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Oligodendroglia metabolically support axons and contribute to neurodegeneration
Open accessAbstract
Oligodendroglia support axon survival and function through mechanisms independent of myelination, and their dysfunction leads to axon degeneration in several diseases. The cause of this degeneration has not been determined, but lack of energy metabolites such as glucose or lactate has been proposed. Lactate is transported exclusively by monocarboxylate transporters, and changes to these transporters alter lactate production and use. Here we show that the most abundant lactate transporter in the central nervous system, monocarboxylate transporter 1 (MCT1, also known as SLC16A1), is highly enriched within oligodendroglia and that disruption of this transporter produces axon damage and neuron loss in animal and cell culture models. In addition, this same transporter is reduced in patients with, and in mouse models of, amyotrophic lateral sclerosis, suggesting a role for oligodendroglial MCT1 in pathogenesis. The role of oligodendroglia in axon function and neuron survival has been elusive; this study defines a new fundamental mechanism by which oligodendroglia support neurons and axons.
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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 [4]
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“It is finally in agreement with axonal degeneration observed in mice lacking the monocarboxylate transporter MCT1 in oligodendrocytes lineage cells (Lee et al., 2012;Philips et al., 2021).”
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 Lee et al., 2012
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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 Lee 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 [6]
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“Pyruvate and lactate can shuttle between glial cells and axons via monocarboxylate transporters.”
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 Lee 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 Lee et al., 2012
In the citing paper
“an essential lactate transporter in the CNS whose expression is regulated by autophagy [458].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [458]
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“and lower levels of SLC16A1/MCT1 (solute carrier family 16 member 1), an essential lactate transporter in the CNS whose expression is regulated by autophagy [458].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [458]
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“blocking neuronal oxidative utilization of lactate affects neuronal survival and even memory formation (Suzuki et al., 2011; Lee et al., 2012).”
From Metabolic reprogramming during neuronal differentiation from aerobic glycolysis to neuronal oxidative phosphorylation (2016) · cites this paper as Lee et al., 2012
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“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 Lee et al., 2012
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Windrem, M. S., Schanz, S. J., Zou, L., Chandler-Militello, D., Kuypers, N. J., Nedergaard, M., Lu, Y. Q., Mariani, J. N., & Goldman, S. A. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107658 · Cited by 62
A hypothesis for the role of axon demyelination in seizure generation
de Curtis, M., Garbelli, R., & Uva, L. (2021) · Epilepsia · doi:10.1111/epi.16824 · Cited by 57
TDP-43 mediates SREBF2-regulated gene expression required for oligodendrocyte myelination
Ho, W. Y., Chang, J., Lim, K., Cazenave‐Gassiot, A., Nguyen, A. T., Foo, J. C., Muralidharan, S., Viera-Ortiz, A., Ong, S. J. M., Hor, J. H., et al. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.201910213 · Cited by 61
“In addition to insulating the axons for saltatory conduction, myelin also provides the neurons with energy and metabolic support essential for the functional integrity of the nervous system (Nave and Werner, 2014; Lee et al., 2012).”
BackgroundHalestrap, A. P. (2013) · Comprehensive physiology · doi:10.1002/j.2040-4603.2013.tb00533.x · Cited by 61
The emerging functions of oligodendrocytes in regulating neuronal network behaviour
de Hoz, L., & Simons, M. (2014) · BioEssays · doi:10.1002/bies.201400127 · Cited by 68
Lorente Pons, A., Higginbottom, A., Cooper‐Knock, J., Alrafiah, A., Alofi, E., Kirby, J., Shaw, P. J., Wood, J. D., & Highley, J. R. (2020) · The Journal of Pathology · doi:10.1002/path.5455 · Cited by 57
“Axonal metabolism is critically dependent on the provision of glucose and lactate by oligodendrocytes [14,34], suggesting that oligodendrocyte function is important for neuronal survival.”
BackgroundA New Outlook on Mental Illnesses: Glial Involvement Beyond the Glue
Elsayed, M., & Magistretti, P. J. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00468 · Cited by 62
Self-citationGibson, E. M., & Monje, M. (2019) · Current Opinion in Oncology · doi:10.1097/cco.0000000000000578 · Cited by 60
“All rights rese aberrant neural transmission due to altered saltatory transduction; however, myelin also imparts an important metabolic role in supporting axon health [91,92].”
BackgroundThe Role of Glial Cells in Synaptic Dysfunction: Insights into Alzheimer's Disease Mechanisms
Yu, Y., Chen, R., Mao, K., Deng, M., & Li, Z. (2023) · Aging and Disease · doi:10.14336/ad.2023.0718 · Cited by 62
“Additionally, OPCs have the potential to contribute to the formation of short-term memory by modulating synaptic transmission or engaging in synapse engulfment [188].”
BackgroundBehavioral experiences as drivers of oligodendrocyte lineage dynamics and myelin plasticity
Tomlinson, L., Leiton, C. V., & Colognato, H. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.09.016 · Cited by 65
Clozapine promotes glycolysis and myelin lipid synthesis in cultured oligodendrocytes
Steiner, J. H., Martins‐de‐Souza, D., Schiltz, K., Sarnyai, Z., Westphal, S., Isermann, B., Dobrowolny, H., Turck, C. W., Bogerts, B., Bernstein, H., et al. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00384 · Cited by 58
Myelination induces axonal hotspots of synaptic vesicle fusion that promote sheath growth
Almeida, R., Williamson, J., Madden, M., Early, J. J., Voas, M. G., Talbot, W. S., Bianco, I. H., & Lyons, D. A. (2021) · Current Biology · doi:10.1016/j.cub.2021.06.036 · Cited by 59
Ma, Y., Jang, H., Jerban, S., Chang, E. Y., Chung, C. B., Bydder, G. M., & Du, J. (2022) · Applied Physics Reviews · doi:10.1063/5.0086459 · Cited by 61
Functions and dysfunctions of oligodendrocytes in neurodegenerative diseases
Han, S.-W., Gim, Y., Jang, E., & Hur, E. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.1083159 · Cited by 67
“It has been shown that disruption of MCT1 causes axonal damage and neuronal loss, and that MCT1 is reduced in patients with amyotrophic lateral sclerosis (Lee et al., 2012).”
BackgroundNeuronal endoplasmic reticulum stress in axon injury and neurodegeneration
Li, S., Liu, Y., Selzer, M. E., & Hu, Y. (2013) · Annals of Neurology · doi:10.1002/ana.24005 · Cited by 56
Self-citationShindo, A., Liang, A. C., Maki, T., Miyamoto, N., Tomimoto, H., Lo, E. H., & Arai, K. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2015.80 · Cited by 58
Differentiation but not ALS mutations in FUS rewires motor neuron metabolism
Vandoorne, T., Veys, K., Guo, W., Sicart, A., Vints, K., Swijsen, A., Moisse, M., Eelen, G., Gounko, N. V., Fumagalli, L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12099-4 · Cited by 59
The Glial Perspective on Sleep and Circadian Rhythms
Artiushin, G., & Sehgal, A. (2020) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-091819-094557 · Cited by 57
“A previous study had also reported that glutamate uptake and glutamine synthetase activity changed with time of day in the SCN, although not during constant dark conditions (Leone et al. 2015).”
BackgroundOligodendroglial Energy Metabolism and (re)Myelination
Tepavčević, V. (2021) · Life · doi:10.3390/life11030238 · Cited by 57
“The first one, which has received much attention, is the so-called “oligodendrocyte-axon lactate shuttle,” by which oligodendrocytes metabolize glucose to pyruvate through glycolysis, convert pyruvate to lactate, and then export lactate via monocarboxylate transporter 1 (MCT1), expressed on myelin [47,48], to the axon…”
BackgroundInfluentialGlial Cells Promote Myelin Formation and Elimination
Hughes, A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.661486 · Cited by 64
Gliotoxicity and Glioprotection: the Dual Role of Glial Cells
Quincozes‐Santos, A., Santos, C. L., Almeida, R. R. D. S., da Silva, A., Thomaz, N. K., Costa, N. L. F., Weber, F. B., Schmitz, I., Medeiros, L. S., Medeiros, L., et al. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02574-9 · Cited by 64
Lu, C., Dong, L., Zhou, H., Li, Q., Huang, G., Bai, S. J., & Liao, L. (2018) · Scientific Reports · doi:10.1038/s41598-018-22452-0 · Cited by 57
Otto, N., Marelja, Z., Schoofs, A., Kranenburg, H., Bittern, J., Yildirim, K., Berh, D., Bethke, M., Thomas, S., Rode, S., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05645-z · Cited by 61
Glial mitochondrial function and dysfunction in health and neurodegeneration
McAvoy, K., & Kawamata, H. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.103417 · Cited by 59
Tse, K., Cheng, A., Ma, F., & Herrup, K. (2018) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2017.11.010 · Cited by 56
Wu, M., Wong, A. Y. H., Leung, J., Kam, C., Wu, K. L., Chan, Y., Liu, K., Ip, N. Y., & Chen, S. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2106143118 · Cited by 56
Zhang, Y., Tian, L., Chen, J., Liu, X., Li, K., Liu, H., Lai, W., Shi, Y., Lin, B., & Xi, Z. (2024) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2024.116393 · Cited by 61
Ghosh, A., Kling, T., Snaidero, N., Sampaio, J. L., Shevchenko, A., Gras, H., Geurten, B. R. H., Göpfert, M. C., Schulz, J. B., Voigt, A., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003980 · Cited by 56
Oligodendrocytes in HIV-associated pain pathogenesis
Shi, Y., Shu, J., Liang, Z., Yuan, S., & Tang, S. (2016) · Molecular Pain · doi:10.1177/1744806916656845 · Cited by 56
Mot, A. I., Liddell, J. R., White, A. R., & Crouch, P. J. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.08.029 · Cited by 55
Current technical approaches to brain energy metabolism
Barros, L. F., Bolaños, J. P., Bonvento, G., Bouzier‐Sore, A., Brown, A. M., Hirrlinger, J., Kasparov, S., Kirchhoff, F., Murphy, A. N., Pellerin, L., et al. (2017) · Glia · doi:10.1002/glia.23248 · Cited by 60
“One example of this type of approach is the expression of tdTomato under the control of the promoter of the lactate transporter MCT1 gene introduced as bacterial artificial chromosome, which revealed preferential MCT1 expression in oligodendrocytes, a finding with consequences for glial-to-neuron lactate shuttling and…”
BackgroundSelf-citationWeil, M., Heibeck, S., Töpperwien, M., Dieck, S. T., Ruhwedel, T., Salditt, T., Rodicio, M. C., Morgan, J. R., Nave, K., Möbius, W., et al. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1034-18.2018 · Cited by 56
Tracey, T. J., Kirk, S. E., Steyn, F. J., & Ngo, S. T. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.08.012 · Cited by 59
Central nervous system cholesterol metabolism in health and disease
Ho, W. Y., Hartmann, H., & Ling, S. (2022) · IUBMB Life · doi:10.1002/iub.2662 · Cited by 58
“The process is known as metabolic coupling and is facilitated by the adaxonal membrane of the myelin sheath.(16,18) In addition to its role in myelin, cholesterol is involved in many aspects of synaptic biology synaptogenesis, synaptic transmission, and plasticity.”
BackgroundHarlow, D. E., Saul, K. E., Komuro, H., & Macklin, W. B. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.5151-14.2015 · Cited by 55
Metadata
- Authors
- Lee, Y., Morrison, B. M., Li, Y., Lengacher, S., Farah, M. H., Hoffman, P. N., Liu, Y., Tsingalia, A., Jin, L., Zhang, P.-W., Pellerin, L., Magistretti, P. J., & Rothstein, J. D.
- Affiliations
- Johns Hopkins University (US)
- École Polytechnique Fédérale de Lausanne (CH)
- University of Lausanne (CH)
- Corresponding author
- Rothstein, Jeffrey D.
- ORCID
- Venue
- Nature
- Published
- 2012-07
- Volume
- 487
- Issue
- 7408
- Pages
- 443-448
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3408792
- OpenAlex
- W2038811384
- Cited by
- 1,664
- References
- 49
- Citations by year
- 2026: 110 · 2025: 107 · 2024: 130 · 2023: 118 · 2022: 133 · 2021: 150 · 2020: 141 · 2019: 107 · 2018: 110 · 2017: 133 · 2016: 107 · 2015: 106 · 2014: 98 · 2013: 97 · 2012: 13
- FWCI
- 72.44
- 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)
- SERVAL (Université de Lausanne) (acceptedVersion, other-oa)
- IRIS (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Funders
- National Science Foundation
- Muscular Dystrophy Association
- Johns Hopkins University
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (31003A, 108336, 125063)
- Fonds De La Recherche Scientifique - FNRS
- National Institutes of Health
- National Institute on Aging (P50AG005146, P50AG05146)
- National Institute of Neurological Disorders and Stroke (P01NS016375, NS 33958, P01 NS16375, R01NS033958)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Multiple Sclerosis Research Studies
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Keywords
- oligodendroglia, MCT1, lactate transport, axonal degeneration, neurodegeneration, amyotrophic lateral sclerosis, oligodendrocytes, neuronal loss, lactate export
- MeSH terms
- Superoxide Dismutase-1, Monocarboxylate Transport Protein 1, Amyotrophic Lateral Sclerosis, Animals, Axons, Cell Line, Cell Survival, Disease Models, Animal, Heterozygote, Humans, Mice, Transgenic, Motor Neurons, Myelin Sheath, Nerve Degeneration, Oligodendroglia, Superoxide Dismutase, Down-Regulation, Lactic Acid, Protein Transport, Monocarboxylic Acid Transporters, Symporters, RNA, Small Interfering, Mice
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