cell fractions of trisomy 19 mice, Hum. Genet. 77, 371-378.
    • (1987) Hum. Genet. , vol.77 , pp. 371-378
    • Zeindl-Eberhart, E.1    Grohé, G.2    Klose, J.3
  • 21
    • 0342565899 scopus 로고
    • High resolution of complex protein solutions by two-dimensional electrophoresis
    • (Tschesche, H., ed.) de Gruyter, Berlin
    • Klose, J. (1983) High resolution of complex protein solutions by two-dimensional electrophoresis, in Modern methods in protein chemistry. Review articles (Tschesche, H., ed.) pp. 49-78, de Gruyter, Berlin.
    • (1983) Modern Methods in Protein Chemistry. Review Articles , pp. 49-78
    • Klose, J.1
  • 22
    • 0018084288 scopus 로고
    • Analytical techniques for cell fractions XXI. Two-dimensional analysis of serum and tissue proteins: Multiple isoelectric focussing
    • Anderson, N. G. & Anderson, N. L. (1978) Analytical techniques for cell fractions XXI. Two-dimensional analysis of serum and tissue proteins: multiple isoelectric focussing. Anal. Biochem. 85, 331-340.
    • (1978) Anal. Biochem. , vol.85 , pp. 331-340
    • Anderson, N.G.1    Anderson, N.L.2
  • 23
    • 0018167339 scopus 로고
    • Analytical techniques for cell fractions XXII. Two-dimensional analysis of serum and tissue proteins: Multiple gradient-slap gel electrophoresis
    • Anderson, N. L. & Anderson, N. G. (1978) Analytical techniques for cell fractions XXII. Two-dimensional analysis of serum and tissue proteins: multiple gradient-slap gel electrophoresis, Anal. Biochem. 85, 341-354.
    • (1978) Anal. Biochem. , vol.85 , pp. 341-354
    • Anderson, N.L.1    Anderson, N.G.2
  • 24
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications, Proc. Natl Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 25
    • 0025142558 scopus 로고
    • Blotting efficiency investigated by using two-dimensional electrophoresis, hydrophobic membranes and proteins from different sources
    • Jungblut, P., Eckerskorn, C., Lottspeich, F. & Klose, J. (1990) Blotting efficiency investigated by using two-dimensional electrophoresis, hydrophobic membranes and proteins from different sources, Electrophoresis 11, 581-588.
    • (1990) Electrophoresis , vol.11 , pp. 581-588
    • Jungblut, P.1    Eckerskorn, C.2    Lottspeich, F.3    Klose, J.4
  • 26
    • 0026580898 scopus 로고
    • Internal protein sequence analysis: Enzymatic digestion for less than 10 μg of protein bound to polyvinylidene difluoride or nitro-cellulose membranes
    • Fernandez, J., DeMott, M., Atherton, D. & Mische, S. M. (1992) Internal protein sequence analysis: Enzymatic digestion for less than 10 μg of protein bound to polyvinylidene difluoride or nitro-cellulose membranes, Anal. Biochem. 201, 255-264.
    • (1992) Anal. Biochem. , vol.201 , pp. 255-264
    • Fernandez, J.1    DeMott, M.2    Atherton, D.3    Mische, S.M.4
  • 27
    • 0015434010 scopus 로고
    • Growth kinetics of diethylnitrosamine-induced enzyme-deficient preneoplastic liver cell populations in vivo and in vitro
    • Rabes, H. M., Scholze, P. & Jantsch, B. (1972) Growth kinetics of diethylnitrosamine-induced enzyme-deficient preneoplastic liver cell populations in vivo and in vitro, Cancer Res. 32, 2577-2586.
    • (1972) Cancer Res. , vol.32 , pp. 2577-2586
    • Rabes, H.M.1    Scholze, P.2    Jantsch, B.3
  • 28
    • 0019423594 scopus 로고
    • Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: A comparison between ABC and unlabelled PAP procedures
    • Hsu, S. M., Raine, L. & Fanger, H. (1981) Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabelled PAP procedures, J. Histochem. Cytochem. 29, 577-580.
    • (1981) J. Histochem. Cytochem. , vol.29 , pp. 577-580
    • Hsu, S.M.1    Raine, L.2    Fanger, H.3
  • 30
    • 0025829982 scopus 로고
    • Purification and characterization of the recombinant human aldose reductase expressed in baculovirus system
    • Nishimura, C., Yamaoka, T., Mizutani, M., Yamashita, K., Akera, T. & Tanimoto, T. (1991) Purification and characterization of the recombinant human aldose reductase expressed in baculovirus system, Biochim. Biophys. Acta 1078, 171-178.
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 171-178
    • Nishimura, C.1    Yamaoka, T.2    Mizutani, M.3    Yamashita, K.4    Akera, T.5    Tanimoto, T.6
  • 32
    • 0024333867 scopus 로고
    • The aldoketo reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases
    • Bohren, K. M., Bullock, B., Wermuth, B. & Gabbay, K. H. (1989) The aldoketo reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases, J. Biol. Chem. 264, 9547-9551.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9547-9551
    • Bohren, K.M.1    Bullock, B.2    Wermuth, B.3    Gabbay, K.H.4
  • 33
    • 0025835877 scopus 로고
    • Cloning and sequencing of the cDNA for rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase
    • Pawlowski, J. E., Huizinga, M. & Penning, T. M. (1991) Cloning and sequencing of the cDNA for rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase, J. Biol. Chem. 266, 8820-8825.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8820-8825
    • Pawlowski, J.E.1    Huizinga, M.2    Penning, T.M.3
  • 34
    • 0025782902 scopus 로고
    • An ABA and GA modulated gene expressed in the barley embryo encodes an aldose reductase related protein
    • Bartels, D., Engelhardt, K., Roncarati, R., Schneider, K., Rotter, M. & Salamini, F. (1991) An ABA and GA modulated gene expressed in the barley embryo encodes an aldose reductase related protein. AMBO J. 10, 1037-1043.
    • (1991) AMBO J. , vol.10 , pp. 1037-1043
    • Bartels, D.1    Engelhardt, K.2    Roncarati, R.3    Schneider, K.4    Rotter, M.5    Salamini, F.6
  • 36
    • 0028970887 scopus 로고
    • 1.7 Å structure of FR-1, a fibroblast growth factor-induced member of the aldoketo reductase family. Complexed with coenzyme and inhibitor
    • Wilson, D. K., Nakano, T., Petrash, J. M. & Quiocho, F. A. (1995) 1.7 Å structure of FR-1, a fibroblast growth factor-induced member of the aldoketo reductase family. Complexed with coenzyme and inhibitor. Biochemistry 34, 14 323-14 330.
    • (1995) Biochemistry , vol.34 , pp. 14323-14330
    • Wilson, D.K.1    Nakano, T.2    Petrash, J.M.3    Quiocho, F.A.4
  • 37
    • 0028797794 scopus 로고
    • Xenobiotic carbonyl reduction and physiological steroid oxidoreduction
    • Maser, E. (1995) Xenobiotic carbonyl reduction and physiological steroid oxidoreduction, Biochem. Pharmacol. 49, 421-440.
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 421-440
    • Maser, E.1
  • 39
    • 0029781857 scopus 로고    scopus 로고
    • Characterisation of the osmotic response element of the human aldose reductase gene pomotor
    • Ruepp, B., Bohren, K. M. & Gabbay, K. H. (1996) Characterisation of the osmotic response element of the human aldose reductase gene pomotor, Proc. Natl Acad. Sci. USA 93, 8624-8629.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8624-8629
    • Ruepp, B.1    Bohren, K.M.2    Gabbay, K.H.3
  • 40
    • 0026065134 scopus 로고
    • Resolving isoforms of aldose reductase by preparative isoelectric focusing in the Rotofor
    • Petrash, J. M., DeLucas, L. J., Bowling, E. & Egen, N. (1991) Resolving isoforms of aldose reductase by preparative isoelectric focusing in the Rotofor, Electrophoresis 12, 84-90.
    • (1991) Electrophoresis , vol.12 , pp. 84-90
    • Petrash, J.M.1    DeLucas, L.J.2    Bowling, E.3    Egen, N.4
  • 41
    • 0025341976 scopus 로고
    • Cloning and prokaryotic expression of a biologically active human placental aldose reductase
    • Grundmann, U., Bohn, H., Obermeier, R. & Amann, E. (1990) Cloning and prokaryotic expression of a biologically active human placental aldose reductase, DNA Cell Biol. 9, 149-157.
    • (1990) DNA Cell Biol. , vol.9 , pp. 149-157
    • Grundmann, U.1    Bohn, H.2    Obermeier, R.3    Amann, E.4
  • 42
    • 0025871012 scopus 로고
    • Localization, isolation and properties of three NADPH-dependent aldehyde reducing enzymes from dog kidney
    • Ohta, M., Tanimoto, T. & Tanaka, A. (1991) Localization, isolation and properties of three NADPH-dependent aldehyde reducing enzymes from dog kidney. Biochim. Biophys. Acta 1078, 395-403.
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 395-403
    • Ohta, M.1    Tanimoto, T.2    Tanaka, A.3
  • 43
    • 0028302333 scopus 로고
    • A qualitative and quantitative protein database approach identifies individual and groups of functionally related proteins that are differentially regulated in simian virus 40 (SV40) transformed human keratinocytes: An overview of the functional changes associated with the transformed phenotype
    • Celis, J. E. & Olson, E. (1994) A qualitative and quantitative protein database approach identifies individual and groups of functionally related proteins that are differentially regulated in simian virus 40 (SV40) transformed human keratinocytes: an overview of the functional changes associated with the transformed phenotype, Electrophoresis 15, 309-344.
    • (1994) Electrophoresis , vol.15 , pp. 309-344
    • Celis, J.E.1    Olson, E.2
  • 44
    • 0021099275 scopus 로고
    • Purification and characterization of two aldose reductase isoenzymes from rabbit muscle
    • Cromlish, J. A. & Flynn, T. G. (1983) Purification and characterization of two aldose reductase isoenzymes from rabbit muscle. J. Biol. Chem. 258, 3416-3424.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3416-3424
    • Cromlish, J.A.1    Flynn, T.G.2
  • 45
    • 0029610824 scopus 로고
    • Tissue-specific expression of two aldose-reductase-like genes in mice: Abundant expression of mouse vas deferens protein and fibroblast growth factor-regulated protein in the adrenal gland
    • Lau, E. T., Cao, D., Lin, C., Chung, S. K. & Chung, S. S. (1995) Tissue-specific expression of two aldose-reductase-like genes in mice: abundant expression of mouse vas deferens protein and fibroblast growth factor-regulated protein in the adrenal gland, Biochem. J. 312, 609-615.
    • (1995) Biochem. J. , vol.312 , pp. 609-615
    • Lau, E.T.1    Cao, D.2    Lin, C.3    Chung, S.K.4    Chung, S.S.5
  • 46
    • 0029963946 scopus 로고    scopus 로고
    • Induction of aldose-reduclase gene expression in LEC rats during development of the hereditary hepatitis and hepatoma
    • Takahashi, M., Hoshi, A., Fujii, J., Miyoshi, E., Kasahara, T., Suzuki, K., Aozasa, K. & Tanaguchi, N. (1996) Induction of aldose-reduclase gene expression in LEC rats during development of the hereditary hepatitis and hepatoma. Jpn. J. Cancer Res. 87, 337-341.
    • (1996) Jpn. J. Cancer Res. , vol.87 , pp. 337-341
    • Takahashi, M.1    Hoshi, A.2    Fujii, J.3    Miyoshi, E.4    Kasahara, T.5    Suzuki, K.6    Aozasa, K.7    Tanaguchi, N.8
  • 47
    • 0029127117 scopus 로고
    • Elevation of aldose reductase gene expression in rat primary hepatoma and hepatoma cell lines: Implication in detoxification of cytotoxic aldehydes
    • Takahashi, M., Fujii, J., Miyoshi, E., Hoshi, A. & Taniguchi, N. (1995) Elevation of aldose reductase gene expression in rat primary hepatoma and hepatoma cell lines: implication in detoxification of cytotoxic aldehydes, Int. J. Cancer 62, 749-754.
    • (1995) Int. J. Cancer , vol.62 , pp. 749-754
    • Takahashi, M.1    Fujii, J.2    Miyoshi, E.3    Hoshi, A.4    Taniguchi, N.5
  • 48
    • 0029133941 scopus 로고
    • Long-term induction of an aldose reductase protein by basic fibroblast growth factor in rat astrocytes in vitro
    • Laeng, P., Bouillon, P., Taupenot, L. & Labourdette, G. (1995) Long-term induction of an aldose reductase protein by basic fibroblast growth factor in rat astrocytes in vitro, Electrophoresis 16, 1240-1250.
    • (1995) Electrophoresis , vol.16 , pp. 1240-1250
    • Laeng, P.1    Bouillon, P.2    Taupenot, L.3    Labourdette, G.4
  • 50
    • 0000237383 scopus 로고
    • L'aldose reductase
    • Hers, H. G. (1960) L'aldose reductase, Biochim. Biophys. Acta 37, 120-126.
    • (1960) Biochim. Biophys. Acta , vol.37 , pp. 120-126
    • Hers, H.G.1
  • 51
    • 4243546541 scopus 로고
    • Le mechanisme de la formation du fructose séminal et du fructose foetal
    • Hers, H. G. (1960) Le mechanisme de la formation du fructose séminal et du fructose foetal, Biochim. Biophys. Acta 37, 127-138.
    • (1960) Biochim. Biophys. Acta , vol.37 , pp. 127-138
    • Hers, H.G.1
  • 52
    • 0000930578 scopus 로고
    • Isolation and properties of lens aldose reductase
    • Hayman, S. & Kinoshita, J. H. (1965) Isolation and properties of lens aldose reductase, J. Biol. Chem. 240, 877-882.
    • (1965) J. Biol. Chem. , vol.240 , pp. 877-882
    • Hayman, S.1    Kinoshita, J.H.2
  • 53
    • 0017387749 scopus 로고
    • Resolution and practial characterization of two aldehyde reductases of mammalian liver
    • Tulsiani, P. & Touster, O. (1977) Resolution and practial characterization of two aldehyde reductases of mammalian liver, J. Biol. Chem. 252, 2545-2550.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2545-2550
    • Tulsiani, P.1    Touster, O.2
  • 54
    • 0020316829 scopus 로고
    • Immunohistochemical distribution of aldose reductase
    • Kern, T. S. & Engerman, R. L. (1982) Immunohistochemical distribution of aldose reductase, Histochem. J. 14, 507-515.
    • (1982) Histochem. J. , vol.14 , pp. 507-515
    • Kern, T.S.1    Engerman, R.L.2
  • 56
    • 0028178333 scopus 로고
    • m aldose reductase and conversion mechanism into aldose reductase
    • m aldose reductase and conversion mechanism into aldose reductase, Int. J. Biochem. 26, 565-573.
    • (1994) Int. J. Biochem. , vol.26 , pp. 565-573
    • Ohta, M.1    Tanimoto, T.2    Hayakawa, T.3
  • 57
    • 0003353655 scopus 로고
    • Activated and unactivated forms of human erythrocyte aldose reductase
    • Srivastava, S. K., Hair, A. G. & Das, B. (1985) Activated and unactivated forms of human erythrocyte aldose reductase, Proc. Natl Acad. Sci. USA 82, 7222-7226.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 7222-7226
    • Srivastava, S.K.1    Hair, A.G.2    Das, B.3
  • 58
    • 0002075559 scopus 로고
    • The pentose phosphate pathway & other pathways of hexose metabolism
    • (Murray, R. K., Mayes, P. A, Granner, D. K. & Rodwell, V. W., eds) 22nd edn, Prentice-Hall Int. Inc, London
    • Mayes, P. A. (1990) The pentose phosphate pathway & other pathways of hexose metabolism, in Harper's Biochemistry (Murray, R. K., Mayes, P. A, Granner, D. K. & Rodwell, V. W., eds) 22nd edn, pp. 189-198, Prentice-Hall Int. Inc, London.
    • (1990) Harper's Biochemistry , pp. 189-198
    • Mayes, P.A.1
  • 60
    • 0015409718 scopus 로고
    • Glycolysis, respiration and anomalous gene expression in ex-perimental hepatomas
    • Weinhouse, S. (1972) Glycolysis, respiration and anomalous gene expression in ex-perimental hepatomas, Cancer Res. 32, 2007-2016.
    • (1972) Cancer Res. , vol.32 , pp. 2007-2016
    • Weinhouse, S.1
  • 61
    • 0020955571 scopus 로고
    • Biochemical strategy of cancer cells and the design of chemotherapy
    • Weber, G. (1983) Biochemical strategy of cancer cells and the design of chemotherapy. Cancer Res. 43, 3466-3492.
    • (1983) Cancer Res. , vol.43 , pp. 3466-3492
    • Weber, G.1
  • 62
    • 0027363936 scopus 로고
    • Aldose reductase gene expression and osmotic dysregulation in cultured human retinal pigment epithelial cells
    • Stevens, M. J., Henry, D. N., Thomas, T. P., Killen, P. D. & Greene, D. A. (1993) Aldose reductase gene expression and osmotic dysregulation in cultured human retinal pigment epithelial cells, Am. J. Physiol. 265, E428-E438.
    • (1993) Am. J. Physiol. , vol.265
    • Stevens, M.J.1    Henry, D.N.2    Thomas, T.P.3    Killen, P.D.4    Greene, D.A.5
  • 64
    • 0023020296 scopus 로고
    • Preneoplastic laesions as end points in carcinogenicity testing. I. Hepatic preneoplasia
    • Bannasch, P. (1986) Preneoplastic laesions as end points in carcinogenicity testing. I. Hepatic preneoplasia, Carcinogenesis (Oxf.) 7, 689-695.
    • (1986) Carcinogenesis (Oxf.) , vol.7 , pp. 689-695
    • Bannasch, P.1
  • 65
    • 0026475568 scopus 로고
    • Aldose reductase: Model for a new paradigm of enzymic perfection in detoxification catalysts
    • Grimshaw, C. E. (1992) Aldose reductase: Model for a new paradigm of enzymic perfection in detoxification catalysts, Biochemistry 31, 10139-10145.
    • (1992) Biochemistry , vol.31 , pp. 10139-10145
    • Grimshaw, C.E.1
  • 68
    • 0027337582 scopus 로고
    • 1 is associated with the expression of a novel aldoketo reductase which has catalytic activity towards a cytotoxic aldehyde-containing metabolite of the toxin
    • 1 is associated with the expression of a novel aldoketo reductase which has catalytic activity towards a cytotoxic aldehyde-containing metabolite of the toxin, Cancer Res. 53, 3887-3894.
    • (1993) Cancer Res. , vol.53 , pp. 3887-3894
    • Hayes, J.D.1    Judah, D.J.2    Neal, G.E.3
  • 69
    • 0003385738 scopus 로고
    • The biochemical-molecular pathology of the stepwise development of liver cancer: New insights and problems
    • (Bannasch, P., Keppler, D. & Weber, G., eds) Kluwer Academic Publishers, Dordrecht, Boston, London
    • Farber, E., Chen, Z.-Y., Harris, L., Lee, G., Rinaudo, J. S., Roomi, W. M., Rotstein, J. & Semple, E. (1988) The biochemical-molecular pathology of the stepwise development of liver cancer: new insights and problems, in Liver cell carcinoma (Bannasch, P., Keppler, D. & Weber, G., eds) pp. 273-291, Kluwer Academic Publishers, Dordrecht, Boston, London.
    • (1988) Liver Cell Carcinoma , pp. 273-291
    • Farber, E.1    Chen, Z.-Y.2    Harris, L.3    Lee, G.4    Rinaudo, J.S.5    Roomi, W.M.6    Rotstein, J.7    Semple, E.8
  • 70
    • 0030926156 scopus 로고    scopus 로고
    • A new method to assign immuno-detected spots in the complex 2-dimensional electrophoresis pattern
    • Zeindl-Eberhart, E., Jungblut, P. R. & Rabes, H. M. (1997) A new method to assign immuno-detected spots in the complex 2-dimensional electrophoresis pattern, Electrophoresis 18, 799-801.
    • (1997) Electrophoresis , vol.18 , pp. 799-801
    • Zeindl-Eberhart, E.1    Jungblut, P.R.2    Rabes, H.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.