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Volumn 143-144, Issue , 2003, Pages 353-361

Cloning, expression and tissue distribution of a tetrameric form of pig carbonyl reductase

Author keywords

Carbonyl reductase; Peroxisomal targeting signal; Retinal reductase; Short chain dehydrogenase reductase family

Indexed keywords

1,2 DICARBONYL DERIVATIVE; ALKYL PHENYL KETONE; CARBONYL REDUCTASE; COMPLEMENTARY DNA; ENZYME; ISOENZYME; MESSENGER RNA; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEPENDENT RETINOL DEHYDROGENASE; RETINAL; TETRAMER; UNCLASSIFIED DRUG;

EID: 0037328409     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(02)00210-7     Document Type: Conference Paper
Times cited : (29)

References (30)
  • 2
    • 0023768323 scopus 로고
    • Human carbonyl reductase. Nucleotide sequence analysis of a cDNA and amino acid sequence of the encoded protein
    • Wermuth B., Bohren K.M., Heinemann G., von Wartburg J.-P., Gabbay K.H. Human carbonyl reductase. Nucleotide sequence analysis of a cDNA and amino acid sequence of the encoded protein. J. Biol. Chem. 263:1988;16185-16188.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16185-16188
    • Wermuth, B.1    Bohren, K.M.2    Heinemann, G.3    Von Wartburg, J.-P.4    Gabbay, K.H.5
  • 3
    • 0026681607 scopus 로고
    • Pig testicular 20β-hydroxysteroid dehydrogenase exhibits carbonyl reductase-like structure and activity
    • Tanaka M., Ohno S., Adachi S., Nakajin S., Shinoda M., Nagahama Y. Pig testicular 20β-hydroxysteroid dehydrogenase exhibits carbonyl reductase-like structure and activity. J. Biol. Chem. 267:1992;13451-13455.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13451-13455
    • Tanaka, M.1    Ohno, S.2    Adachi, S.3    Nakajin, S.4    Shinoda, M.5    Nagahama, Y.6
  • 4
    • 0028898587 scopus 로고
    • Cloning and expression of the cDNA encoding rabbit liver carbonyl reductase
    • Gonzalez B., Sapra A., Rivera H., Kaplan W.D., Yam B., Forrest G.L. Cloning and expression of the cDNA encoding rabbit liver carbonyl reductase. Gene. 154:1995;297-298.
    • (1995) Gene , vol.154 , pp. 297-298
    • Gonzalez, B.1    Sapra, A.2    Rivera, H.3    Kaplan, W.D.4    Yam, B.5    Forrest, G.L.6
  • 6
    • 0035173178 scopus 로고    scopus 로고
    • Characterization of a major form of human isatin reductase and the reduced metabolite
    • Usami N., Kitahara K., Ishikura S., Nagano M., Sakai S., Hara A. Characterization of a major form of human isatin reductase and the reduced metabolite. Eur. J. Biochem. 268:2001;5755-5763.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5755-5763
    • Usami, N.1    Kitahara, K.2    Ishikura, S.3    Nagano, M.4    Sakai, S.5    Hara, A.6
  • 10
    • 0035830422 scopus 로고    scopus 로고
    • Enzymatic characteristics and subcellular distribution of a short-chain dehydrogenase/reductase family protein, P26h, in hamster testis and epididymis
    • Ishikura S., Usami N., Kitahara K., Isaji T., Oda K., Nakagawa J., Hara A. Enzymatic characteristics and subcellular distribution of a short-chain dehydrogenase/reductase family protein, P26h, in hamster testis and epididymis. Biochemistry. 40:2001;214-224.
    • (2001) Biochemistry , vol.40 , pp. 214-224
    • Ishikura, S.1    Usami, N.2    Kitahara, K.3    Isaji, T.4    Oda, K.5    Nakagawa, J.6    Hara, A.7
  • 11
    • 0027291816 scopus 로고
    • Cloning and sequence analysis of a cDNA encoding tetrameric carbonyl reductase of pig lung
    • Nakanishi M., Deyashiki Y., Nakayama T., Sato K., Hara A. Cloning and sequence analysis of a cDNA encoding tetrameric carbonyl reductase of pig lung. Biochem. Biophys. Res. Commun. 194:1993;1311-1316.
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 1311-1316
    • Nakanishi, M.1    Deyashiki, Y.2    Nakayama, T.3    Sato, K.4    Hara, A.5
  • 12
    • 0028932550 scopus 로고
    • Cloning, expression and tissue distribution of mouse tetrameric carbonyl reductase. Identity with an adipocyte 27-kDa protein
    • Nakanishi M., Deyashiki Y., Ohshima K., Hara A. Cloning, expression and tissue distribution of mouse tetrameric carbonyl reductase. Identity with an adipocyte 27-kDa protein. Eur. J. Biochem. 228:1995;381-387.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 381-387
    • Nakanishi, M.1    Deyashiki, Y.2    Ohshima, K.3    Hara, A.4
  • 13
    • 0028872766 scopus 로고
    • Cloning and primary structure of murine 11β-hydroxysteroid dehydrogenase/microsomal carbonyl reductase
    • Oppermann U.C.T., Netter K.J., Maser E. Cloning and primary structure of murine 11β-hydroxysteroid dehydrogenase/microsomal carbonyl reductase. Eur. J. Biochem. 227:1995;202-208.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 202-208
    • Oppermann, U.C.T.1    Netter, K.J.2    Maser, E.3
  • 14
    • 0027379926 scopus 로고
    • Postnatal development, sex-related differences and hormonal regulation of acetohexamide reductase activities in rat liver and kidney
    • Imamura Y., Iwamoto K., Yanachi Y., Higuchi T., Otagiri M. Postnatal development, sex-related differences and hormonal regulation of acetohexamide reductase activities in rat liver and kidney. J. Pharmacol. Exp. Ther. 264:1993;166-171.
    • (1993) J. Pharmacol. Exp. Ther. , vol.264 , pp. 166-171
    • Imamura, Y.1    Iwamoto, K.2    Yanachi, Y.3    Higuchi, T.4    Otagiri, M.5
  • 15
    • 0032219602 scopus 로고    scopus 로고
    • 20β-Hydroxysteroid dehydrogenase catalyzes ketone-reduction of acetohexamide, an oral antidiabetic drug, in liver microsomes of adult male rats
    • Takada H., Otagiri M., Imamura Y. 20β-Hydroxysteroid dehydrogenase catalyzes ketone-reduction of acetohexamide, an oral antidiabetic drug, in liver microsomes of adult male rats. J. Pharmacol. Exp. Ther. 287:1998;504-507.
    • (1998) J. Pharmacol. Exp. Ther. , vol.287 , pp. 504-507
    • Takada, H.1    Otagiri, M.2    Imamura, Y.3
  • 16
    • 0033043581 scopus 로고    scopus 로고
    • Purification and catalytic properties of a tetrameric carbonyl reductase from rabbit heart
    • Imamura Y., Migita T., Otagiri M., Choshi T., Hibino S. Purification and catalytic properties of a tetrameric carbonyl reductase from rabbit heart. J. Biochem. (Tokyo). 125:1999;41-47.
    • (1999) J. Biochem. (Tokyo) , vol.125 , pp. 41-47
    • Imamura, Y.1    Migita, T.2    Otagiri, M.3    Choshi, T.4    Hibino, S.5
  • 17
    • 0022586418 scopus 로고
    • Carbonyl reductase of dog liver: Purification, properties and kinetic mechanism
    • Hara A., Nakayama T., Deyashiki Y., Kariya K., Sawada H. Carbonyl reductase of dog liver: purification, properties and kinetic mechanism. Arch. Biochem. Biophys. 244:1986;238-247.
    • (1986) Arch. Biochem. Biophys. , vol.244 , pp. 238-247
    • Hara, A.1    Nakayama, T.2    Deyashiki, Y.3    Kariya, K.4    Sawada, H.5
  • 18
    • 0018936973 scopus 로고
    • Reductases for aromatic aldehydes and ketones from rabbit liver. Purification and characterization
    • Sawada H., Hara A., Nakayama T., Kato F. Reductases for aromatic aldehydes and ketones from rabbit liver. Purification and characterization. J. Biochem. (Tokyo). 87:1980;1153-1165.
    • (1980) J. Biochem. (Tokyo) , vol.87 , pp. 1153-1165
    • Sawada, H.1    Hara, A.2    Nakayama, T.3    Kato, F.4
  • 19
    • 0033153285 scopus 로고    scopus 로고
    • Identification of peroxisomal proteins by using M13 phage protein VI phage display: Molecular evidence that mammalian peroxisomes contain a 2,4-dienoyl-CoA reductase
    • Fransen M., Van Veldhoven P.P., Subramani S. Identification of peroxisomal proteins by using M13 phage protein VI phage display: molecular evidence that mammalian peroxisomes contain a 2,4-dienoyl-CoA reductase. Biochem. J. 340:1999;561-568.
    • (1999) Biochem. J. , vol.340 , pp. 561-568
    • Fransen, M.1    Van Veldhoven, P.P.2    Subramani, S.3
  • 20
    • 0025598328 scopus 로고
    • Isoenzymes of alcohol dehydrogenase in retinoid metabolism
    • Parés X., Julià P. Isoenzymes of alcohol dehydrogenase in retinoid metabolism. Methods Enz. 189:1990;436-441.
    • (1990) Methods Enz. , vol.189 , pp. 436-441
    • Parés, X.1    Julià, P.2
  • 21
    • 0031019150 scopus 로고    scopus 로고
    • Purification and characterization of a novel cytosolic NADP(H)-dependent retinol oxidoreductase from rabbit liver
    • Huang D.-Y., Ichikawa Y. Purification and characterization of a novel cytosolic NADP(H)-dependent retinol oxidoreductase from rabbit liver. Biochim. Biophys. Acta. 1338:1997;47-59.
    • (1997) Biochim. Biophys. Acta , vol.1338 , pp. 47-59
    • Huang, D.-Y.1    Ichikawa, Y.2
  • 22
    • 0035022533 scopus 로고    scopus 로고
    • SDR: Structure, mechanism of action and substrate recognition
    • Tanaka N., Nonaka T., Nakamura K.T., Hara A. SDR: structure, mechanism of action and substrate recognition. Cur. Org. Chem. 5:2001;89-111.
    • (2001) Cur. Org. Chem. , vol.5 , pp. 89-111
    • Tanaka, N.1    Nonaka, T.2    Nakamura, K.T.3    Hara, A.4
  • 23
    • 0032803033 scopus 로고    scopus 로고
    • Inhibition of rabbit heart carbonyl reductase by fatty acids
    • Imamura Y., Migita T., Anraku M., Otagiri M. Inhibition of rabbit heart carbonyl reductase by fatty acids. Biol. Pharm. Bull. 22:1999;731-733.
    • (1999) Biol. Pharm. Bull. , vol.22 , pp. 731-733
    • Imamura, Y.1    Migita, T.2    Anraku, M.3    Otagiri, M.4
  • 27
    • 0033569574 scopus 로고    scopus 로고
    • 1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members
    • 1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members. Biochem. J. 343:1999;487-504.
    • (1999) Biochem. J. , vol.343 , pp. 487-504
    • O'Connor, T.1    Ireland, L.S.2    Harrison, D.J.3    Hayes, J.D.4
  • 29
    • 0033911401 scopus 로고    scopus 로고
    • Families of retinoid dehydrogenases regulating vitamin A function. Production of visual pigment and retinoic acid
    • Duester G. Families of retinoid dehydrogenases regulating vitamin A function. Production of visual pigment and retinoic acid. Eur. J. Biochem. 267:2000;4315-4324.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4315-4324
    • Duester, G.1
  • 30
    • 0034867911 scopus 로고    scopus 로고
    • Localization of cytosolic NADP-dependent isocitrate dehydrogenase in the peroxisomes of rat liver cells: Biochemical and immunochemical studies
    • Yoshihara T., Hamamoto T., Munakata R., Tajiri R., Ohsumi M., Yokota S. Localization of cytosolic NADP-dependent isocitrate dehydrogenase in the peroxisomes of rat liver cells: biochemical and immunochemical studies. J. Histochem. Cytochem. 49:2001;1123-1131.
    • (2001) J. Histochem. Cytochem. , vol.49 , pp. 1123-1131
    • Yoshihara, T.1    Hamamoto, T.2    Munakata, R.3    Tajiri, R.4    Ohsumi, M.5    Yokota, S.6


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