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Volumn 121, Issue 2, 2004, Pages 123-130

Carbonyl stress and detoxification ability in the male genital tract and testis of rats

Author keywords

Acrolein; Aldo keto reductase; Carbonyl compounds; Lipid peroxidation

Indexed keywords

ACROLEIN; ALDEHYDE REDUCTASE; CARBONYL DERIVATIVE; GLUTATHIONE REDUCTASE; MONOCLONAL ANTIBODY; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 1542283583     PISSN: 09486143     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00418-003-0607-3     Document Type: Article
Times cited : (34)

References (33)
  • 1
    • 0032913309 scopus 로고    scopus 로고
    • Role of oxidative stress in diabetic complications: A new perspective on an old paradigm
    • Baynes JW, Thorpe SR (1999) Role of oxidative stress in diabetic complications: a new perspective on an old paradigm. Diabetes 48:1-9
    • (1999) Diabetes , vol.48 , pp. 1-9
    • Baynes, J.W.1    Thorpe, S.R.2
  • 3
    • 0034212444 scopus 로고    scopus 로고
    • Redox capacity of cells affects inactivation of glutathione reductase by nitrosative stress
    • Fujii T, Hamaoka R, Fujii J, Taniguchi N (2000) Redox capacity of cells affects inactivation of glutathione reductase by nitrosative stress. Arch Biochem Biophys 378:123-130
    • (2000) Arch Biochem Biophys , vol.378 , pp. 123-130
    • Fujii, T.1    Hamaoka, R.2    Fujii, J.3    Taniguchi, N.4
  • 4
    • 0042280453 scopus 로고    scopus 로고
    • Cooperative function of antioxidant and redox systems against oxidative stress in male reproductive tissues
    • Fujii J, Iuchi Y, Matsuki S, Ishii T (2003) Cooperative function of antioxidant and redox systems against oxidative stress in male reproductive tissues. Asian J Androl 5:231-242
    • (2003) Asian J Androl , vol.5 , pp. 231-242
    • Fujii, J.1    Iuchi, Y.2    Matsuki, S.3    Ishii, T.4
  • 5
    • 0021330940 scopus 로고
    • Hyperacetylation of histone H4 in rat testis spermatids
    • Grimes SR Jr, Henderson N (1984) Hyperacetylation of histone H4 in rat testis spermatids. Exp Cell Res 152:91-97
    • (1984) Exp Cell Res , vol.152 , pp. 91-97
    • Grimes Jr., S.R.1    Henderson, N.2
  • 7
    • 0034752798 scopus 로고    scopus 로고
    • The expression of a Y-box protein, YB2/RYB-a, precedes protamine 2 during spermatogenesis in rodents
    • Iuchi Y, Kobayashi T, Kaneko T, Takahara M, Ogino T, Fujii J (2001) The expression of a Y-box protein, YB2/RYB-a, precedes protamine 2 during spermatogenesis in rodents. Mol Hum Reprod 7:1023-1031
    • (2001) Mol Hum Reprod , vol.7 , pp. 1023-1031
    • Iuchi, Y.1    Kobayashi, T.2    Kaneko, T.3    Takahara, M.4    Ogino, T.5    Fujii, J.6
  • 9
    • 0034761387 scopus 로고    scopus 로고
    • Alteration of glutathione reductase expression in the female reproductive organs during the estrous cycle
    • Kaneko T, Iuchi Y, Kawachiya S, Fujii T, Saito H, Kurachi H, Fujii J (2001) Alteration of glutathione reductase expression in the female reproductive organs during the estrous cycle. Biol Reprod 65:1410-1416
    • (2001) Biol Reprod , vol.65 , pp. 1410-1416
    • Kaneko, T.1    Iuchi, Y.2    Kawachiya, S.3    Fujii, T.4    Saito, H.5    Kurachi, H.6    Fujii, J.7
  • 10
    • 0036121169 scopus 로고    scopus 로고
    • Expression of glutathione reductase in the male reproductive system of rats supports the enzymatic basis of glutathione function in spermatogenesis
    • Kaneko T, Iuchi Y, Kobayashi T, Fujii T, Saito H, Kurachi H, Fujii J (2002) Expression of glutathione reductase in the male reproductive system of rats supports the enzymatic basis of glutathione function in spermatogenesis. Eur J Biochem 269:1570-1578
    • (2002) Eur J Biochem , vol.269 , pp. 1570-1578
    • Kaneko, T.1    Iuchi, Y.2    Kobayashi, T.3    Fujii, T.4    Saito, H.5    Kurachi, H.6    Fujii, J.7
  • 11
    • 0038702522 scopus 로고    scopus 로고
    • Colocalization of polyol-metabolizing enzymes and immunological detection of fructated proteins in the female reproductive system of the rat
    • Kaneko T, Iuchi Y, Takahashi M, Fujii J (2003) Colocalization of polyol-metabolizing enzymes and immunological detection of fructated proteins in the female reproductive system of the rat. Histochem Cell Biol 119:309-315
    • (2003) Histochem Cell Biol , vol.119 , pp. 309-315
    • Kaneko, T.1    Iuchi, Y.2    Takahashi, M.3    Fujii, J.4
  • 12
    • 0033864802 scopus 로고    scopus 로고
    • The molecular effects of acrolein
    • Kehrer JP, Biswal SS (2000) The molecular effects of acrolein. Toxicol Sci 57:6-15
    • (2000) Toxicol Sci , vol.57 , pp. 6-15
    • Kehrer, J.P.1    Biswal, S.S.2
  • 13
    • 0036708430 scopus 로고    scopus 로고
    • Localization and physiological implication of aldose reductase and sorbitol dehydrogenase in male reproductive systems, accessory glands, and spermatozoa of rats
    • Kobayashi T, Kaneko T, Iuchi Y, Matsuki S, Takahashi M, Sasagawa I, Nakada T, Fujii J (2002) Localization and physiological implication of aldose reductase and sorbitol dehydrogenase in male reproductive systems, accessory glands, and spermatozoa of rats. J Androl 23:674-683
    • (2002) J Androl , vol.23 , pp. 674-683
    • Kobayashi, T.1    Kaneko, T.2    Iuchi, Y.3    Matsuki, S.4    Takahashi, M.5    Sasagawa, I.6    Nakada, T.7    Fujii, J.8
  • 14
    • 0028213845 scopus 로고
    • Aldose reductase-catalyzed reduction of acrolein: Implications in cyclophosphamide toxicity
    • Kolb NS, Hunsaker LA, Vander Jagt DL (1994) Aldose reductase-catalyzed reduction of acrolein: implications in cyclophosphamide toxicity. Mol Pharmacol 45:797-801
    • (1994) Mol Pharmacol , vol.45 , pp. 797-801
    • Kolb, N.S.1    Hunsaker, L.A.2    Vander Jagt, D.L.3
  • 15
    • 2542508838 scopus 로고    scopus 로고
    • Product of side-chain cleavage of cholesterol, isocaproaldehyde, is an endogenous specific substrate of mouse vas deferens protein, an aldose reductase-like protein in adrenocortical cells
    • Lefrancois-Martinez AM, Tournaire C, Martinez A, Berger M, Daoudal S, Tritsch D, Veyssiere G, Jean C (1999) Product of side-chain cleavage of cholesterol, isocaproaldehyde, is an endogenous specific substrate of mouse vas deferens protein, an aldose reductase-like protein in adrenocortical cells. J Biol Chem 274:32875-32880
    • (1999) J Biol Chem , vol.274 , pp. 32875-32880
    • Lefrancois-Martinez, A.M.1    Tournaire, C.2    Martinez, A.3    Berger, M.4    Daoudal, S.5    Tritsch, D.6    Veyssiere, G.7    Jean, C.8
  • 16
    • 0019301485 scopus 로고
    • Immunohistochemical localization of aldose reductase. I. Enzyme purification and antibody preparation: Localization in peripheral nerve, artery, and testis
    • Ludvigson MA, Sorenson RL (1980) Immunohistochemical localization of aldose reductase. I. Enzyme purification and antibody preparation: localization in peripheral nerve, artery, and testis. Diabetes 29:438-449
    • (1980) Diabetes , vol.29 , pp. 438-449
    • Ludvigson, M.A.1    Sorenson, R.L.2
  • 17
    • 0020074181 scopus 로고
    • Immunocytochemical evidence for the specific localization of aldose reductase in rat Sertoli cells
    • Ludvigson MA, Waites GM, Hamilton DW (1982) Immunocytochemical evidence for the specific localization of aldose reductase in rat Sertoli cells. Biol Reprod 26:311-317
    • (1982) Biol Reprod , vol.26 , pp. 311-317
    • Ludvigson, M.A.1    Waites, G.M.2    Hamilton, D.W.3
  • 19
    • 0034455620 scopus 로고    scopus 로고
    • Androgen-regulated expression of a novel member of the aldo-keto reductase superfamily in regrowing rat prostate
    • Nishi N, Shoji H, Miyanaka H, Nakamura T (2000) Androgen-regulated expression of a novel member of the aldo-keto reductase superfamily in regrowing rat prostate. Endocrinology 141:3194-3199
    • (2000) Endocrinology , vol.141 , pp. 3194-3199
    • Nishi, N.1    Shoji, H.2    Miyanaka, H.3    Nakamura, T.4
  • 20
    • 0033603599 scopus 로고    scopus 로고
    • Methylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts
    • Oya T, Hattori N, Mizuno Y, Miyata S, Maeda S, Osawa T, Uchida K (1999) Methylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts. J Biol Chem 274:18492-18502
    • (1999) J Biol Chem , vol.274 , pp. 18492-18502
    • Oya, T.1    Hattori, N.2    Mizuno, Y.3    Miyata, S.4    Maeda, S.5    Osawa, T.6    Uchida, K.7
  • 21
    • 0035039021 scopus 로고    scopus 로고
    • Protein oxidation in aging and age-related diseases
    • Stadtman ER (2001) Protein oxidation in aging and age-related diseases. Ann N Y Acad Sci 928:22-38
    • (2001) Ann N Y Acad Sci , vol.928 , pp. 22-38
    • Stadtman, E.R.1
  • 22
    • 0027322593 scopus 로고
    • Identity of a major 3-deoxyglucosone-reducing enzyme with aldehyde reductase in rat liver established by amino acid sequencing and cDNA expression
    • Takahashi M, Fujii J, Teshima T, Suzuki K, Shiba T, Taniguchi N (1993) Identity of a major 3-deoxyglucosone-reducing enzyme with aldehyde reductase in rat liver established by amino acid sequencing and cDNA expression. Gene 127:249-253
    • (1993) Gene , vol.127 , pp. 249-253
    • Takahashi, M.1    Fujii, J.2    Teshima, T.3    Suzuki, K.4    Shiba, T.5    Taniguchi, N.6
  • 23
    • 0029127117 scopus 로고
    • Elevation of aldose reductase gene expression in rat primary hepatoma and hepatoma cell lines. Implication 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 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
  • 24
    • 0029963946 scopus 로고    scopus 로고
    • Induction of aldose reductase gene expression in LEC rats during the development of the hereditary hepatitis and hepatoma
    • Takahashi M, Hoshi A, Fujii J, Miyoshi E, Kasahara T, Suzuki K, Aozasa K, Taniguchi N (1996) Induction of aldose reductase gene expression in LEC rats during the 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    Taniguchi, N.8
  • 25
    • 0034659147 scopus 로고    scopus 로고
    • Role of reactive aldehyde in cardiovascular diseases
    • Uchida K (2000) Role of reactive aldehyde in cardiovascular diseases. Free Radic Biol Med 28:1685-1696
    • (2000) Free Radic Biol Med , vol.28 , pp. 1685-1696
    • Uchida, K.1
  • 27
    • 0026646131 scopus 로고
    • Reduction of trioses by NADPH-dependent aldo-keto reductases: Aldose reductase, methylglyoxal, and diabetic complications
    • Vander Jagt DL, Robinson B, Taylor KK, Hunsaker LA (1992) Reduction of trioses by NADPH-dependent aldo-keto reductases: aldose reductase, methylglyoxal, and diabetic complications. J Biol Chem 267:4364-4369
    • (1992) J Biol Chem , vol.267 , pp. 4364-4369
    • Vander Jagt, D.L.1    Robinson, B.2    Taylor, K.K.3    Hunsaker, L.A.4
  • 30
    • 0027461303 scopus 로고
    • Molecular cloning of testicular 20 alpha-hydroxysteroid dehydrogenase: Identity with aldose reductase
    • Warren JC, Murdock GL, Ma Y, Goodman SR, Zimmer WE (1993) Molecular cloning of testicular 20 alpha-hydroxysteroid dehydrogenase: identity with aldose reductase. Biochemistry 32:1401-1406
    • (1993) Biochemistry , vol.32 , pp. 1401-1406
    • Warren, J.C.1    Murdock, G.L.2    Ma, Y.3    Goodman, S.R.4    Zimmer, W.E.5
  • 31
    • 0020620332 scopus 로고
    • Aldose and aldehyde reductase exhibit isocorticosteroid reductase activity
    • Wermuth B, Monder C (1983) Aldose and aldehyde reductase exhibit isocorticosteroid reductase activity. Eur J Biochem 131:423-426
    • (1983) Eur J Biochem , vol.131 , pp. 423-426
    • Wermuth, B.1    Monder, C.2
  • 32
    • 0031920049 scopus 로고    scopus 로고
    • Aldose reductase in glucose toxicity: A potential target for the prevention of diabetic complications
    • Yabe-Nishimura C (1998) Aldose reductase in glucose toxicity: a potential target for the prevention of diabetic complications. Pharmacol Rev 50:21-33
    • (1998) Pharmacol Rev , vol.50 , pp. 21-33
    • Yabe-Nishimura, C.1


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