Articles de revues : « Transplasma membrane »

1

Misra, Prakash C. « Transplasma membrane electron transport in plants ». Journal of Bioenergetics and Biomembranes 23, n^o 3 (juin 1991) : 425–41. http://dx.doi.org/10.1007/bf00771013.

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Crane, Frederick L., et Hans Löw. « The Oxidative Function of Diferric Transferrin ». Biochemistry Research International 2012 (2012) : 1–7. http://dx.doi.org/10.1155/2012/592806.

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There is evidence for an unexpected role of diferric transferrin as a terminal oxidase for the transplasma membrane oxidation of cytosolic NADH. In the original studies which showed the reduction of iron in transferrin by the plasma membranes NADH oxidase, the possible role of the reduction on iron uptake was emphasized. The rapid reoxidation of transferrin iron under aerobic conditions precludes a role for surface reduction at neutral pH for release of iron for uptake at the plasma membrane. The stimulation of cytosolic NADH oxidation by diferric transferrin indicates that the transferrin can act as a terminal oxidase for the transplasma membrane NADH oxidase or can bind to a site which activates the oxidase. Since plasma membrane NADH oxidases clearly play a role in cell signaling, the relation of ferric transferrin stimulation of NADH oxidase to cell control should be considered, especially in relation to the growth promotion by transferrin not related to iron uptake. The oxidase can also contribute to control of cytosolic NAD concentration, and thereby can activate sirtuins for control of ageing and growth.

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3

Baoutina, A., R. T. dean et W. Jessup. « Transplasma membrane redox activity of monocytes/macrophages ». Redox Report 5, n^o 2-3 (avril 2000) : 85–86. http://dx.doi.org/10.1179/135100000101535591.

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Revis, Shalini, et Prakash C. Misra. « Transplasma Membrane Electron Transport in Angiospermic Parasites ». Journal of Plant Physiology 122, n^o 4 (mars 1986) : 337–45. http://dx.doi.org/10.1016/s0176-1617(86)80166-3.

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DATTA, GAUTAM, et TANMOY BERA. « Transplasma Membrane Electron Transport in Leishmania donovani Promastigotes ». Journal of Eukaryotic Microbiology 49, n^o 1 (janvier 2002) : 24–29. http://dx.doi.org/10.1111/j.1550-7408.2002.tb00335.x.

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Baker, Mark A., Darius J. R. Lane, Jennifer D. Ly, Vito De Pinto et Alfons Lawen. « VDAC1 Is a Transplasma Membrane NADH-Ferricyanide Reductase ». Journal of Biological Chemistry 279, n^o 6 (22 octobre 2003) : 4811–19. http://dx.doi.org/10.1074/jbc.m311020200.

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Crane, F. L., I. L. Sun, M. G. Clark, C. Grebing et H. Löw. « Transplasma-membrane redox systems in growth and development ». Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics 811, n^o 3 (août 1985) : 233–64. http://dx.doi.org/10.1016/0304-4173(85)90013-8.

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Lane, Darius J. R., et Alfons Lawen. « Transplasma membrane electron transport comes in two flavors ». BioFactors 34, n^o 3 (2008) : 191–200. http://dx.doi.org/10.1002/biof.5520340303.

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Ly, Jennifer D., et Alfons Lawen. « Transplasma membrane electron transport : enzymes involved and biological function ». Redox Report 8, n^o 1 (février 2003) : 3–21. http://dx.doi.org/10.1179/135100003125001198.

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Sun, I. L., E. E. Sun, F. L. Crane et D. J. Morré. « Evidence for coenzyme Q function in transplasma membrane electron transport ». Biochemical and Biophysical Research Communications 172, n^o 3 (novembre 1990) : 979–84. http://dx.doi.org/10.1016/0006-291x(90)91542-z.

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Sun, I. L., F. L. Crane et H. Löw. « Bombesin stimulates transplasma-membrane electron transport by Swiss 3T3 cells ». Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1221, n^o 2 (mars 1994) : 206–10. http://dx.doi.org/10.1016/0167-4889(94)90015-9.

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Stahl, James D., et Steven D. Aust. « Properties of a transplasma membrane redox system of Phanerochaete chrysosporium ». Archives of Biochemistry and Biophysics 320, n^o 2 (juillet 1995) : 369–74. http://dx.doi.org/10.1016/0003-9861(95)90021-7.

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Sun, I. L., E. E. Sun, F. L. Crane, D. J. Morré et W. P. Faulk. « Inhibition of transplasma membrane electron transport by transferrin-adriamycin conjugates ». Biochimica et Biophysica Acta (BBA) - Biomembranes 1105, n^o 1 (mars 1992) : 84–88. http://dx.doi.org/10.1016/0005-2736(92)90165-i.

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Merker, Marilyn P., Lars E. Olson, Robert D. Bongard, Meha K. Patel, John H. Linehan et Christopher A. Dawson. « Ascorbate-mediated transplasma membrane electron transport in pulmonary arterial endothelial cells ». American Journal of Physiology-Lung Cellular and Molecular Physiology 274, n^o 5 (1 mai 1998) : L685—L693. http://dx.doi.org/10.1152/ajplung.1998.274.5.l685.

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Pulmonary endothelial cells are capable of reducing certain electron acceptors at the luminal plasma membrane surface. Motivation for studying this phenomenon comes in part from the expectation that it may be important both as an endothelial antioxidant defense mechanism and in redox cycling of toxic free radicals. Pulmonary arterial endothelial cells in culture reduce the oxidized forms of thiazine compounds that have been used as electron acceptor probes for studying the mechanisms of transplasma membrane electron transport. However, they reduce another commonly studied electron acceptor, ferricyanide, only very slowly by comparison. In the present study, we examined the influence of ascorbate [ascorbic acid (AA)] and dehydroascorbate [dehydroascorbic acid (DHAA)] on the ferricyanide and thiazine reductase activities of the bovine pulmonary arterial endothelial cell surface. The endothelial cells were grown on microcarrier beads so that the reduction of ferricyanide and methylene blue could be studied colorimetrically in spectrophotometer cuvettes and in flow-through cell columns. The ferricyanide reductase activity could be increased 80-fold by adding DHAA to the medium, with virtually no effect on methylene blue reduction. The DHAA effect persisted after the DHAA was removed from the medium. AA also stimulated the ferricyanide reductase activity but was less potent, and the relative potencies of AA and DHAA correlated with their relative rates of uptake by the cells. The results are consistent with the hypothesis that AA is an intracellular electron donor for an endothelial plasma membrane ferricyanide reductase and that the stimulatory effect of DHAA is the result of increasing intracellular AA. Adding sufficient DHAA to markedly increase extracellular ferricyanide reduction had little effect on the plasma membrane methylene blue reductase activity, suggesting that pulmonary arterial endothelial cells have at least two separate transplasma membrane electron transport systems.

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15

L�w, Hans, Frederick L. Crane, Carin Grebing, Monica Isaksson, Annika Lindgren et Iris L. Sun. « Modification of transplasma membrane oxidoreduction by SV40 transformation of 3T3 cells ». Journal of Bioenergetics and Biomembranes 23, n^o 6 (décembre 1991) : 903–17. http://dx.doi.org/10.1007/bf00786008.

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Baoutina, A., R. T. Dean et W. Jessup. « Involvement of transplasma-membrane electron transport in macrophage-mediated LDL oxidation ». Atherosclerosis 151, n^o 1 (juillet 2000) : 262. http://dx.doi.org/10.1016/s0021-9150(00)81188-0.

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17

Yong, Yue, et Jean-Luc Dreyer. « Distribution of six transplasma membrane NADH-dehydrogenases in rat brain tissue ». Developmental Brain Research 89, n^o 2 (novembre 1995) : 235–52. http://dx.doi.org/10.1016/0165-3806(95)00124-v.

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TEPEL, M., S. HEIDENREICH, H. SCHLUTER, A. BEINLICH, J. R. NOFER, M. WALTER, G. ASSMANN et W. ZIDEK. « Diadenosine polyphosphates induce transplasma membrane calcium influx in cultured glomerular mesangial cells ». European Journal of Clinical Investigation 26, n^o 12 (décembre 1996) : 1077–84. http://dx.doi.org/10.1046/j.1365-2362.1996.400592.x.

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Rodríguez-Aguilera, J. C., K. Nakayama, A. Arroyo, J. M. Villalba et P. Navas. « Transplasma membrane redox system of HL-60 cells is controlled by cAMP. » Journal of Biological Chemistry 268, n^o 35 (décembre 1993) : 26346–49. http://dx.doi.org/10.1016/s0021-9258(19)74321-x.

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20

Crane, F. L., R. Barr, T. A. Craig et D. J. Morré. « Transplasma membrane electron transport in relation to cell growth and iron uptake ». Journal of Plant Nutrition 11, n^o 6-11 (juin 1988) : 1117–26. http://dx.doi.org/10.1080/01904168809363872.

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21

Crowe, R. A., E. J. Taparowsky et F. L. Crane. « Ha-ras Stimulates the Transplasma Membrane Oxidoreductase Activity of C3H10T1/2 Cells ». Biochemical and Biophysical Research Communications 196, n^o 2 (octobre 1993) : 844–50. http://dx.doi.org/10.1006/bbrc.1993.2326.

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22

Merker, Marilyn P., Bruce R. Pitt, Augustine M. Choi, Paul M. Hassoun, Christopher A. Dawson et Aron B. Fisher. « Lung redox homeostasis : emerging concepts ». American Journal of Physiology-Lung Cellular and Molecular Physiology 279, n^o 3 (1 septembre 2000) : L413—L417. http://dx.doi.org/10.1152/ajplung.2000.279.3.l413.

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This symposium was organized to present some aspects of current research pertaining to lung redox function. Focuses of the symposium were on roles of pulmonary endothelial NADPH oxidase, xanthine oxidase (XO)/xanthine dehydrogenase (XDH), heme oxygenase (HO), transplasma membrane electron transport (TPMET), and the zinc binding protein metallothionein (MT) in the propagation and/or protection of the lung or other organs from oxidative injury. The presentations were chosen to reflect the roles of both intracellular (metallothionein, XO/XDH, and HO) and plasma membrane (NADPH oxidase, XO/XDH, and unidentified TPMET) redox proteins in these processes. Although the lung endothelium was the predominant cell type under consideration, at least some of the proposed mechanisms operate in or affect other cell types and organs as well.

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23

Merker, Marilyn P., Robert D. Bongard, Nicholas J. Kettenhofen, Yoshiyuki Okamoto et Christopher A. Dawson. « Intracellular redox status affects transplasma membrane electron transport in pulmonary arterial endothelial cells ». American Journal of Physiology-Lung Cellular and Molecular Physiology 282, n^o 1 (1 janvier 2002) : L36—L43. http://dx.doi.org/10.1152/ajplung.00283.2001.

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Pulmonary arterial endothelial cells possess transplasma membrane electron transport (TPMET) systems that transfer intracellular reducing equivalents to extracellular electron acceptors. As one aspect of determining cellular mechanisms involved in one such TPMET system in pulmonary arterial endothelial cells in culture, glycolysis was inhibited by treatment with iodoacetate (IOA) or by replacing the glucose in the cell medium with 2-deoxy-d-glucose (2-DG). TPMET activity was measured as the rate of reduction of the extracellular electron acceptor polymer toluidine blue O polyacrylamide. Intracellular concentrations of NADH, NAD+, NADPH, and NADP+ were determined by high-performance liquid chromatography of KOH cell extracts. IOA decreased TPMET activity to 47% of control activity concomitant with a decrease in the NADH/NAD+ ratio to 34% of the control level, without a significant change in the NADPH/NADP+ ratio. 2-DG decreased TPMET activity to 53% of control and decreased both NADH/NAD+ and NADPH/NADP+ ratios to 51% and 55%, respectively, of control levels. When lactate was included in the medium along with the inhibitors, the effects of IOA and 2-DG on both TPMET activity and the NADPH/NADP+ ratios were prevented. The results suggest that cellular redox status is a determinant of pulmonary arterial endothelial cell TPMET activity, with TPMET activity more highly correlated with the poise of the NADH/NAD+redox pair.

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24

Toole-Simms, W., I. L. Sun, W. P. Faulk, H. Löw, A. Lindgren, F. L. Crane et D. J. Morré. « Inhibition of transplasma membrane electron transport by monoclonal antibodies to the transferrin receptor ». Biochemical and Biophysical Research Communications 176, n^o 3 (mai 1991) : 1437–42. http://dx.doi.org/10.1016/0006-291x(91)90447-f.

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Sun, Iris L., et Frederick L. Cran. « Bleomycin control of transplasma membrane redox activity and proton movement in HeLa cells ». Biochemical Pharmacology 34, n^o 5 (mars 1985) : 617–22. http://dx.doi.org/10.1016/0006-2952(85)90254-0.

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Buron, M. I., J. C. Rodriguezaguilera, F. J. Alcain et P. Navas. « Transplasma Membrane Redox System in HL-60 Cells Is Modulated during TPA-Induced Differentiation ». Biochemical and Biophysical Research Communications 192, n^o 2 (avril 1993) : 439–45. http://dx.doi.org/10.1006/bbrc.1993.1434.

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Qi, Weihong, et Jody Jellison. « Characterization of a transplasma membrane redox system of the brown rot fungus Gloeophyllum trabeum ». International Biodeterioration & ; Biodegradation 53, n^o 1 (janvier 2004) : 37–42. http://dx.doi.org/10.1016/j.ibiod.2003.09.002.

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Medina, Miguel Angel, Pilar Luque et Ignacio NÚñez De Castro. « Mitoxantrone toxicity on ehrlich ascites tumour cells : Inhibition of the transplasma membrane redox activity ». Cell Biochemistry and Function 9, n^o 2 (avril 1991) : 95–98. http://dx.doi.org/10.1002/cbf.290090205.

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Bera, Tanmoy, Kuruba Lakshman, Debiprasad Ghanteswari, Sabita Pal, Dharmalingam Sudhahar, Md Nurul Islam, Nihar Ranjan Bhuyan et Pradeep Das. « Characterization of the redox components of transplasma membrane electron transport system from Leishmania donovani promastigotes ». Biochimica et Biophysica Acta (BBA) - General Subjects 1725, n^o 3 (octobre 2005) : 314–26. http://dx.doi.org/10.1016/j.bbagen.2005.05.024.

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Löw, Hans, Carin Grebing, Annika Lindgren, Michael Tally, Iris L. Sun et Frederick L. Crane. « Involvement of transferrin in the reduction of iron by the transplasma membrane electron transport system ». Journal of Bioenergetics and Biomembranes 19, n^o 5 (octobre 1987) : 535–49. http://dx.doi.org/10.1007/bf00770036.

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Yong, Yue, et Jean-Luc Dreyer. « Developmental changes in the localization of the transplasma membrane NADH-dehydrogenases in the rat brain ». Developmental Brain Research 89, n^o 2 (novembre 1995) : 253–63. http://dx.doi.org/10.1016/0165-3806(95)00125-w.

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Ayling, SM, et DT Clarkson. « The Cytoplasmic Streaming Response of Tomato Root Hairs to Auxin ; the Role of Calcium ». Functional Plant Biology 23, n^o 6 (1996) : 699. http://dx.doi.org/10.1071/pp9960699.

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The effects of IAA on the cytoplasmic streaming response of tomato root hairs were observed at different external calcium concentrations. The sensitivity of tomato root hairs to IAA was increased by increasing the calcium content of the bathing medium; lower concentrations of IAA were needed to stimulate cytoplasmic streaming at high [Ca2+]ext. The transplasma membrane electrical potential difference was rapidly depolarised by IAA across a wide range of auxin and calcium concentrations; subsequent hyperpolarisation was only seen in the presence of high [Ca2+]ext. Measurements of cytoplasmic calcium levels, using the dye fluo-3, revealed the dynamic nature of the cytoplasm. As in earlier experiments, in which indo-1 and fura-2 were used, IAA appeared to have only small effects on [Ca2+]cyt. Clear, auxin-induced changes in [Ca2+]cyt were recorded only under non-physiological conditions.

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Revis, Shalini, et Prakash C. Misra. « Changes in intracellular redox and energy status during induced transplasma membrane electron transport in Cuscuta protoplasts ». Biochemical and Biophysical Research Communications 156, n^o 2 (octobre 1988) : 940–46. http://dx.doi.org/10.1016/s0006-291x(88)80934-3.

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Seidenberg, S., O. D�ring, S. Kr�ger, S. L�thje et M. B�ttger. « Changes in the glutathione level induced by transplasma membrane electron transport in maize (Zea mays L.) ». Protoplasma 184, n^o 1-4 (mars 1995) : 238–48. http://dx.doi.org/10.1007/bf01276927.

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Morr�, D. James, Dorothy M. Morr� et Lian-Ying Wu. « Response to adriamycin of transplasma membrane electron transport in adriamycin-resistant and nonresistant HL-60 cells ». Journal of Bioenergetics and Biomembranes 26, n^o 1 (février 1994) : 137–42. http://dx.doi.org/10.1007/bf00763225.

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Debnath, Dipti, Md Akil Hossain, Munny Das, Asma Kabir, Md Ibrahim, Mohammad Nurul Amin, Amrita Chowdhury et Rokeya Pervin. « Characterization of Transplasma Membrane Electron Transport Chain in Wild and Drug-Resistant Leishmania donovani Promastigote and Amastigote ». Acta Parasitologica 64, n^o 4 (2 avril 2019) : 710–19. http://dx.doi.org/10.2478/s11686-019-00050-y.

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Blein, J. P., M. C. Canivenc, X. De Cherade, M. Bergon, J. P. Calmon et R. Scalla. « Transplasma-membrane ferricyanide reduction in sycamore cells. Characterization of the system and inhibition by some phenyl biscarbamates ». Plant Science 46, n^o 2 (janvier 1986) : 77–85. http://dx.doi.org/10.1016/0168-9452(86)90113-5.

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Barbar, Élie, Marek Rola-Pleszczynski, Marcel D. Payet et Gilles Dupuis. « Protein kinase C inhibits the transplasma membrane influx of Ca2+ triggered by 4-aminopyridine in Jurkat T lymphocytes ». Biochimica et Biophysica Acta (BBA) - General Subjects 1622, n^o 2 (juillet 2003) : 89–98. http://dx.doi.org/10.1016/s0304-4165(03)00120-x.

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Datta, Gautam, et Tanmoy Bera. « Evidence for the extracellular reduction of α-lipoic acid by Leishmania donovani promastigotes : a transplasma membrane redox system ». Biochimica et Biophysica Acta (BBA) - Biomembranes 1512, n^o 2 (juin 2001) : 149–57. http://dx.doi.org/10.1016/s0005-2736(01)00306-6.

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Lane, Darius J. R., Stephen R. Robinson, Hania Czerwinska et Alfons Lawen. « A role for Na+/H+ exchangers and intracellular pH in regulating vitamin C-driven electron transport across the plasma membrane ». Biochemical Journal 428, n^o 2 (13 mai 2010) : 191–200. http://dx.doi.org/10.1042/bj20100064.

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Ascorbate (vitamin C) is the major electron donor to a tPMET (transplasma membrane electron transport) system that was originally identified in human erythrocytes. This plasma membrane redox system appears to transfer electrons from intracellular ascorbate to extracellular oxidants (e.g. non-transferrin-bound iron). Although this phenomenon has been observed in nucleated cells, its mechanism and regulation are not well understood. In the present study we have examined both facets of this phenomenon in K562 cells and primary astrocyte cultures. Using ferricyanide as the analytical oxidant we demonstrate that tPMET is enhanced by dehydroascorbate uptake via facilitative glucose transporters, and subsequent accumulation of intracellular ascorbate. Additionally, we demonstrate that this stimulation is not due to ascorbate that is released from the cells, but is dependent only on a restricted intracellular pool of the vitamin. Substrate-saturation kinetics suggest an enzyme-catalysed reaction across the plasma membrane by an as-yet-unidentified reductase that relies on extensive recycling of intracellular ascorbate. Inhibition of ascorbate-stimulated tPMET by the NHE (Na+/H+-exchanger) inhibitors amiloride and 5-(N-ethyl-N-isopropyl)amiloride, which is diminished by bicarbonate, suggests that tPMET activity may be regulated by intracellular pH. In support of this hypothesis, tPMET in astrocytes was significantly inhibited by ammonium chloride-pulse-induced intracellular acidification, whereas it was significantly stimulated by bicarbonate-induced intracellular alkalinization. These results suggest that ascorbate-dependent tPMET is enzyme-catalysed and is modulated by NHE activity and intracellular pH.

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Lane, Darius J. R., et Alfons Lawen. « A highly sensitive colorimetric microplate ferrocyanide assay applied to ascorbate-stimulated transplasma membrane ferricyanide reduction and mitochondrial succinate oxidation ». Analytical Biochemistry 373, n^o 2 (février 2008) : 287–95. http://dx.doi.org/10.1016/j.ab.2007.09.009.

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Stuart, Jeffrey A., Joao Fonseca, Fereshteh Moradi, Cassandra Cunningham, Bishoy Seliman, Cydney R. Worsfold, Sarah Dolan, John Abando et Lucas A. Maddalena. « How Supraphysiological Oxygen Levels in Standard Cell Culture Affect Oxygen-Consuming Reactions ». Oxidative Medicine and Cellular Longevity 2018 (30 septembre 2018) : 1–13. http://dx.doi.org/10.1155/2018/8238459.

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Most mammalian tissue cells experience oxygen partial pressuresin vivoequivalent to 1–6% O2(i.e., physioxia). In standard cell culture, however, headspace O2levels are usually not actively regulated and under these conditions are ~18%. This drives hyperoxia in cell culture media that can affect a wide variety of cellular activities and may compromise the ability ofin vitromodels to reproducein vivobiology. Here, we review and discuss some specific O2-consuming organelles and enzymes, including mitochondria, NADPH oxidases, the transplasma membrane redox system, nitric oxide synthases, xanthine oxidase, and monoamine oxidase with respect to their sensitivities to O2levels. Many of these produce reactive oxygen and/or nitrogen species (ROS/RNS) as either primary end products or byproducts and are acutely sensitive to O2levels in the range from 1% to 18%. Interestingly, many of them are also transcriptional targets of hypoxia-inducible factors (HIFs) and chronic cell growth at physioxia versus 18% O2may alter their expression. Aquaporins, which facilitate hydrogen peroxide diffusion into and out of cells, are also regulated by HIFs, indicating that O2levels may affect intercellular communication via hydrogen peroxide. The O2sensitivities of these important activities emphasize the importance of maintaining physioxia in culture.

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Audi, Said H., Robert D. Bongard, Yoshiyuki Okamoto, Marilyn P. Merker, David L. Roerig et Christopher A. Dawson. « Pulmonary reduction of an intravascular redox polymer ». American Journal of Physiology-Lung Cellular and Molecular Physiology 280, n^o 6 (1 juin 2001) : L1290—L1299. http://dx.doi.org/10.1152/ajplung.2001.280.6.l1290.

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Pulmonary endothelial cells in culture reduce external electron acceptors via transplasma membrane electron transport (TPMET). In studying endothelial TPMET in intact lungs, it is difficult to exclude intracellular reduction and reducing agents released by the lung. Therefore, we evaluated the role of endothelial TPMET in the reduction of a cell-impermeant redox polymer, toluidine blue O polyacrylamide (TBOP+), in intact rat lungs. When added to the perfusate recirculating through the lungs, the venous effluent TBOP+concentration decreased to an equilibrium level reflecting TBOP+ reduction and autooxidation of its reduced (TBOPH) form. Adding superoxide dismutase (SOD) to the perfusate increased the equilibrium TBOP+ concentration. Kinetic analysis indicated that the SOD effect could be attributed to elimination of the superoxide product of TBOPH autooxidation rather than of superoxide released by the lungs, and experiments with lung-conditioned perfusate excluded release of other TBOP+ reductants in sufficient quantities to cause significant TBOP+ reduction. Thus the results indicate that TBOP+ reduction is via TPMET and support the utility of TBOP+ and the kinetic model for investigating TPMET mechanisms and their adaptations to physiological and pathophysiological stresses in the intact lung.

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Biswas, Shibendu, Rabiul Haque, Nihar R. Bhuyan et Tanmoy Bera. « Participation of chlorobiumquinone in the transplasma membrane electron transport system of Leishmania donovani promastigote : Effect of near-ultraviolet light on the redox reaction of plasma membrane ». Biochimica et Biophysica Acta (BBA) - General Subjects 1780, n^o 2 (février 2008) : 116–27. http://dx.doi.org/10.1016/j.bbagen.2007.09.006.

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Baroja-Mazo, Alberto, Pilar Del Valle, Javier Rúa, Félix Busto, Sergio De Cima et Dolores De Arriaga. « A Transplasma Membrane Redox System in Phycomyces blakesleeanus : Properties of a Ferricyanide Reductase Activity Regulated by Iron Level and Vitamin K3 ». Journal of Bioenergetics and Biomembranes 36, n^o 5 (octobre 2004) : 481–92. http://dx.doi.org/10.1023/b:jobb.0000047330.65632.5d.

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Bera, Tanmoy, Nilay Nandi, D. Sudhahar, Md Ali Akbar, Abhik Sen et Pradeep Das. « Preliminary evidence on existence of transplasma membrane electron transport in Entamoeba histolytica trophozoites : a key mechanism for maintaining optimal redox balance ». Journal of Bioenergetics and Biomembranes 38, n^o 5-6 (13 octobre 2006) : 299–308. http://dx.doi.org/10.1007/s10863-006-9047-9.

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Nandi, Nilay, Tanmoy Bera, Sudeep Kumar, Bidyut Purkait, Ashish Kumar et Pradeep Das. « Involvement of thermoplasmaquinone-7 in transplasma membrane electron transport of Entamoeba histolytica trophozoites : a key molecule for future rational chemotherapeutic drug designing ». Journal of Bioenergetics and Biomembranes 43, n^o 2 (avril 2011) : 203–15. http://dx.doi.org/10.1007/s10863-011-9347-6.

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Oliveira, Ma Benigna M., Annibal P. Campello et Ma Lúcia W. Klüppel. « Methotrexate : Studies on cellular metabolism. III.-Effect on the transplasma-membrane redox activity and on ferricyanide-induced proton extrusion by HeLa cells ». Cell Biochemistry and Function 7, n^o 2 (avril 1989) : 135–37. http://dx.doi.org/10.1002/cbf.290070209.

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Crowe, Ruth A., et F. L. Crane. « Effect of growth factors and antitumor drugs on normal and Vall2Ha-ras transformed C3H 10T1/2 cell transplasma membrane electron transport and growth ». Protoplasma 184, n^o 1-4 (mars 1995) : 209–13. http://dx.doi.org/10.1007/bf01276922.

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Diaz, Julia M., Sydney Plummer, Colleen M. Hansel, Peter F. Andeer, Mak A. Saito et Matthew R. McIlvin. « NADPH-dependent extracellular superoxide production is vital to photophysiology in the marine diatom Thalassiosira oceanica ». Proceedings of the National Academy of Sciences 116, n^o 33 (25 juillet 2019) : 16448–53. http://dx.doi.org/10.1073/pnas.1821233116.

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Reactive oxygen species (ROS) like superoxide drive rapid transformations of carbon and metals in aquatic systems and play dynamic roles in biological health, signaling, and defense across a diversity of cell types. In phytoplankton, however, the ecophysiological role(s) of extracellular superoxide production has remained elusive. Here, the mechanism and function of extracellular superoxide production by the marine diatom Thalassiosira oceanica are described. Extracellular superoxide production in T. oceanica exudates was coupled to the oxidation of NADPH. A putative NADPH-oxidizing flavoenzyme with predicted transmembrane domains and high sequence similarity to glutathione reductase (GR) was implicated in this process. GR was also linked to extracellular superoxide production by whole cells via quenching by the flavoenzyme inhibitor diphenylene iodonium (DPI) and oxidized glutathione, the preferred electron acceptor of GR. Extracellular superoxide production followed a typical photosynthesis-irradiance curve and increased by 30% above the saturation irradiance of photosynthesis, while DPI significantly impaired the efficiency of photosystem II under a wide range of light levels. Together, these results suggest that extracellular superoxide production is a byproduct of a transplasma membrane electron transport system that serves to balance the cellular redox state through the recycling of photosynthetic NADPH. This photoprotective function may be widespread, consistent with the presence of putative homologs to T. oceanica GR in other representative marine phytoplankton and ocean metagenomes. Given predicted climate-driven shifts in global surface ocean light regimes and phytoplankton community-level photoacclimation, these results provide implications for future ocean redox balance, ecological functioning, and coupled biogeochemical transformations of carbon and metals.

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