메뉴 건너뛰기




Volumn 13, Issue 3, 1999, Pages 513-522

Carbonic anhydrase III protects cells from hydrogen peroxide-induced apoptosis

Author keywords

Overexpression; Oxidative stress; Skeletal muscle

Indexed keywords

CARBONATE DEHYDRATASE;

EID: 0345003848     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.13.3.513     Document Type: Article
Times cited : (188)

References (49)
  • 1
    • 0024688008 scopus 로고
    • The carbonic anhydrases: Widening perspectives on their evolution, expression and function
    • Tashian, R. E. (1989) The carbonic anhydrases: widening perspectives on their evolution, expression and function. BioEssays 10, 186-192
    • (1989) BioEssays , vol.10 , pp. 186-192
    • Tashian, R.E.1
  • 3
    • 0029057703 scopus 로고
    • Human carbonic anhydrases and carbonic anhydrase deficiencies
    • Sly, W. S., and Hu, P. Y. (1995) Human carbonic anhydrases and carbonic anhydrase deficiencies. Annu. Rev. Biochem. 64, 365-401
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 365-401
    • Sly, W.S.1    Hu, P.Y.2
  • 4
    • 0030076314 scopus 로고    scopus 로고
    • Functional diversity, conservation, and convergence in the evolution of the alpha-, beta-, and gamma-carbonic anhydrase gene families
    • Hewett-Emmet, D., and Tashian, R. E. (1996) Functional diversity, conservation, and convergence in the evolution of the alpha-, beta-, and gamma-carbonic anhydrase gene families. Mol. Phylogenet. Evol. 5, 50-77
    • (1996) Mol. Phylogenet. Evol. , vol.5 , pp. 50-77
    • Hewett-Emmet, D.1    Tashian, R.E.2
  • 6
    • 0014135426 scopus 로고
    • Carbonic anhydrase: Chemistry, physiology, and inhibition
    • Maren, T. H. (1967) Carbonic anhydrase: chemistry, physiology, and inhibition. Physiol. Rev. 47:595-781
    • (1967) Physiol. Rev. , vol.47 , pp. 595-781
    • Maren, T.H.1
  • 7
    • 0001885532 scopus 로고
    • Hormonal and neuronal control of carbonic anhydrase III gene expression in skeletal muscle
    • Dodgson, S. J., Tashian, R. E., Gross, G., and Carter, N. D., eds Plenum Publishing Corp., New York
    • Carter, N. D. (1991) Hormonal and neuronal control of carbonic anhydrase III gene expression in skeletal muscle. In: The Carbonic Anhydrases: Cellular Physiology and Molecular Genetics (Dodgson, S. J., Tashian, R. E., Gross, G., and Carter, N. D., eds) pp. 247-256, Plenum Publishing Corp., New York
    • (1991) The Carbonic Anhydrases: Cellular Physiology and Molecular Genetics , pp. 247-256
    • Carter, N.D.1
  • 8
    • 0025019414 scopus 로고
    • Comparative distribution of carbonic anhydrase isozymes III and II in rodent tissues
    • Spicer, S. S., Ge, Z. H., Tashian, R. E., Hazen-Martin, D. J., and Shulte, B. (1990) Comparative distribution of carbonic anhydrase isozymes III and II in rodent tissues. Am. J. Anat. 187, 55-64
    • (1990) Am. J. Anat. , vol.187 , pp. 55-64
    • Spicer, S.S.1    Ge, Z.H.2    Tashian, R.E.3    Hazen-Martin, D.J.4    Shulte, B.5
  • 9
    • 0019766977 scopus 로고
    • The p-nitrophenyl phosphatase activity of muscle carbonic anhydrase
    • Koester, M. K., Pullan, L. M., and Noltman, E. A. (1981) The p-nitrophenyl phosphatase activity of muscle carbonic anhydrase. Arch. Biochem. Biophys. 211, 632-642
    • (1981) Arch. Biochem. Biophys. , vol.211 , pp. 632-642
    • Koester, M.K.1    Pullan, L.M.2    Noltman, E.A.3
  • 10
    • 0030666934 scopus 로고    scopus 로고
    • Carbohydrate utilization in rat soleus is influenced by carbonic anhydrase III activity
    • Coté, C. H., Peneault, G., and Frenette, J. (1997) Carbohydrate utilization in rat soleus is influenced by carbonic anhydrase III activity. Am. J. Physiol. 273, R1211-R1218
    • (1997) Am. J. Physiol. , vol.273
    • Coté, C.H.1    Peneault, G.2    Frenette, J.3
  • 11
    • 0026011118 scopus 로고
    • Identification of an abundant S-thiolated rat liver protein as carbonic anhydrase III; characterization of S-thiolation and dethiolation reactions
    • Chai, Y.-C., Jung, C.-H., Lu, C.-K., Asharif, S. S., Hendrich, S., Wolf, B., Sies, H., and Thomas, J. A. (1991) Identification of an abundant S-thiolated rat liver protein as carbonic anhydrase III; characterization of S-thiolation and dethiolation reactions. Arch. Biochem. Biophys. 284, 270-278
    • (1991) Arch. Biochem. Biophys. , vol.284 , pp. 270-278
    • Chai, Y.-C.1    Jung, C.-H.2    Lu, C.-K.3    Asharif, S.S.4    Hendrich, S.5    Wolf, B.6    Sies, H.7    Thomas, J.A.8
  • 12
    • 0026004924 scopus 로고
    • Phagocytosis and stimulation of the respiratory burst by phorbol diester initiate S-thiolation of specific proteins in macrophages
    • Rokutan, K., Thomas, J. A., and Johnston, R. B., Jr. (1991) Phagocytosis and stimulation of the respiratory burst by phorbol diester initiate S-thiolation of specific proteins in macrophages. J. Immunol. 147, 260-264
    • (1991) J. Immunol. , vol.147 , pp. 260-264
    • Rokutan, K.1    Thomas, J.A.2    Johnston R.B., Jr.3
  • 13
    • 0028355875 scopus 로고
    • Protein S-thiolation in hepatocytes stimulated by t-butyl hydroperoxide, menadione, and neutrophils
    • Chai, Y.-C., Hendrich, S., and Thomas, J. A. (1994) Protein S-thiolation in hepatocytes stimulated by t-butyl hydroperoxide, menadione, and neutrophils. Arch. Biochem. Biophys. 310, 364-272
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 364-1272
    • Chai, Y.-C.1    Hendrich, S.2    Thomas, J.A.3
  • 14
    • 0028355875 scopus 로고
    • S-thiolation of individual human neutrophil proteins including acting by stimulation of the respiratory burst: Evidence against a role for glutathione disulfide
    • Chai, Y.-C., Asharf, S. S., Rokutan, K., Johnston, R. B., Jr., and Thomas, J. A. (1994) S-thiolation of individual human neutrophil proteins including acting by stimulation of the respiratory burst: evidence against a role for glutathione disulfide. Arch. Biochem. Biophys. 310, 264-272
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 264-272
    • Chai, Y.-C.1    Asharf, S.S.2    Rokutan, K.3    Johnston R.B., Jr.4    Thomas, J.A.5
  • 15
    • 0030008246 scopus 로고    scopus 로고
    • The phosphatase activity of carbonic anhydrase III is reversibly regulated by glutathiolation
    • Cabiscol, E., and Levine, R. L. (1996) The phosphatase activity of carbonic anhydrase III is reversibly regulated by glutathiolation. Proc. Natl. Acad. Sci. USA 93, 4170-4174
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4170-4174
    • Cabiscol, E.1    Levine, R.L.2
  • 16
    • 0023464342 scopus 로고
    • Free radical tissue damage: Protective role of antioxidant nutrients
    • Maclin, L. J., and Bendich, A. (1987) Free radical tissue damage: protective role of antioxidant nutrients FASEB J. 1, 441-445
    • (1987) FASEB J. , vol.1 , pp. 441-445
    • Maclin, L.J.1    Bendich, A.2
  • 17
    • 0028223829 scopus 로고
    • S-thiolation and irreversible oxidation of sulfhydryls on carbonic anhydrase III during oxidative stress: A method for studying protein modification in intact cells and tissues
    • Lii, C.-K., Chai, Y.-C., Zhao, W., Thomas, J. A., and Hendrich, S. (1994) S-thiolation and irreversible oxidation of sulfhydryls on carbonic anhydrase III during oxidative stress: a method for studying protein modification in intact cells and tissues. Arch. Biochem. Biophys. 308, 231-239
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 231-239
    • Lii, C.-K.1    Chai, Y.-C.2    Zhao, W.3    Thomas, J.A.4    Hendrich, S.5
  • 18
    • 0029015864 scopus 로고
    • Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation
    • Thomas, J. A., Poland, B., and Honzatko, R. (1995) Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch. Biochem. Biophys. 319, 1-9
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 1-9
    • Thomas, J.A.1    Poland, B.2    Honzatko, R.3
  • 19
    • 0029060701 scopus 로고
    • Carbonic anhydrase III. Oxidative modification in vivo and loss of phosphatase activity during aging
    • Cabiscol, E., and Levine, R. L. (1995) Carbonic anhydrase III. Oxidative modification in vivo and loss of phosphatase activity during aging. J. Biol. Chem. 270, 14742-14747
    • (1995) J. Biol. Chem. , vol.270 , pp. 14742-14747
    • Cabiscol, E.1    Levine, R.L.2
  • 21
    • 0023846309 scopus 로고
    • Free radical chemistry: Relation to exercise
    • Jenkins, R. R. (1988) Free radical chemistry: relation to exercise. Sports Med. 5, 156-170
    • (1988) Sports Med. , vol.5 , pp. 156-170
    • Jenkins, R.R.1
  • 22
    • 0032488513 scopus 로고    scopus 로고
    • Recent trends in glutathione biochemistry-glutathione-protein interactions: A molecular link between oxidative stress and cell proliferation?
    • Cotgreave, I. A., and Gredes, R. (1998) Recent trends in glutathione biochemistry-glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation? Biochem. Biophys Res. Commun. 242, 1-9
    • (1998) Biochem. Biophys Res. Commun. , vol.242 , pp. 1-9
    • Cotgreave, I.A.1    Gredes, R.2
  • 23
    • 0024150344 scopus 로고
    • Steroid hormone regulation of cultured breast cancer cells
    • Lippman, M. E., Dickson, R. B., eds Kluwer, Boston
    • Darbre, P. D., King, R. J. B. (1988) Steroid hormone regulation of cultured breast cancer cells. In: Breast Cancer: Cellular and Molecular Biology (Lippman, M. E., Dickson, R. B., eds) pp. 307-341, Kluwer, Boston
    • (1988) Breast Cancer: Cellular and Molecular Biology , pp. 307-341
    • Darbre, P.D.1    King, R.J.B.2
  • 24
    • 0026739751 scopus 로고
    • Plasmid pLTRpoly: A versatile high-efficiency mammalian expression vector
    • Mäkelä, T. P., Partanen, J., Schwab, M., and Alitalo, K. (1992) Plasmid pLTRpoly: a versatile high-efficiency mammalian expression vector. Gene 118, 293-294
    • (1992) Gene , vol.118 , pp. 293-294
    • Mäkelä, T.P.1    Partanen, J.2    Schwab, M.3    Alitalo, K.4
  • 25
    • 0019989719 scopus 로고
    • Construction and characterization of SV40 recombinants with beta-globin cDNA substitutions in their early regions
    • Southern, P. J., and Berg, P. (1982) Construction and characterization of SV40 recombinants with beta-globin cDNA substitutions in their early regions. J. Mol. Appl. Genet. 4, 327-341
    • (1982) J. Mol. Appl. Genet. , vol.4 , pp. 327-341
    • Southern, P.J.1    Berg, P.2
  • 27
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J., Leboviz, R., and Roeder, R. (1983) Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acid Res. 11, 1475-1489
    • (1983) Nucleic Acid Res. , vol.11 , pp. 1475-1489
    • Dignam, J.1    Leboviz, R.2    Roeder, R.3
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0022258260 scopus 로고
    • Purification and localization of human carbonic anhydrase III. Typing of skeletal muscle fibers in paraffin embedded sections
    • Väänänen, H. K., Paloniemi, M., and Vuori J. (1985) Purification and localization of human carbonic anhydrase III. Typing of skeletal muscle fibers in paraffin embedded sections. Histochemistry 83, 231-235
    • (1985) Histochemistry , vol.83 , pp. 231-235
    • Väänänen, H.K.1    Paloniemi, M.2    Vuori, J.3
  • 31
    • 0025786654 scopus 로고
    • Overexpression of seleno-ghitathione peroxidase by gene transfer enhances the resistance of T47D human breast cells to clastogenic oxidants
    • Mirault, M.-E., Tremblay, A., Beaudoin, N., and Tremblay, M. (1991) Overexpression of seleno-ghitathione peroxidase by gene transfer enhances the resistance of T47D human breast cells to clastogenic oxidants. J. Biol. Chem. 266, 20752-20760
    • (1991) J. Biol. Chem. , vol.266 , pp. 20752-20760
    • Mirault, M.-E.1    Tremblay, A.2    Beaudoin, N.3    Tremblay, M.4
  • 32
    • 0027445007 scopus 로고
    • Carbonic anhydrases in cytosol, nucleus, and membranes of rat liver
    • Dodgson S. J., Quistroff, B., and Ridderstrale, Y. (1993) Carbonic anhydrases in cytosol, nucleus, and membranes of rat liver. J. Appl. Physiol. 75, 1186-1193
    • (1993) J. Appl. Physiol. , vol.75 , pp. 1186-1193
    • Dodgson, S.J.1    Quistroff, B.2    Ridderstrale, Y.3
  • 34
    • 0025218905 scopus 로고
    • Flow cytometric analysis of respiratory burst activity in phagocytes with hydroethidine and 2′, 7′-dichlorofluorescin
    • Rothe, G., and Valet, J. (1990) Flow cytometric analysis of respiratory burst activity in phagocytes with hydroethidine and 2′, 7′-dichlorofluorescin.J. Leukoc. Biol. 47, 440-446
    • (1990) J. Leukoc. Biol. , vol.47 , pp. 440-446
    • Rothe, G.1    Valet, J.2
  • 35
    • 0028369668 scopus 로고
    • Intracellular hydrogen peroxide and superoxide anion detection in endothelial cells
    • Carter, W. O., Narayana, P. K., and Robinson, J. P. (1994) Intracellular hydrogen peroxide and superoxide anion detection in endothelial cells. J. Leukoc. Biol. 55, 253-258
    • (1994) J. Leukoc. Biol. , vol.55 , pp. 253-258
    • Carter, W.O.1    Narayana, P.K.2    Robinson, J.P.3
  • 36
    • 0022381068 scopus 로고
    • Ferric iron and superoxide ions are required for the killing of cultured hepatocytes by hydrogen peroxide. Evidence for the participation of hydroxyl radicals formed by an iron-catalyzed Haber-Weiss reaction
    • Starke, P. E., and Farber, J. L. (1985) Ferric iron and superoxide ions are required for the killing of cultured hepatocytes by hydrogen peroxide. Evidence for the participation of hydroxyl radicals formed by an iron-catalyzed Haber-Weiss reaction. J. Biol. Chem. 260, 10099-10104
    • (1985) J. Biol. Chem. , vol.260 , pp. 10099-10104
    • Starke, P.E.1    Farber, J.L.2
  • 37
    • 0028147329 scopus 로고
    • Inhibition of activation-induced death in T cell hybridomas by thiol antioxidants: Oxidative stress as a mediator of apoptosis
    • Sandstrom, P., Mannie, M., and Buttke, T. (1994) Inhibition of activation-induced death in T cell hybridomas by thiol antioxidants: oxidative stress as a mediator of apoptosis. J. Leukoc. Biol. 55, 221-226
    • (1994) J. Leukoc. Biol. , vol.55 , pp. 221-226
    • Sandstrom, P.1    Mannie, M.2    Buttke, T.3
  • 38
    • 0031034890 scopus 로고    scopus 로고
    • The induction of apoptosis in proliferating human fibroblasts by oxygen radicals in associated with p53-and p21WAF1CIP1 induction
    • Gansauge, S., Gansauge, F., Gause, H., Poch, H., Schoenberg, M., and Beger, H. (1997) The induction of apoptosis in proliferating human fibroblasts by oxygen radicals in associated with p53-and p21WAF1CIP1 induction. FEBS Lett. 404, 6-10
    • (1997) FEBS Lett. , vol.404 , pp. 6-10
    • Gansauge, S.1    Gansauge, F.2    Gause, H.3    Poch, H.4    Schoenberg, M.5    Beger, H.6
  • 40
    • 0027155884 scopus 로고
    • Autocrine production of extracellular catalase prevents apoptosis of the human CEM T-cell line in serum-free medium
    • Sandstrom, P. A., and Buttke, T. M. (1993) Autocrine production of extracellular catalase prevents apoptosis of the human CEM T-cell line in serum-free medium. Proc. Natl. Acad. Sci. USA 90, 4708-4712
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4708-4712
    • Sandstrom, P.A.1    Buttke, T.M.2
  • 41
    • 0027747273 scopus 로고
    • Exercise, oxidative stress, and antioxidants: A review
    • Jenkins, R. R. (1993) Exercise, oxidative stress, and antioxidants: a review. Int. J. Sports Nutr. 3, 356-375
    • (1993) Int. J. Sports Nutr. , vol.3 , pp. 356-375
    • Jenkins, R.R.1
  • 42
    • 0019860295 scopus 로고
    • Differential regulation of the messenger RNA for three major senescence marker protein in male rat liver
    • Chatterjee, B., Nath, T. S., and Roy, A. K. (1981) Differential regulation of the messenger RNA for three major senescence marker protein in male rat liver. J. Biol. Chem. 256, 5939-5941
    • (1981) J. Biol. Chem. , vol.256 , pp. 5939-5941
    • Chatterjee, B.1    Nath, T.S.2    Roy, A.K.3
  • 43
    • 0028918334 scopus 로고
    • Superoxide and hydrogenperoxide in relation to mammalian cell proliferation
    • Burdon, R. H. (1995) Superoxide and hydrogenperoxide in relation to mammalian cell proliferation. Free Rad. Biol. Med. 18, 775-749
    • (1995) Free Rad. Biol. Med. , vol.18 , pp. 775-1749
    • Burdon, R.H.1
  • 44
    • 0026341905 scopus 로고
    • Rapid and preferential activation of the c-jun gene during the mammalian UV-response
    • Devary, Y., Gottlieb, R. A., Lau, L. F., and Karin, M. (1991) Rapid and preferential activation of the c-jun gene during the mammalian UV-response. Mol. Cell. Biol. 11, 2804-2811
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2804-2811
    • Devary, Y.1    Gottlieb, R.A.2    Lau, L.F.3    Karin, M.4
  • 45
    • 0025916445 scopus 로고
    • Transcriptional activation of early response genes by hydrogen peroxide in mouse osteoblastic cell line
    • Nose, K., Shibanuma, M., Mikuchi, K., Kageyama, H., Sakiyama, S., and Kuroki, T. (1991) Transcriptional activation of early response genes by hydrogen peroxide in mouse osteoblastic cell line. Eur. J. Biochem. 201, 99-106
    • (1991) Eur. J. Biochem. , vol.201 , pp. 99-106
    • Nose, K.1    Shibanuma, M.2    Mikuchi, K.3    Kageyama, H.4    Sakiyama, S.5    Kuroki, T.6
  • 46
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of NF-κB transcription factor and HIV-1
    • Schreck, R., Rieher, P., and Bauerle, P. A. (1991) Reactive oxygen intermediates as apparently widely used messengers in the activation of NF-κB transcription factor and HIV-1. EMBO J. 10, 2247-2258
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieher, P.2    Bauerle, P.A.3
  • 47
    • 0029009883 scopus 로고
    • Activation of DNA synthesis and expression of the JE gene by catalase in mouse osteoblastic cells: Possible involvement of hydrogen peroxide in negative growth regulation
    • Shibanuma, M., Arata, S., Murata, M., and Nose, K. (1995) Activation of DNA synthesis and expression of the JE gene by catalase in mouse osteoblastic cells: possible involvement of hydrogen peroxide in negative growth regulation. Exp. Cell Res. 218, 132-136
    • (1995) Exp. Cell Res. , vol.218 , pp. 132-136
    • Shibanuma, M.1    Arata, S.2    Murata, M.3    Nose, K.4
  • 48
    • 0029832625 scopus 로고    scopus 로고
    • Identification of a novel growth-promoting factor with a wide target cell spectrum from various tumor cells as catalase
    • Miyamoto, T., Hayashi, M., Takeuchi, A., Okamoto, T., Kawashima, S., Takii, T., Hayashi, H., and Onozaki, K. (1996) Identification of a novel growth-promoting factor with a wide target cell spectrum from various tumor cells as catalase. J. Biochem 120, 725-730
    • (1996) J. Biochem , vol.120 , pp. 725-730
    • Miyamoto, T.1    Hayashi, M.2    Takeuchi, A.3    Okamoto, T.4    Kawashima, S.5    Takii, T.6    Hayashi, H.7    Onozaki, K.8
  • 49
    • 0030068056 scopus 로고    scopus 로고
    • Elevation in the ratio of Cu/Zn-superoxide dismutase to glutathione peroxidase activity induces features of cellular senescence and this effect is mediated by hydrogen peroxide
    • de Haan, J., Cristiano, F., Iannello, R., Bladier, C., Keiner, M., and Kola, I. (1996) Elevation in the ratio of Cu/Zn-superoxide dismutase to glutathione peroxidase activity induces features of cellular senescence and this effect is mediated by hydrogen peroxide. Hum. Mol. Genet. 2, 283-292
    • (1996) Hum. Mol. Genet. , vol.2 , pp. 283-292
    • De Haan, J.1    Cristiano, F.2    Iannello, R.3    Bladier, C.4    Keiner, M.5    Kola, I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.