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Glycolytic oligodendrocytes maintain myelin and long-term axonal integrity
Open accessAbstract
Oligodendrocytes, the myelin-forming glial cells of the central nervous system, maintain long-term axonal integrity. However, the underlying support mechanisms are not understood. Here we identify a metabolic component of axon-glia interactions by generating conditional Cox10 (protoheme IX farnesyltransferase) mutant mice, in which oligodendrocytes and Schwann cells fail to assemble stable mitochondrial cytochrome c oxidase (COX, also known as mitochondrial complex IV). In the peripheral nervous system, Cox10 conditional mutants exhibit severe neuropathy with dysmyelination, abnormal Remak bundles, muscle atrophy and paralysis. Notably, perturbing mitochondrial respiration did not cause glial cell death. In the adult central nervous system, we found no signs of demyelination, axonal degeneration or secondary inflammation. Unlike cultured oligodendrocytes, which are sensitive to COX inhibitors, post-myelination oligodendrocytes survive well in the absence of COX activity. More importantly, by in vivo magnetic resonance spectroscopy, brain lactate concentrations in mutants were increased compared with controls, but were detectable only in mice exposed to volatile anaesthetics. This indicates that aerobic glycolysis products derived from oligodendrocytes are rapidly metabolized within white matter tracts. Because myelinated axons can use lactate when energy-deprived, our findings suggest a model in which axon-glia metabolic coupling serves a physiological function.
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“However, there is so far no experimental approach to the question of whether oligodendrocytes release lactate or pyruvate (Fünfschilling et al., 2012) for the support of axonal energy metabolism.”
From Downregulated expression of lactate dehydrogenase in adult oligodendrocytes and its implication for the transfer of glycolysis products to axons (2024) · cites this paper as Fünfschilling et al., 2012
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“Remyelination is a crucial regenerative process in demyelinating diseases, limiting persisting damage to the CNS. It restores saltatory nerve conduction and ensures trophic support of axons.”
From BCAS1-positive oligodendrocytes enable efficient cortical remyelination in multiple sclerosis (2025) · cites this paper as [3]
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In the citing paper
“Oligodendrocytes with impaired oxidative phosphorylation instead boost aerobic glycolysis, as indicated by increased lactate levels [127].”
From Oligodendrocyte death and myelin loss in the cuprizone model: an updated overview of the intrinsic and extrinsic causes of cuprizone demyelination (2022) · cites this paper as [127]
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“This shift of normal myelin turnover to lipid-based ATP generation allows OLs to share more glucose-derived pyruvate/lactate with the axons to support ATP generation and prevent axon degeneration [278,280].”
From Revisiting the Pathogenesis of X-Linked Adrenoleukodystrophy (2025) · cites this paper as [280]
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“This led to a working model of glycolytic oligodendrocytes providing direct metabolic support to axons via non-compacted cytoplasmic channels in myelin and monocarboxylate transporters, which preserves functional integrity and axon survival (Amaral et al., 2013;Fünfschilling et al., 2012;Lee et al., 2012).”
From Downregulated expression of lactate dehydrogenase in adult oligodendrocytes and its implication for the transfer of glycolysis products to axons (2024) · cites this paper as Fünfschilling et al., 2012
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“This is compatible with the idea that adult oligodendrocytes become predominantly glycolytic with a reduced rate of oxidative phosphorylation (OXPHOS) (Fünfschilling et al., 2012).”
From Downregulated expression of lactate dehydrogenase in adult oligodendrocytes and its implication for the transfer of glycolysis products to axons (2024) · cites this paper as Fünfschilling et al., 2012
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“Our data are thus compatible with a revised working model of Fünfschilling et al. (2012), in which lactate is preferentially produced in astrocytes close to their gap junctions with neighboring cells, and in which myelinic channels funnel astroglial lactate and oligodendroglial pyruvate to the periaxonal space of myelinated internodes.”
From Downregulated expression of lactate dehydrogenase in adult oligodendrocytes and its implication for the transfer of glycolysis products to axons (2024) · cites this paper as Fünfschilling et al., 2012
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“As oligodendrocytes support axonal energy metabolism and neuronal health4–7, we hypothesized that loss of myelin integrity could be an upstream risk factor for neuronal amyloid-β (Aβ) deposition, the central neuropathological hallmark of AD.”
From Myelin dysfunction drives amyloid-β deposition in models of Alzheimer’s disease (2023) · cites this paper as [5]
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“Oligodendrocyte-specific deletion of Cox10, which encodes a crucial component for cyt c oxidase assembly and is necessary for oxidative phosphorylation, failed to cause demyelination or neurodegeneration even at 14-months of age.”
From Oligodendrocyte death and myelin loss in the cuprizone model: an updated overview of the intrinsic and extrinsic causes of cuprizone demyelination (2022) · cites this paper as [127]
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“For example, impaired mitochondrial metabolism alone does not induce oligodendrocyte death in vivo [127].”
From Oligodendrocyte death and myelin loss in the cuprizone model: an updated overview of the intrinsic and extrinsic causes of cuprizone demyelination (2022) · cites this paper as [127]
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“we found that mature oligodendrocytes survive well in Cox10 (protoheme IX farnesyltransferase)-deficient mice, in which oligodendrocytes lack an assembly factor of stable mitochondrial cytochrome c oxidase (COX, mitochondrial complex IV).”
From Downregulated expression of lactate dehydrogenase in adult oligodendrocytes and its implication for the transfer of glycolysis products to axons (2024) · cites this paper as Fünfschilling et al., 2012
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“This opens the possibility that glycolytic oligodendrocytes, which are suggested to support electrically active axons with an excess of glycolysis products (Fünfschilling et al., 2012;Lee et al., 2012;Saab et al., 2016;Trevisiol et al., 2017) do so primarily by self-made pyruvate.”
From Downregulated expression of lactate dehydrogenase in adult oligodendrocytes and its implication for the transfer of glycolysis products to axons (2024) · cites this paper as Fünfschilling et al., 2012
In the citing paper
“This confirms that axons readily use lactate for ATP generation”
From Oligodendroglial NMDA receptors regulate glucose import and axonal energy metabolism (2016) · cites this paper as Fünfschilling et al., 2012
In the citing paper
“Myelin modulates the speed of neural impulse conduction (Smith and Koles, 1970; Waxman, 1980), provides metabolic support to axons (Fünfschilling et al., 2012), and exhibits adaptive plasticity (Gibson et al., 2014);”
From Mild respiratory COVID can cause multi-lineage neural cell and myelin dysregulation (2022) · cites this paper as Fünfschilling et al., 2012
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Citations
Cites
Estimation of metabolite concentrations from localized in vivo proton NMR spectra
Provencher, S. W. (1993) · Magnetic Resonance in Medicine · doi:10.1002/mrm.1910300604 · Cited by 3,659
Pellerin, L., & Magistretti, P. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10625 · Cited by 2,927
Astrocyte-Neuron Lactate Transport Is Required for Long-Term Memory Formation
Suzuki, A., Stern, S. A., Bozdagi, O., Huntley, G. W., Walker, R. H., Magistretti, P. J., & Alberini, C. M. (2011) · Cell · doi:10.1016/j.cell.2011.02.018 · Cited by 1,711
Disruption of Cnp1 uncouples oligodendroglial functions in axonal support and myelination
Lappe-Siefke, C., Goebbels, S., Gravel, M., Nicksch, E., Lee, J., Braun, P. E., Griffiths, I. R., & Nave, K.-A. (2003) · Nature Genetics · doi:10.1038/ng1095 · Cited by 1,036
Self-citationAxonal Swellings and Degeneration in Mice Lacking the Major Proteolipid of Myelin
Griffiths, I., Klugmann, M., Anderson, T., Yool, D., Thomson, C., Schwab, M. H., Schneider, A., Zimmermann, F., McCulloch, M., Nadon, N., et al. (1998) · Science · doi:10.1126/science.280.5369.1610 · Cited by 889
Self-citationEssential Role for TrkB Receptors in Hippocampus-Mediated Learning
Minichiello, L., Korte, M., Wolfer, D., Kühn, R., Unsicker, K., Cestari, V., Rossi-Arnaud, C., Lipp, H.-P., Bonhoeffer, T., & Klein, R. (1999) · Neuron · doi:10.1016/s0896-6273(00)80853-3 · Cited by 799
Myelination and the trophic support of long axons
Nave, K.-A. (2010) · Nature Reviews Neuroscience · doi:10.1038/nrn2797 · Cited by 648
Self-citationRegulation of Oligodendrocyte Development and Myelination by Glucose and Lactate
Rinholm, J. E., Hamilton, N. B., Kessaris, N., Richardson, W. D., Bergersen, L. H., & Attwell, D. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3516-10.2011 · Cited by 383
Mitochondrial potassium transport: the K+ cycle
Garlid, K. D., & Paucek, P. (2003) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(03)00108-7 · Cited by 365
Axonal loss and neuroinflammation caused by peroxisome-deficient oligodendrocytes
Kassmann, C. M., Lappe-Siefke, C., Baes, M., Brügger, B., Mildner, A., Werner, H. B., Natt, O., Michaelis, T., Prinz, M., Frahm, J., et al. (2007) · Nature Genetics · doi:10.1038/ng2070 · Cited by 357
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Kang, Z., Wang, C., Zepp, J., Wu, L., Sun, K., Zhao, J., Chandrasekharan, U., DiCorleto, P. E., Trapp, B. D., Ransohoff, R. M., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3505 · Cited by 218
The Drosophila blood-brain barrier: development and function of a glial endothelium
Limmer, S., Weiler, A., Volkenhoff, A., Babatz, F., & Klämbt, C. (2014) · Frontiers in Neuroscience · doi:10.3389/fnins.2014.00365 · Cited by 214
Spaas, J., van Veggel, L., Schepers, M., Tiane, A., van Horssen, J., Wilson, D. M., Moya, P. R., Piccart, E., Hellings, N., Eijnde, B. O., et al. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03802-0 · Cited by 224
Keough, M. B., Rogers, J. A., Zhang, P., Jensen, S. K., Stephenson, E. L., Chen, T., Hurlbert, M. G., Lau, L. W., Rawji, K. S., Plemel, J. R., et al. (2016) · Nature Communications · doi:10.1038/ncomms11312 · Cited by 217
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Snaidero, N., Velte, C., Myllykoski, M., Raasakka, A., Ignatev, A., Werner, H. B., Erwig, M. S., Möbius, W., Kursula, P., Nave, K., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2016.12.053 · Cited by 227
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Beirowski, B., Babetto, E., Golden, J. P., Chen, Y., Yang, K., Gross, R. W., Patti, G. J., & Milbrandt, J. (2014) · Nature Neuroscience · doi:10.1038/nn.3809 · Cited by 210
The multifaceted role of astrocytes in regulating myelination
Kıray, H., Lindsay, S. L., Hosseinzadeh, S., & Barnett, S. C. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2016.03.009 · Cited by 212
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Nemes-Baran, A. D., White, D. R., & DeSilva, T. M. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108047 · Cited by 196
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Frühbeis, C., Kuo, W. P., Müller, C., Barth, K., Peris, L., Tenzer, S., Möbius, W., Werner, H. B., Nave, K., Fröhlich, D., et al. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3000621 · Cited by 201
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Huang, B., Wei, W., Wang, G., Gaertig, M. A., Feng, Y., Wang, W., Li, X., & Li, S. (2015) · Neuron · doi:10.1016/j.neuron.2015.02.026 · Cited by 179
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Chamberlain, K. A., Huang, N., Xie, Y., Licausi, F., Li, S., Li, Y., & Sheng, Z. (2021) · Neuron · doi:10.1016/j.neuron.2021.08.011 · Cited by 184
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Yang, D., Wang, X., Zhang, L., Fang, Y., Zheng, Q., Liu, X., Yu, W., Chen, S., Ying, J., & Hua, F. (2022) · Cell & Bioscience · doi:10.1186/s13578-022-00828-0 · Cited by 179
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Dimas, P., Montani, L., Pereira, J. A., Moreno, D., Trötzmüller, M., Gerber, J., Semenkovich, C. F., Köfeler, H. C., & Suter, U. (2019) · eLife · doi:10.7554/elife.44702 · Cited by 178
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BackgroundKoudelka, S., Voas, M. G., Almeida, R., Baraban, M., Soetaert, J., Meyer, M. P., Talbot, W. S., & Lyons, D. A. (2016) · Current Biology · doi:10.1016/j.cub.2016.03.070 · Cited by 170
Gundersen, V., Storm‐Mathisen, J., & Bergersen, L. H. (2015) · Physiological Reviews · doi:10.1152/physrev.00024.2014 · Cited by 179
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Correale, J., Marrodan, M., & Ysrraelit, M. C. (2019) · Biomedicines · doi:10.3390/biomedicines7010014 · Cited by 167
Goodwin, J., Choi, H., Hsieh, M.-H., Neugent, M. L., Ahn, J., Hayenga, H. N., Singh, P. K., Shackelford, D. B., Lee, I., Shulaev, V., et al. (2017) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2016-0186oc · Cited by 174
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Bogie, J. F. J., Haidar, M., Kooij, G., & Hendriks, J. J. A. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.01.004 · Cited by 167
Stedehouder, J., Couey, J. J., Brizee, D., Hosseini, B., Slotman, J. A., Dirven, C. M. F., Shpak, G., Houtsmuller, A. B., & Kushner, S. A. (2017) · Cerebral Cortex · doi:10.1093/cercor/bhx203 · Cited by 166
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Wolf, N. I., ffrench‐Constant, C., & van der Knaap, M. S. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-00432-1 · Cited by 173
Anandhan, A., Jacome, M. S., Lei, S., Hernández-Franco, P., Pappa, A., Panayiotidis, M. I., Powers, R., & Franco, R. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.03.009 · Cited by 165
Dutta, R., Chomyk, A. M., Chang, A., Ribaudo, M. V., Deckard, S. A., Doud, M. K., Edberg, D. D., Bai, B., Li, M., Baranzini, S. E., et al. (2013) · Annals of Neurology · doi:10.1002/ana.23860 · Cited by 155
Haddad, D., & Nakamura, K. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.10.021 · Cited by 167
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Pathak, D., Berthet, A., & Nakamura, K. (2013) · Annals of Neurology · doi:10.1002/ana.24014 · Cited by 162
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Barros, L. F., & Weber, B. (2018) · The Journal of Physiology · doi:10.1113/jp274944 · Cited by 154
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Campbell, G. R., Worrall, J. T., & Mahad, D. (2014) · Multiple Sclerosis · doi:10.1177/1352458514544537 · Cited by 137
Self-citationQian, Y., Yuan, W., Cheng, Y. G., Yang, Y., Qu, X., & Fan, C. (2019) · Nano Letters · doi:10.1021/acs.nanolett.9b03980 · Cited by 146
Inak, G., Rybak‐Wolf, A., Lisowski, P., Pentimalli, T. M., Jüttner, R., Glažar, P., Uppal, K., Bottani, E., Brunetti, D., Secker, C., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22117-z · Cited by 151
Bonora, M., Marchi, E. D., Patergnani, S., Suski, J. M., Celsi, F., Bononi, A., Giorgi, C., Marchi, S., Rimessi, A., Duszyński, J., et al. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.35 · Cited by 147
Diverse cellular and molecular modes of axon degeneration
Neukomm, L. J., & Freeman, M. R. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.04.003 · Cited by 144
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Duncan, I. D., & Radcliff, A. B. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2016.04.002 · Cited by 146
Goyal, M. S., Venkatesh, S., Milbrandt, J., Gordon, J. I., & Raichle, M. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1511465112 · Cited by 141
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Micu, I., Plemel, J. R., Lachance, C., Proft, J., Jansen, A. J., Cummins, K., van Minnen, J., & Stys, P. K. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2015.10.006 · Cited by 140
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Kane, D. A. (2014) · Frontiers in Neuroscience · doi:10.3389/fnins.2014.00366 · Cited by 142
Yao, S., Xu, M.-D., Wang, Y., Zhao, S., Wang, J., Chen, G.-F., Chen, W., Liu, J., Huang, G., Sun, W.-J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36209-5 · Cited by 144
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Self-citationRegulation of myelination by microglia
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Rone, M. B., Cui, Q., Fang, J. Q., Wang, L., Zhang, J., Khan, D., Bedard, M., Almazán, G., Ludwin, S. K., Jones, R., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.4077-15.2016 · Cited by 136
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Cai, Z., & Xiao, M. (2015) · International Journal of Neuroscience · doi:10.3109/00207454.2015.1025778 · Cited by 140
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Freeman, S. A., Desmazières, A., Fricker, D., Lubetzki, C., & Sol‐Foulon, N. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2081-1 · Cited by 149
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Miljković, D. M., & Spasojević, I. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5068 · Cited by 143
Joutel, A., & Chabriat, H. (2017) · Clinical Science · doi:10.1042/cs20160380 · Cited by 141
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Knowles, J. K., Xu, H., Soane, C., Batra, A., Saucedo, T., Frost, E., Tam, L. T., Fraga, D. A., Ni, L., Villar, K., et al. (2022) · Nature Neuroscience · doi:10.1038/s41593-022-01052-2 · Cited by 130
Philips, T., Mironova, Y. A., Jouroukhin, Y., Chew, J., Vidensky, S., Farah, M. H., Pletnikov, M. V., Bergles, D. E., Morrison, B. M., & Rothstein, J. D. (2021) · Cell Reports · doi:10.1016/j.celrep.2020.108610 · Cited by 126
Newton, S. E. B., Lloreda, C. L., Gannon, P. J., Akay, C., & Jordan‐Sciutto, K. L. (2020) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlz129 · Cited by 139
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Cooper, M., Pasini, S., Lambert, W. S., D’Alessandro, K. B., Yao, V., Risner, M. L., & Calkins, D. J. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009425117 · Cited by 132
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Correale, J. D. (2014) · Multiple Sclerosis Journal · doi:10.1177/1352458514533230 · Cited by 133
Griemsmann, S., Höft, S. P., Bedner, P., Zhang, J., von Staden, E., Beinhauer, A., Degen, J., Dublin, P., Cope, D. W., Richter, N., et al. (2015) · Cerebral Cortex · doi:10.1093/cercor/bhu157 · Cited by 132
Oligodendroglial fatty acid metabolism as a central nervous system energy reserve
Asadollahi, E., Trevisiol, A., Saab, A. S., Looser, Z. J., Dibaj, P., Ebrahimi, R., Kusch, K., Ruhwedel, T., Möbius, W., Jahn, O., et al. (2024) · Nature Neuroscience · doi:10.1038/s41593-024-01749-6 · Cited by 130
Self-citationRetinal energy metabolism in health and glaucoma
Casson, R. J., Chidlow, G., Crowston, J. G., Williams, P. A., & Wood, J. P. M. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100881 · Cited by 132
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Moore, S., Meschkat, M., Ruhwedel, T., Trevisiol, A., Tzvetanova, I. D., Battefeld, A., Kusch, K., Kole, M. H. P., Strenzke, N., Möbius, W., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19152-7 · Cited by 136
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Yao, L., Bojic, D., & Liu, M. (2023) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2023.06.001 · Cited by 136
Dulamea, A. O. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-47861-6_7 · Cited by 128
Myelin plasticity in the central nervous system
Purger, D. A., Gibson, E. M., & Monje, M. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.08.001 · Cited by 133
White matter aging and its impact on brain function
Groh, J., & Simons, M. (2025) · Neuron · doi:10.1016/j.neuron.2024.10.019 · Cited by 124
Yang, Y., Cheng, Z., Tang, H., Jiao, H., Sun, X., Cui, Q., Luo, F., Pan, H., Ma, C., & Li, B. (2016) · Cerebral Cortex · doi:10.1093/cercor/bhw121 · Cited by 124
Mei, F., Mayoral, S. R., Nobuta, H., Wang, F., Desponts, C., Lorrain, D. S., Xiao, L., Green, A., Rowitch, D. H., Whistler, J. L., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.1493-16.2016 · Cited by 126
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Köhler, S., Winkler, U., & Hirrlinger, J. (2021) · Neurochemical Research · doi:10.1007/s11064-019-02926-x · Cited by 123
Boullerne, A. I. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2016.06.005 · Cited by 121
Social isolation and the brain: effects and mechanisms
Xiong, Y., Hong, H., Liu, C., & Zhang, Y. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01835-w · Cited by 137
Mitochondrial dysfunction and axon degeneration in progressive multiple sclerosis
Campbell, G. R., & Mahad, D. (2018) · FEBS Letters · doi:10.1002/1873-3468.13013 · Cited by 121
Self-citationOligodendrocyte–axon metabolic coupling is mediated by extracellular K+ and maintains axonal health
Looser, Z. J., Faik, Z., Ravotto, L., Zanker, H. S., Jung, R. B., Werner, H. B., Ruhwedel, T., Möbius, W., Bergles, D. E., Barros, L. F., et al. (2024) · Nature Neuroscience · doi:10.1038/s41593-023-01558-3 · Cited by 130
Self-citation
Metadata
- Authors
- Fünfschilling, U., Supplie, L. M., Mahad, D., Boretius, S., Saab, A. S., Edgar, J., Brinkmann, B. G., Kassmann, C. M., Tzvetanova, I. D., Möbius, W., Diaz, F., Meijer, D., Suter, U., Hamprecht, B., Sereda, M. W., Moraes, C. T., Frahm, J., Goebbels, S., & Nave, K.-A.
- Affiliations
- Max Planck Institute of Experimental Medicine (DE)
- Max Planck Society (DE)
- Newcastle University (GB)
- Erasmus MC (NL)
- ETH Zurich (CH)
- University of Miami (US)
- Corresponding author
- Nave, Klaus-Armin
- ORCID
- Venue
- Nature
- Published
- 2012-04-29
- Volume
- 485
- Issue
- 7399
- Pages
- 517-521
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3613737
- OpenAlex
- W2085029391
- Cited by
- 1,523
- References
- 33
- Citations by year
- 2026: 121 · 2025: 120 · 2024: 127 · 2023: 107 · 2022: 125 · 2021: 142 · 2020: 121 · 2019: 107 · 2018: 91 · 2017: 128 · 2016: 95 · 2015: 93 · 2014: 64 · 2013: 65 · 2012: 13
- FWCI
- 25.34
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- GRO (submittedVersion, cc-by)
- Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, other-oa)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Wellcome Trust (078415)
- Topics
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Health Sciences › Medicine › Clinical Neurology › Multiple Sclerosis Research Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- oligodendrocytes, myelination, aerobic glycolysis, lactate, mitochondrial cytochrome c oxidase, COX10, axonal integrity, demyelination, Schwann cells, white matter, brain lactate, mitochondrial respiration
- MeSH terms
- Action Potentials, Animals, Axons, Brain, Cell Survival, Electron Transport Complex IV, Demyelinating Diseases, Glycolysis, Membrane Proteins, Mitochondria, Myelin Sheath, Magnetic Resonance Spectroscopy, Oligodendroglia, Protons, Schwann Cells, Time Factors, Cell Respiration, Lactic Acid, Alkyl and Aryl Transferases, Mutant Proteins, Mice
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