메뉴 건너뛰기




Volumn 2, Issue 2, 2000, Pages 231-242

High-capacity redox control at the plasma membrane of mammalian cells: Trans-membrane, cell surface, and serum NADH-oxidases

Author keywords

[No Author keywords available]

Indexed keywords

REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; TETRAZOLIUM;

EID: 0033923221     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2000.2.2-231     Document Type: Review
Times cited : (77)

References (39)
  • 1
    • 0030933696 scopus 로고    scopus 로고
    • Regulation of glucose transport by interleukin-3 in growth factor-dependent and oncogene-transformed bone marrow-derived cell lines
    • AHMED, N., and BERRIDGE, M.V. (1997). Regulation of glucose transport by interleukin-3 in growth factor-dependent and oncogene-transformed bone marrow-derived cell lines. Leukemia Res., 21, 609-618.
    • (1997) Leukemia Res. , vol.21 , pp. 609-618
    • Ahmed, N.1    Berridge, M.V.2
  • 2
    • 0032538581 scopus 로고    scopus 로고
    • Transforming oncogenes regulate glucose transport by increasing transporter affinity for glucose: Contrasting effects of oncogenes and heat stress in a murine marrow-derived cell line
    • AHMED, N., and BERRIDGE, M.V. (1998). Transforming oncogenes regulate glucose transport by increasing transporter affinity for glucose: contrasting effects of oncogenes and heat stress in a murine marrow-derived cell line. Life Sci., 63, 1887-1903.
    • (1998) Life Sci. , vol.63 , pp. 1887-1903
    • Ahmed, N.1    Berridge, M.V.2
  • 4
    • 0027270211 scopus 로고
    • Characterization of the cellular reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT): Subcellular localization, substrate dependence, and involvement of mitochondrial electron transport in MTT reduction
    • BERRIDGE, M.V., and TAN, A.S. (1993). Characterization of the cellular reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT): subcellular localization, substrate dependence, and involvement of mitochondrial electron transport in MTT reduction. Arch. Biochem. Biophys. 303, 474-482.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 474-482
    • Berridge, M.V.1    Tan, A.S.2
  • 5
    • 0028961431 scopus 로고
    • Interleukin-3 facilitates glucose transport in a myeloid cell line by regulating the affinity of the glucose transporter for glucose: Involvement of protein phosphorylation in transporter activation
    • BERRIDGE, M.V., and TAN, A.S. (1995). Interleukin-3 facilitates glucose transport in a myeloid cell line by regulating the affinity of the glucose transporter for glucose: involvement of protein phosphorylation in transporter activation. Biochem. J. 305, 843-851.
    • (1995) Biochem. J. , vol.305 , pp. 843-851
    • Berridge, M.V.1    Tan, A.S.2
  • 6
    • 0032421938 scopus 로고    scopus 로고
    • Trans-plasma membrane electron transport: A cellular assay for NADH- and NADPH-oxidase based on extracellular, superoxide-mediated reduction of the sulfonated tetrazolium salt WST-1
    • BERRIDGE, M.V., and TAN, A.S. (1998). Trans-plasma membrane electron transport: a cellular assay for NADH-and NADPH-oxidase based on extracellular, superoxide-mediated reduction of the sulfonated tetrazolium salt WST-1. Protoplasma 205, 74-82.
    • (1998) Protoplasma , vol.205 , pp. 74-82
    • Berridge, M.V.1    Tan, A.S.2
  • 7
    • 85037966189 scopus 로고    scopus 로고
    • Diagnosis and monitoring of cancer. Provisional Patent, NZ334232
    • BERRIDGE, M.V., and TAN, A.S. (1999). Diagnosis and monitoring of cancer. Provisional Patent, NZ334232.
    • (1999)
    • Berridge, M.V.1    Tan, A.S.2
  • 8
    • 0033924222 scopus 로고    scopus 로고
    • Cell surface NAD(P)H-oxidase: Relationship to trans-plasma membrane NADH-oxidoreductase and a potential source of circulating NADH-oxidase
    • BERRIDGE, M.V., and TAN, A.S. (2000). Cell surface NAD(P)H-oxidase: relationship to trans-plasma membrane NADH-oxidoreductase and a potential source of circulating NADH-oxidase. Antiox. Redox Signal. 2,. 277-288.
    • (2000) Antiox. Redox Signal. , vol.2 , pp. 277-288
    • Berridge, M.V.1    Tan, A.S.2
  • 9
    • 0002531429 scopus 로고    scopus 로고
    • The biochemical and cellular basis of cell proliferation assays that use tetrazolium salts
    • BERRIDGE, M.V., TAN, A.S., McCOY, K.D., and WANG, R. (1996). The biochemical and cellular basis of cell proliferation assays that use tetrazolium salts. Biochemica 4,15-20.
    • (1996) Biochemica , vol.4 , pp. 15-20
    • Berridge, M.V.1    Tan, A.S.2    McCoy, K.D.3    Wang, R.4
  • 11
    • 0031172858 scopus 로고    scopus 로고
    • A 33.5-kDa heat- and protease-resistant NADH oxidase inhibited by capsaicin from sera of cancer patients
    • CHUEH, P.J., MORRÉ, D.J., WILKINSON, F.E., GIBSON, J., and MORRÉ, D.M. (1997). A 33.5-kDa heat-and protease-resistant NADH oxidase inhibited by capsaicin from sera of cancer patients. Archiv. Biochem. Biophys. 342, 38-47.
    • (1997) Archiv. Biochem. Biophys. , vol.342 , pp. 38-47
    • Chueh, P.J.1    Morré, D.J.2    Wilkinson, F.E.3    Gibson, J.4    Morré, D.M.5
  • 15
    • 0023926013 scopus 로고
    • Activation and proliferation signals in murine macrophages: Stimulation of glucose uptake by hemopoietic growth factors and other agents
    • HAMILTON, J.A., VAIRO, G., and LINGELBACH, S.R. (1988). Activation and proliferation signals in murine macrophages: stimulation of glucose uptake by hemopoietic growth factors and other agents. J. Cell. Physiol. 134, 405-412.
    • (1988) J. Cell. Physiol. , vol.134 , pp. 405-412
    • Hamilton, J.A.1    Vairo, G.2    Lingelbach, S.R.3
  • 16
    • 0027249291 scopus 로고
    • A new sulfonated tetrazolium salt that produces a highly water-soluble formazan dye
    • ISHIYAMA, M., SHIGA, M., SASAMOTO, K., MIZOGUCHI, M., and HE, P.G. (1993). A new sulfonated tetrazolium salt that produces a highly water-soluble formazan dye. Chem. Pharmaceut. Bull. 41, 1118-1122.
    • (1993) Chem. Pharmaceut. Bull. , vol.41 , pp. 1118-1122
    • Ishiyama, M.1    Shiga, M.2    Sasamoto, K.3    Mizoguchi, M.4    He, P.G.5
  • 17
    • 0043065851 scopus 로고
    • Novel disulfonated tetrazolium salt that can be reduced to a water-soluble formazan and its application to the assay of lactate-dehydrogenase
    • ISHIYAMA, M., SASAMOTO, K., SHIGA, M., OHKURA, Y., UENO, K., NISHIYAMA, K., and TANIGUCHI, I. (1995). Novel disulfonated tetrazolium salt that can be reduced to a water-soluble formazan and its application to the assay of lactate-dehydrogenase. Analyst 120, 113-116.
    • (1995) Analyst , vol.120 , pp. 113-116
    • Ishiyama, M.1    Sasamoto, K.2    Shiga, M.3    Ohkura, Y.4    Ueno, K.5    Nishiyama, K.6    Taniguchi, I.7
  • 18
    • 0032943350 scopus 로고    scopus 로고
    • The plasma membrane NADH oxidase of HeLa cells has hydroquinone oxidase activity
    • KISHI, T., MORRÉ, D.M., and MORRÉ, D.J. (1999). The plasma membrane NADH oxidase of HeLa cells has hydroquinone oxidase activity. Biochim. Biophys. Acta 1412, 66-77.
    • (1999) Biochim. Biophys. Acta , vol.1412 , pp. 66-77
    • Kishi, T.1    Morré, D.M.2    Morré, D.J.3
  • 19
    • 0028028302 scopus 로고
    • Up-regulation of the plasma membrane oxidoreductase as a prerequisite for the viability of human Namalwa rho 0 cells
    • LARM, J.A., VAILLANT, F., LINNANE, A.W., and LAWEN, A. (1994). Up-regulation of the plasma membrane oxidoreductase as a prerequisite for the viability of human Namalwa rho 0 cells. J. Biol. Chem. 269, 30097-30100.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30097-30100
    • Larm, J.A.1    Vaillant, F.2    Linnane, A.W.3    Lawen, A.4
  • 20
    • 0030859012 scopus 로고    scopus 로고
    • The hemopoietic growth factor, interleukin-3, promotes glucose transport by increasing the specific activity and maintaining the affinity for glucose of plasma membrane glucose transporters
    • McCOY, K.D., AHMED, N., TAN, A.S., and BERRIDGE, M.V. (1997). The hemopoietic growth factor, interleukin-3, promotes glucose transport by increasing the specific activity and maintaining the affinity for glucose of plasma membrane glucose transporters. J. Biol. Chem. 272, 17276-17282.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17276-17282
    • McCoy, K.D.1    Ahmed, N.2    Tan, A.S.3    Berridge, M.V.4
  • 21
    • 0027772521 scopus 로고
    • Growth factors, mitogens, oncogenes and the regulation of glucose transport
    • MERRALL, N.W., PLEVIN, R., and GOULD, G.W. (1993). Growth factors, mitogens, oncogenes and the regulation of glucose transport. Cell. Signal., 5, 667-675.
    • (1993) Cell. Signal. , vol.5 , pp. 667-675
    • Merrall, N.W.1    Plevin, R.2    Gould, G.W.3
  • 24
    • 0028925916 scopus 로고
    • Capsaicin inhibits preferentially the NADH oxidase and growth of transformed cells in culture
    • MORRÉ, D.J., CHUEH, P.J., and MORRÉ, D.M. (1995a). Capsaicin inhibits preferentially the NADH oxidase and growth of transformed cells in culture. Proc. Natl. Acad. Sci. USA, 92, 1831-1835.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1831-1835
    • Morré, D.J.1    Chueh, P.J.2    Morré, D.M.3
  • 28
    • 0031570783 scopus 로고    scopus 로고
    • NADH oxidase activity from sera altered by capsaicin is widely distributed among cancer patients
    • MORRÉ, D.J., CALDWELL, S., MAYORGA, A., WU, L.Y., and MORRÉ, D.M. (1997). NADH oxidase activity from sera altered by capsaicin is widely distributed among cancer patients. Archiv. Biochem. Biophys. 342, 224-230.
    • (1997) Archiv. Biochem. Biophys. , vol.342 , pp. 224-230
    • Morré, D.J.1    Caldwell, S.2    Mayorga, A.3    Wu, L.Y.4    Morré, D.M.5
  • 29
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxic assays
    • MOSMANN, T. (1983). Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxic assays. J. Immunol. Meth. 65, 55-63.
    • (1983) J. Immunol. Meth. , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 30
    • 0029761703 scopus 로고    scopus 로고
    • High rates of extracellular superoxide generation by cultured human fibroblasts: Involvement of a lipid-metabolizing enzyme
    • O'DONNELL, V.B., and AZZI, A. (1996). High rates of extracellular superoxide generation by cultured human fibroblasts: involvement of a lipid-metabolizing enzyme. Biochem. J. 318, 805-812.
    • (1996) Biochem. J. , vol.318 , pp. 805-812
    • O'Donnell, V.B.1    Azzi, A.2
  • 32
    • 0024574153 scopus 로고
    • Capsaicin and its analogs inhibit the activity of NADH-coenzyme Q oxidoreductase of the mitochondrial respiratory chain
    • SHIMOMURA, Y., KAWADA, T., and SUZUKI, M. (1989). Capsaicin and its analogs inhibit the activity of NADH-coenzyme Q oxidoreductase of the mitochondrial respiratory chain. Arch. Biochem. Biophys. 270, 573-577.
    • (1989) Arch. Biochem. Biophys. , vol.270 , pp. 573-577
    • Shimomura, Y.1    Kawada, T.2    Suzuki, M.3
  • 33
    • 0034697387 scopus 로고    scopus 로고
    • Superoxide produced by activated neutrophils efficiently reduces the tetrazolium salt, WST-1 to produce a soluble formazan: A simple colorimetric assay for measuring respiratory burst activation and for screening anti-inflammatory agents
    • TAN, A.S., and BERRIDGE, M.V. (2000). Superoxide produced by activated neutrophils efficiently reduces the tetrazolium salt, WST-1 to produce a soluble formazan: a simple colorimetric assay for measuring respiratory burst activation and for screening anti-inflammatory agents. J. Immunol. Methods 238, 59-68.
    • (2000) J. Immunol. Methods , vol.238 , pp. 59-68
    • Tan, A.S.1    Berridge, M.V.2
  • 34
    • 0025144664 scopus 로고
    • + exchange involvement in colony-stimulating factor-1-stimulated macrophage proliferation. Evidence for a requirement during late G1 of the cell cycle but not for early growth factor responses
    • + exchange involvement in colony-stimulating factor-1-stimulated macrophage proliferation. Evidence for a requirement during late G1 of the cell cycle but not for early growth factor responses. J. Biol. Chem. 265, 16929-16939.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16929-16939
    • Vairo, G.1    Argyriou, S.2    Bordun, A.3    Gonda, T.J.4    Cragoe, E.J.5    Hamilton, J.A.6
  • 35
    • 0029065701 scopus 로고
    • Coenzyme Q reductase from liver plasma membrane: Purification and role in trans-plasma-membrane electron transport
    • VILLALBA, J.M., NAVARRO, F., CORDOBA, F., SERRANO, A., ARROYO, A., CRANE, F.L., and NAVAS, P. (1995). Coenzyme Q reductase from liver plasma membrane: purification and role in trans-plasma-membrane electron transport. Proc. Natl. Acad. Sci. USA, 92, 4887-4891.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4887-4891
    • Villalba, J.M.1    Navarro, F.2    Cordoba, F.3    Serrano, A.4    Arroyo, A.5    Crane, F.L.6    Navas, P.7
  • 36
    • 0008595699 scopus 로고
    • Quantitative estimation of the reducing power of normal and cancer tissue
    • VOEGTLIN, C., JOHNSON, J.M., and DYER, H.A. (1925). Quantitative estimation of the reducing power of normal and cancer tissue. J. Pharmacol. Exp. Ther. 24, 305.
    • (1925) J. Pharmacol. Exp. Ther. , vol.24 , pp. 305
    • Voegtlin, C.1    Johnson, J.M.2    Dyer, H.A.3
  • 37
    • 0027455325 scopus 로고
    • GM-CSF triggers a rapid, glucose dependent extracellular acidification by TF-1 cells-evidence for sodium/proton antiporter and PKC mediated activation of acid production
    • WADA, H.G., INDELICATO, S.R., MEYER, L., KITAMURA, T., MIYAJIMA, A., KIRK, G., MUIR, V.C., and PARCE, J.W. (1993). GM-CSF triggers a rapid, glucose dependent extracellular acidification by TF-1 cells-evidence for sodium/proton antiporter and PKC mediated activation of acid production. J. Cell Physiol. 154, 129-138.
    • (1993) J. Cell Physiol. , vol.154 , pp. 129-138
    • Wada, H.G.1    Indelicato, S.R.2    Meyer, L.3    Kitamura, T.4    Miyajima, A.5    Kirk, G.6    Muir, V.C.7    Parce, J.W.8
  • 38
    • 0030013044 scopus 로고    scopus 로고
    • The chronic administration of drugs that inhibit the regulation of intracellular pH: In vitro and anti-tumour effects
    • YAMAGATA, M., and TANNOCK, I.F. (1996). The chronic administration of drugs that inhibit the regulation of intracellular pH: in vitro and anti-tumour effects. Br. J. Cancer 73, 1328-1334.
    • (1996) Br. J. Cancer , vol.73 , pp. 1328-1334
    • Yamagata, M.1    Tannock, I.F.2
  • 39
    • 0030600225 scopus 로고    scopus 로고
    • The plasma membrane NADH-diaphorase is active during selective phases of the cell cycle in mouse neuroblastoma cell line NB41A3. Its relation to cell growth and differentiation
    • ZURBRIGGEN, R., and DREYER, J.L. (1996). The plasma membrane NADH-diaphorase is active during selective phases of the cell cycle in mouse neuroblastoma cell line NB41A3. Its relation to cell growth and differentiation. Biochim. Biophys. Acta 1312, 215-222.
    • (1996) Biochim. Biophys. Acta , vol.1312 , pp. 215-222
    • Zurbriggen, R.1    Dreyer, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.