Molecular Cloning and Characterization of a Candidate Plant Growth-Related and Time-Keeping Constitutive Cell Surface Hydroquinone (NADH) Oxidase (ENOX1) from Arabidopsis lyrata
ABSTRACT
ENOX (ECTO-NOX) proteins are proteins of the external surface of the plasma membrane that catalyze oxidation of both NADH and hydroquinones as well as carry out protein disulfidethiol interchange. They exhibit both prion-like and time-keeping (clock) properties. The oxidative and interchange activities alternate to generate a regular period of 24 min in length. Here we report the cloning, expression, and characterization of a plant candidate constitutive ENOX (CNOX or ENOX1) protein from Arabidopsis lyrata. The gene encoding the 335 (165) amino acid protein is found in accession XP-002882467. Functional motifs characteristics of ENOX proteins previously identified by site-directed mutagenesis and present in the candidate ENOX1 protein from plants include adenine nucleotide and copper binding motifs along with essential cysteines. However, the drug binding motif (EEMTE) sequence of human ENOX2 is absent. The activities of the recombinant protein expressed in E. coli were unaffected by capsaicin, EGCg, and other ENOX2-inhibiting substances. Periodic oxidative activity was exhibited both with NAD(P)H and reduced coenzyme Q as substrate. Bound copper was necessary for activity and activity was inhibited by the ENOX1-specific inhibitor simalikalactone D. Addition of melatonin phased the 24-min period such that the next complete period began 24 min after the melatonin addition as appeared to be characteristic of ENOX1 activities in general. Periodic protein disulfide-thiol interchange activity also was demonstrated along with the 2 oxidative plus 3 interchange activity pattern characteristics of the 24-min ENOX1 protein period. Concentrated solutions of the purified plant ENOX1 protein formed insoluble aggregates, devoid of enzymatic activity, resembling amyloid. Activity was restored to aggregate preparations by isoelectric focusing.
ENOX (ECTO-NOX) proteins are proteins of the external surface of the plasma membrane that catalyze oxidation of both NADH and hydroquinones as well as carry out protein disulfidethiol interchange. They exhibit both prion-like and time-keeping (clock) properties. The oxidative and interchange activities alternate to generate a regular period of 24 min in length. Here we report the cloning, expression, and characterization of a plant candidate constitutive ENOX (CNOX or ENOX1) protein from Arabidopsis lyrata. The gene encoding the 335 (165) amino acid protein is found in accession XP-002882467. Functional motifs characteristics of ENOX proteins previously identified by site-directed mutagenesis and present in the candidate ENOX1 protein from plants include adenine nucleotide and copper binding motifs along with essential cysteines. However, the drug binding motif (EEMTE) sequence of human ENOX2 is absent. The activities of the recombinant protein expressed in E. coli were unaffected by capsaicin, EGCg, and other ENOX2-inhibiting substances. Periodic oxidative activity was exhibited both with NAD(P)H and reduced coenzyme Q as substrate. Bound copper was necessary for activity and activity was inhibited by the ENOX1-specific inhibitor simalikalactone D. Addition of melatonin phased the 24-min period such that the next complete period began 24 min after the melatonin addition as appeared to be characteristic of ENOX1 activities in general. Periodic protein disulfide-thiol interchange activity also was demonstrated along with the 2 oxidative plus 3 interchange activity pattern characteristics of the 24-min ENOX1 protein period. Concentrated solutions of the purified plant ENOX1 protein formed insoluble aggregates, devoid of enzymatic activity, resembling amyloid. Activity was restored to aggregate preparations by isoelectric focusing.
KEYWORDS
ENOX1, ECTO-NOX Proteins, Plant Growth, Hydroquinone (NADH) Oxidation, Plasma Membrane Electron Transport, Arabadopsis lyrata
ENOX1, ECTO-NOX Proteins, Plant Growth, Hydroquinone (NADH) Oxidation, Plasma Membrane Electron Transport, Arabadopsis lyrata
Cite this paper
Tang, X. , Ades, L. , Morré, D. and Morré, D. (2015) Molecular Cloning and Characterization of a Candidate Plant Growth-Related and Time-Keeping Constitutive Cell Surface Hydroquinone (NADH) Oxidase (ENOX1) from Arabidopsis lyrata. Advances in Biological Chemistry, 5, 1-15. doi: 10.4236/abc.2015.51001.
Tang, X. , Ades, L. , Morré, D. and Morré, D. (2015) Molecular Cloning and Characterization of a Candidate Plant Growth-Related and Time-Keeping Constitutive Cell Surface Hydroquinone (NADH) Oxidase (ENOX1) from Arabidopsis lyrata. Advances in Biological Chemistry, 5, 1-15. doi: 10.4236/abc.2015.51001.
References
[1] Morré, D.J. (1998) NADH Oxidase: A Multifunctional Ectoproteins of the Eukaryotic Cell Surface. In: Asard, H., Bérczi, A. and Caubergs, R., Eds., Plasma Membrane Redox Systems and Their Role in Biological Stress and Disease, Kluwer Academic Publishers, Dordrecht, 121-156.
http://dx.doi.org/10.1007/978-94-017-2695-5_5 [2] Morré, D.J. and Morré, D.M. (2003) Cell Surface NADH Oxidases (ECTO-NOX Proteins) with Roles in Cancer, Cellular Time-Keeping, Growth, Aging and Neurodegenerative Disease. Free Radical Research, 37, 795-808.
http://dx.doi.org/10.1080/1071576031000083107 [3] Morré, D.J. and Morré, D.M. (2013) ECTO-NOX Proteins. Springer, New York, 507 p.
http://dx.doi.org/10.1007/978-1-4614-3958-5 [4] Jiang, Z., Gorenstein, N.M., Morré, D.M. and Morré, D.J. (2008) Molecular Cloning and Characterization of a Candidate Human Growth-Related and Time-Keeping Constitutive Cell Surface Hydroquinone (NADH) Oxidase. Biochemistry, 47, 14028-14038.
http://dx.doi.org/10.1021/bi801073p [5] Chueh, P.-J., Morré, D.J., Wilkinson, F.E., Gibson, J. and Morré, D.M. (l997) A 33.5 kDa Heat- and Protease-Resistant NADH Oxidase Inhibited by Capsaicin from Sera of Cancer Patients. Archives of Biochemistry and Biophysics, 342, 38-47.
http://dx.doi.org/10.1006/abbi.1997.9992 [6] Chueh, P.-J., Kim, C., Cho, N., Morré, D.M. and Morré, D.J. (2002) Molecular Cloning and Characterization of a Tumor-Associated, Growth-Related and Time-Keeping Hydro-quinone (NADH) Oxidase (NOX) of the HeLa Cell Surface. Biochemistry, 41, 3732-3741.
http://dx.doi.org/10.1021/bi012041t [7] Morré, D.J., Chueh, P.-J. and Morré, D.M. (1995) Capsaicin Inhibits Preferentially the NADH Oxidase and Growth of Transformed Cells in Culture. Proceedings of the National Academy of Sciences USA, 92, 1831-1835.
http://dx.doi.org/10.1073/pnas.92.6.1831 [8] Morré, D.J., Sun, E., Geilen, C., Wu, L.-Y., De Cabo, R., Krasagakis, K., Orfanos, C.E. and Morré, D.M. (1996) Capsaicin Inhibits Plasma Membrane NADH Oxidase and Growth of Human and Mouse Melanoma Lines. European Journal of Cancer, 32A, 1995-2003.
http://dx.doi.org/10.1016/0959-8049(96)00234-1 [9] Morré, D.J., Wu, L.-Y. and Morré, D.M. (1995) The Antitumor Sulfonylurea N-(4-methylphenylsulfonyl)-N(-(chlorophenyl)urea (LY181984) Inhibits NADH Oxidase Activity of HeLa Plasma Membranes. Biochimica et Biophysica Acta, 1240, 11-17.
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http://dx.doi.org/10.1016/S0024-3205(98)00310-5 [13] Morré, D.J. and Greico, P.A. (1999) Glaucarubolone and Simalikalactone D, Respectively, Preferentially Inhibit Auxin-Induced and Constitutive Components of Plant Cell Enlargement and the Plasma Membrane NADH Oxidase. International Journal of Plant Sciences, 160, 291-297.
http://dx.doi.org/10.1086/314133 [14] Wilkinson, F.E., Kim, C., Cho, N., Chueh, P.-J., Leslie, S., Mo-ya-Camarena, S., Wu, L.-Y., Morré, D.M. and Morré, D.J. (l996) Isolation and Identification of a Protein with Capsaicin-Inhibited NADH Oxidase Activity from Culture Media Conditioned by Growth of HeLa Cells. Archives of Bio-chemistry and Biophysics, 336, 275-282.
http://dx.doi.org/10.1006/abbi.1996.0558 [15] Sedlak, D., Morré, D.M. and Morré, D.J. (2001) A Drug-Unresponsive and Protease-Resistant CNOX Protein from Human Sera. Archives of Biochemistry and Biophysics, 386, 106-116.
http://dx.doi.org/10.1006/abbi.2000.2180 [16] Morré, D.M. and Morré, D.J. (2003) Specificity of Coenzyme Q Inhibition of an Aging-Related Cell Surface NADH Oxidase (ECTO-NOX) That Generates Superoxide. BioFactors, 18, 33-43.
http://dx.doi.org/10.1002/biof.5520180205 [17] Dick, S., Phung, C., Morré, D.M. and Morré, D.J. (2013) Molecular Cloning and Characterization of an ECTO-NOX3 (ENOX3) of Saccharomyces cerevisiae. Advances in Biological Chemistry, 3, 505-511.
http://dx.doi.org/10.4236/abc.2013.35055 [18] Morré, D.M., Guo, F. and Morré, D.J. (2003) An Aging-Related Cell Surface NADH Oxidase (arNOX) Generates Superoxide and Is Inhibited by Coenzyme Q. Molecular and Cellular Biochemistry, 254, 101-109.
http://dx.doi.org/10.1023/A:1027301405614 [19] Pogue, R., Morré, D.M. and Morré, D.J. (2000) CHO Cell Enlargement Oscillates with a Temperature-Compensated Period of 24 Minutes. Biochimica et Biophysica Acta, 1498, 44-51.
http://dx.doi.org/10.1016/S0167-4889(00)00076-8 [20] Morré, D.J., Pogue, R. and Morré, D.M. (2001) Soybean Cell Enlargement Oscillates with a Temperature-Compensated Period Length of ca. 24 Min. In Vitro Cellular & Devel-opmental Biology-Plant, 37, 19-23.
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http://dx.doi.org/10.1079/IVP2001249 [22] Morré, D.J., Brightman, A.O., Hidalgo, A. and Navas, P. (1995) Selective Inhibition of Auxin-Stimulated NADH Oxidase Activity and Elongation Growth of Soybean Hypocotyls by Thiol Reagents. Plant Physiology, 107, 1285-1291. [23] Kishi, T., Morré, D.M. and Morré, D.J. (1999) The Plasma Membrane NADH Oxidase of HeLa Cells Has Hydroquinone Oxidase Activity. Biochimica et Biophysica Acta, 1412, 66-77.
http://dx.doi.org/10.1016/S0005-2728(99)00049-3 [24] Morré, D.J., De Cabo, R., Jacobs, E. and Morré, D.M. (1995) Auxin-Modulated Protein Disulfide-Thiol Interchange Activity from Soybean Plasma Membranes. Plant Physiology, 109, 573-578. [25] Morré, D.J., Gomez-Rey, M.L., Schramke, C., Em, O., Lawler, J., Hobeck, J. and Morré, D.M. (1999) Use of Dipyridyl-Dithio Substrates to Measure Directly the Protein Disulfide-Thiol Interchange Activity of the Auxin Stimulated NADH: Protein Disulfide Reductase (NADH Oxidase) of Soybean Plasma Membranes. Molecular and Cellular Biochemistry, 200, 7-13.
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[1] Morré, D.J. (1998) NADH Oxidase: A Multifunctional Ectoproteins of the Eukaryotic Cell Surface. In: Asard, H., Bérczi, A. and Caubergs, R., Eds., Plasma Membrane Redox Systems and Their Role in Biological Stress and Disease, Kluwer Academic Publishers, Dordrecht, 121-156.
http://dx.doi.org/10.1007/978-94-017-2695-5_5 [2] Morré, D.J. and Morré, D.M. (2003) Cell Surface NADH Oxidases (ECTO-NOX Proteins) with Roles in Cancer, Cellular Time-Keeping, Growth, Aging and Neurodegenerative Disease. Free Radical Research, 37, 795-808.
http://dx.doi.org/10.1080/1071576031000083107 [3] Morré, D.J. and Morré, D.M. (2013) ECTO-NOX Proteins. Springer, New York, 507 p.
http://dx.doi.org/10.1007/978-1-4614-3958-5 [4] Jiang, Z., Gorenstein, N.M., Morré, D.M. and Morré, D.J. (2008) Molecular Cloning and Characterization of a Candidate Human Growth-Related and Time-Keeping Constitutive Cell Surface Hydroquinone (NADH) Oxidase. Biochemistry, 47, 14028-14038.
http://dx.doi.org/10.1021/bi801073p [5] Chueh, P.-J., Morré, D.J., Wilkinson, F.E., Gibson, J. and Morré, D.M. (l997) A 33.5 kDa Heat- and Protease-Resistant NADH Oxidase Inhibited by Capsaicin from Sera of Cancer Patients. Archives of Biochemistry and Biophysics, 342, 38-47.
http://dx.doi.org/10.1006/abbi.1997.9992 [6] Chueh, P.-J., Kim, C., Cho, N., Morré, D.M. and Morré, D.J. (2002) Molecular Cloning and Characterization of a Tumor-Associated, Growth-Related and Time-Keeping Hydro-quinone (NADH) Oxidase (NOX) of the HeLa Cell Surface. Biochemistry, 41, 3732-3741.
http://dx.doi.org/10.1021/bi012041t [7] Morré, D.J., Chueh, P.-J. and Morré, D.M. (1995) Capsaicin Inhibits Preferentially the NADH Oxidase and Growth of Transformed Cells in Culture. Proceedings of the National Academy of Sciences USA, 92, 1831-1835.
http://dx.doi.org/10.1073/pnas.92.6.1831 [8] Morré, D.J., Sun, E., Geilen, C., Wu, L.-Y., De Cabo, R., Krasagakis, K., Orfanos, C.E. and Morré, D.M. (1996) Capsaicin Inhibits Plasma Membrane NADH Oxidase and Growth of Human and Mouse Melanoma Lines. European Journal of Cancer, 32A, 1995-2003.
http://dx.doi.org/10.1016/0959-8049(96)00234-1 [9] Morré, D.J., Wu, L.-Y. and Morré, D.M. (1995) The Antitumor Sulfonylurea N-(4-methylphenylsulfonyl)-N(-(chlorophenyl)urea (LY181984) Inhibits NADH Oxidase Activity of HeLa Plasma Membranes. Biochimica et Biophysica Acta, 1240, 11-17.
http://dx.doi.org/10.1016/0005-2736(95)00164-7 [10] Morré, D.J., Wilkinson, F.E., Kim, C., Cho, N., Lawrence, J., Morré, D.M. and McClure, D. (l996) Antitumor Sulfonylurea-Inhibited NADH Oxidase of Cultured HeLa Cells Shed into Media. Biochimica et Biophysica Acta, 1280, 197- 206.
http://dx.doi.org/10.1016/0005-2736(95)00290-1 [11] Morré, D.J., Chueh, P.-J., Yagiz, K., Balicki, A., Kim, C. and Morré, D.M. (2007) ECTO-NOX Target for the Anticancer Isoflavene Phenoxodiol. Oncology Research, 16, 299-312. [12] Morré, D.J., Grieco, P.A. and Morré, D.M. (1998) Mode of Action of the Anticancer Quas-sinoids-Inhibition of the Plasma Membrane NADH Oxidase. Life Science, 63, 595-604.
http://dx.doi.org/10.1016/S0024-3205(98)00310-5 [13] Morré, D.J. and Greico, P.A. (1999) Glaucarubolone and Simalikalactone D, Respectively, Preferentially Inhibit Auxin-Induced and Constitutive Components of Plant Cell Enlargement and the Plasma Membrane NADH Oxidase. International Journal of Plant Sciences, 160, 291-297.
http://dx.doi.org/10.1086/314133 [14] Wilkinson, F.E., Kim, C., Cho, N., Chueh, P.-J., Leslie, S., Mo-ya-Camarena, S., Wu, L.-Y., Morré, D.M. and Morré, D.J. (l996) Isolation and Identification of a Protein with Capsaicin-Inhibited NADH Oxidase Activity from Culture Media Conditioned by Growth of HeLa Cells. Archives of Bio-chemistry and Biophysics, 336, 275-282.
http://dx.doi.org/10.1006/abbi.1996.0558 [15] Sedlak, D., Morré, D.M. and Morré, D.J. (2001) A Drug-Unresponsive and Protease-Resistant CNOX Protein from Human Sera. Archives of Biochemistry and Biophysics, 386, 106-116.
http://dx.doi.org/10.1006/abbi.2000.2180 [16] Morré, D.M. and Morré, D.J. (2003) Specificity of Coenzyme Q Inhibition of an Aging-Related Cell Surface NADH Oxidase (ECTO-NOX) That Generates Superoxide. BioFactors, 18, 33-43.
http://dx.doi.org/10.1002/biof.5520180205 [17] Dick, S., Phung, C., Morré, D.M. and Morré, D.J. (2013) Molecular Cloning and Characterization of an ECTO-NOX3 (ENOX3) of Saccharomyces cerevisiae. Advances in Biological Chemistry, 3, 505-511.
http://dx.doi.org/10.4236/abc.2013.35055 [18] Morré, D.M., Guo, F. and Morré, D.J. (2003) An Aging-Related Cell Surface NADH Oxidase (arNOX) Generates Superoxide and Is Inhibited by Coenzyme Q. Molecular and Cellular Biochemistry, 254, 101-109.
http://dx.doi.org/10.1023/A:1027301405614 [19] Pogue, R., Morré, D.M. and Morré, D.J. (2000) CHO Cell Enlargement Oscillates with a Temperature-Compensated Period of 24 Minutes. Biochimica et Biophysica Acta, 1498, 44-51.
http://dx.doi.org/10.1016/S0167-4889(00)00076-8 [20] Morré, D.J., Pogue, R. and Morré, D.M. (2001) Soybean Cell Enlargement Oscillates with a Temperature-Compensated Period Length of ca. 24 Min. In Vitro Cellular & Devel-opmental Biology-Plant, 37, 19-23.
http://dx.doi.org/10.1007/s11627-001-0004-3 [21] Morré, D.J., Ternes, P. and Morré, D.M. (2002) Cell Enlargement of Plant Tissue Explants Oscillates with a Temperature-Compensated Period Length of ca. 24 Min. In Vitro Cellular & Developmental Biology-Plant, 38, 18-28.
http://dx.doi.org/10.1079/IVP2001249 [22] Morré, D.J., Brightman, A.O., Hidalgo, A. and Navas, P. (1995) Selective Inhibition of Auxin-Stimulated NADH Oxidase Activity and Elongation Growth of Soybean Hypocotyls by Thiol Reagents. Plant Physiology, 107, 1285-1291. [23] Kishi, T., Morré, D.M. and Morré, D.J. (1999) The Plasma Membrane NADH Oxidase of HeLa Cells Has Hydroquinone Oxidase Activity. Biochimica et Biophysica Acta, 1412, 66-77.
http://dx.doi.org/10.1016/S0005-2728(99)00049-3 [24] Morré, D.J., De Cabo, R., Jacobs, E. and Morré, D.M. (1995) Auxin-Modulated Protein Disulfide-Thiol Interchange Activity from Soybean Plasma Membranes. Plant Physiology, 109, 573-578. [25] Morré, D.J., Gomez-Rey, M.L., Schramke, C., Em, O., Lawler, J., Hobeck, J. and Morré, D.M. (1999) Use of Dipyridyl-Dithio Substrates to Measure Directly the Protein Disulfide-Thiol Interchange Activity of the Auxin Stimulated NADH: Protein Disulfide Reductase (NADH Oxidase) of Soybean Plasma Membranes. Molecular and Cellular Biochemistry, 200, 7-13.
http://dx.doi.org/10.1023/A:1006916116297 [26] Morré, D.J., Chueh, P.-J., Pletcher, J., Tang, X.Y., Wu, L.-Y. and Morré, D.M. (2002) Biochemical Basis for the Biological Clock. Biochemistry, 41, 11941-11945.
http://dx.doi.org/10.1021/bi020392h [27] Chueh, P.-J., Morré, D.M. and Morré, D.J. (2002) A Site-Directed Mutagenesis Analysis of tNOX Functional Domains. Biochimica et Biophysica Acta, 1594, 74-83.
http://dx.doi.org/10.1016/S0167-4838(01)00286-2 [28] Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W. and Lipman, D.J. (1997) Gapped BLAST and PSI-BLAST: A New Generation of Protein Database Search Programs. Nucleic Acids Research, 25, 3389-3402.
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http://dx.doi.org/10.4236/abc.2013.33036 [30] Smith, P.K., Krohn, R.I., Hermanson, G.T., Mailia, A.K., Gartner, F.F., Provenzano, M.D., Fujimoto, E.K., Groeke, N.M., Olson, B.J. and Klenk, D.C. (1985) Measurement of Protein Using Bicinchoninic Acid. Analytical Biochemistry, 150, 76-85.
http://dx.doi.org/10.1016/0003-2697(85)90442-7 [31] Braman, J., Papworth, C. and Greener, A. (1996) Site-Directed Mutagenesis Using Double-Stranded Plasmid DNA Templates. Methods Molecular Biology, 57, 31-44. [32] Brightman, A.O., Wang, J., Miu, R.K., Sun, I.L., Barr, R., Crane, F.L. and Morré, D.J. (1992) A Growth Factor- and Hormone-Stimulated NADH Oxidase from Rat Liver Plasma Membrane. Biochimica et Biophysica Acta, 1105, 109-117.
http://dx.doi.org/10.1016/0005-2736(92)90168-L [33] Morré, D.J. and Brightman, A.O. (1991) NADH Oxidase of Plasma Membranes. Journal of Bioenergetics and Biomembranes, 23, 469-489.
http://dx.doi.org/10.1007/BF00771015 [34] Brightman, A.O., Barr, R., Crane, F.L. and Morré, D.J. (1988) Aux-in-Stimulated NADH Oxidase Purified from Plasma Membrane of Soybean. Plant Physiology, 86, 1264-1269.
http://dx.doi.org/10.1104/pp.86.4.1264 [35] Morré, D.J. and Morré, D.M. (1998) NADH Oxidase Activity of Soybean Plasma Membrane Oscillates with a Temperature Compensated Period of 24 Min. The Plant Journal, 16, 279-284.
http://dx.doi.org/10.1046/j.1365-313x.1998.00293.x [36] Morré, D.J., Penel, C., Greppin, H. and Morré, D.M. (2002) The Plasma Membrane-Associated NADH Oxidase of Spinach Leaves Responds to Blue Light. Inter-national Journal of Plant Sciences, 613, 543-547.
http://dx.doi.org/10.1086/340543 [37] Kelker, M., Kim, C., Chueh, P.J., Guimont, R., Morré, D.M. and Morré, D.J. (2001) Cancer Isoform of a Tumor-As- sociated Cell Surface NADH Oxidase (tNOX) Has Properties of a Prion. Biochemistry, 40, 7351-7354.
http://dx.doi.org/10.1021/bi010596i [38] Kim, C. and Morré, D.J. (2004) Prion Proteins and ECTO-NOX Proteins Exhibit Similar Oscillating Redox Activities. Biochemical and Biophysical Research Communications, 315, 1140-1146.
http://dx.doi.org/10.1016/j.bbrc.2004.02.007 [39] Griffith, J.S. (1964) Self-Replication and Scrapie. Nature, 315, 1043-1044. [40] Prusiner, S.B. (1994) Biology and Genetics of Prion Diseases. Annual Review of Microbiology, 48, 655-686.
http://dx.doi.org/10.1146/annurev.mi.48.100194.003255 [41] Multhaup, G. (1997) Amyloid Precursor Protein, Copper and Alzheimer’s Disease. Biomedicine & Pharmacotherapy, 51, 105-111.
http://dx.doi.org/10.1016/S0753-3322(97)86907-7 [42] del Castillo-Olivares, A., Yantiri, F., Chueh, P.-J., Wang, S., Sweeting, M., Sedlak, D., Morré, D.M., Burgess, J. and Morré, D.J. (1998) A Drug-Responsive and Protease-Resistant Peripheral NADH Oxidase Complex from the Surface of HeLa S Cells. Archives of Biochemistry and Biophysics, 358, 125-140.
http://dx.doi.org/10.1006/abbi.1998.0823 [43] Rangachari, V., Morré, B.D., Reed, D.K., Sonoda, L.K., Bridges, A.W., Conboy, E., Hartigan, D. and Rosenberry, T.L. (2007) Amyloid-(1-42) Rapidly Forms Protofibrils and Oligomers by Distinct Pathways in Low Concentrations of Sodium Dodecylsulfate. Biochemistry, 46, 12451-12462.
http://dx.doi.org/10.1021/bi701213s [44] Orczyk, J., Morré, D.M. and Morré, D.J. (2005) Periodic Fluctuations in Oxygen Consumption Comparing HeLa (Cancer) and CHO (Non-Cancer) Cells and Response to External NAD(P)+/NAD(P)H. Molecular and Cellular Biochemistry, 273, 161-167.
http://dx.doi.org/10.1007/s11010-005-0326-2 [45] Berridge, M.V. and Tan, A.S. (2000) High-Capacity Redox Control at the Plasma Membrane of Mammalian Cells: Trans-Membrane, Cell Surface, and Serum NADH-Oxidases. Antioxidants & Redox Signaling, 2, 231-242.
http://dx.doi.org/10.1089/ars.2000.2.2-231 [46] Hyun, D.-H., Hunt, N.D., Emerson, S.S., Hernandez, J.O., Mattson, M.P. and de Cabo, R. (2007) Up-Regulation of Plasma Membrane-Associated Redox Activities in Neuronal Cells Lacking Functional Mitochondria. Journal of Neurochemistry, 100, 1364-1374.
http://dx.doi.org/10.1111/j.1471-4159.2006.04411.x [47] Crane, F.L. and Low, H. (2008) Reactive Oxygen Species Generation at the Plasma Membrane for Antibody Control. Autoimmunity Reviews, 7, 518-522.
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http://dx.doi.org/10.1089/ars.2000.2.2-197