The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“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]
The cited source says what the claim attributes to it.
In the citing paper
“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
The cited source says what the claim attributes to it.
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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
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 Lee et al., 2012
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Axonal transection in the lesions of multiple sclerosis
Trapp, B. D., Peterson, J., Ransohoff, R. M., Rudick, R., Mörk, S., & Bö, L. (1998) · New England Journal of Medicine · doi:10.1056/nejm199801293380502 · Cited by 4,029
Pellerin, L., & Magistretti, P. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10625 · Cited by 2,927
Self-citationAstrocyte-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
Self-citationGlycolytic oligodendrocytes maintain myelin and long-term axonal integrity
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., et al. (2012) · Nature · doi:10.1038/nature11007 · Cited by 1,523
The proton-linked monocarboxylate transporter (MCT) family: structure, function and regulation
Halestrap, A. P., & Price, N. T. (1999) · Biochemical Journal · doi:10.1042/bj3430281 · Cited by 1,346
Astrocytes as determinants of disease progression in inherited amyotrophic lateral sclerosis
Yamanaka, K., Chun, S. J., Boillee, S., Fujimori-Tonou, N., Yamashita, H., Gutmann, D. H., Takahashi, R., Misawa, H., & Cleveland, D. W. (2008) · Nature Neuroscience · doi:10.1038/nn2047 · Cited by 1,140
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
Application of a translational profiling approach for the comparative analysis of CNS cell types
Doyle, J. P., Dougherty, J. D., Heiman, M., Schmidt, E. F., Stevens, T. R., Ma, G., Bupp, S., Shrestha, P., Shah, R. D., Doughty, M. L., et al. (2008) · Cell · doi:10.1016/j.cell.2008.10.029 · Cited by 912
Axonal 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
Kang, S. H., Fukaya, M., Yang, J. K., Rothstein, J. D., & Bergles, D. E. (2010) · Neuron · doi:10.1016/j.neuron.2010.09.009 · Cited by 815
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- Rinholm, J. E. et al. Regulation of oligodendrocyte development and myelination by glucose and lactate. J. Neurosci. 31, 538–548 (2011) · DOI · Paper page
Cited by
Sorted by citations
Items 801–900 of 1,001
Exploring the selective vulnerability in Alzheimer disease using tissue specific variant analysis
Dharshini, S. A. P., Taguchi, Y., & Gromiha, M. M. (2018) · Genomics · doi:10.1016/j.ygeno.2018.05.024 · Cited by 25
The Role of Glia in Canine Degenerative Myelopathy: Relevance to Human Amyotrophic Lateral Sclerosis
Gołubczyk, D., Małysz‐Cymborska, I., Kalkowski, L., Janowski, M., Coates, J. R., Wojtkiewicz, J., Maksymowicz, W., & Walczak, P. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-1488-3 · Cited by 25
“shown by Lee and others [4], oligodendroglia do, indeed, participate in the transportation of energy substrates into axons through specialized monocarboxylate transporters”
InfluentialStimulating myelin restoration with BDNF: a promising therapeutic approach for Alzheimer's disease
Zota, I., Chanoumidou, K., Gravanis, A., & Charalampopoulos, I. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1422130 · Cited by 25
“In conclusion, the mechanisms underlying myelin breakdown in Alzheimer’s disease and the potential therapeutic benefits of enhancing myelin renewal are areas of ongoing investigation (Lee et al., 2012; Mei et al., 2016; Depp et al., 2023).”
BackgroundZhai, Y., Lu, K., Yuan, Y., Zhang, Z., Xue, L., Zhao, F., Xu, X., & Wang, H. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251329439 · Cited by 24
Beyond cell replacement: unresolved roles of NG2-expressing progenitors
Boda, E., & Buffo, A. (2014) · Frontiers in Neuroscience · doi:10.3389/fnins.2014.00122 · Cited by 26
Vasistha, N. A., Johnstone, M., Barton, S. K., Mayerl, S. E., Selvaraj, B. T., Thomson, P. A., Dando, O., Grünewald, E., Alloza, C., Bastin, M. E., et al. (2019) · Molecular Psychiatry · doi:10.1038/s41380-019-0505-2 · Cited by 21
Why TDP-43? Why Not? Mechanisms of Metabolic Dysfunction in Amyotrophic Lateral Sclerosis
Floare, M.-L., & Allen, S. P. (2020) · Neuroscience Insights · doi:10.1177/2633105520957302 · Cited by 25
Ferraiuolo, L., & Maragakis, N. J. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.135911 · Cited by 28
Glial Metabolic Reprogramming in Amyotrophic Lateral Sclerosis
Cassina, P., Miquel, E., Palma, L. M., & Cassina, A. (2021) · NeuroImmunoModulation · doi:10.1159/000516926 · Cited by 25
Zhang, M., Wang, Y., Bai, Y., Dai, L., & Guo, H. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.781063 · Cited by 26
“In the central nervous system (CNS), lactate is mainly produced by astrocytes and oligodendrocytes (OLs), and then metabolized in neurons to sustain neuronal growth (10, 11).”
BackgroundGregorio, I. D., Russo, L., Torretta, E., Barbacini, P., Contarini, G., Pacinelli, G., Bizzotto, D., Moriggi, M., Braghetta, P., Papaleo, F., et al. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00713-z · Cited by 25
Axon ensheathment and metabolic supply by glial cells in Drosophila
Schirmeier, S., Matzat, T., & Klämbt, C. (2015) · Brain Research · doi:10.1016/j.brainres.2015.09.003 · Cited by 24
Advances in Cellular Models to Explore the Pathophysiology of Amyotrophic Lateral Sclerosis
Veyrat‐Durebex, C., Corcia, P., Dangoumau, A., Laumonnier, F., Piver, É., Gordon, P. H., Andres, C. R., Vourc’h, P., & Blasco, H. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8573-9 · Cited by 28
Erickson, R. P. (2013) · Journal of Applied Genetics · doi:10.1007/s13353-012-0130-0 · Cited by 24
Novel therapeutic approaches in multiple system atrophy
Palma, J.-A., & Kaufmann, H. (2015) · Clinical Autonomic Research · doi:10.1007/s10286-014-0249-7 · Cited by 24
Neuronal expression of pathological tau accelerates oligodendrocyte progenitor cell differentiation
Ossola, B., Zhao, C., Compston, A., Pluchino, S., Franklin, R. J. M., & Spillantini, M. G. (2015) · Glia · doi:10.1002/glia.22940 · Cited by 27
GDE2 is essential for neuronal survival in the postnatal mammalian spinal cord
Cave, C., Park, S., Rodriguez, M., Nakamura, M., Höke, A., Pletnikov, M. V., & Sockanathan, S. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0148-1 · Cited by 24
Wasseff, S. K., & Scherer, S. S. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.05.018 · Cited by 24
Tissue-resident glial cells associate with tumoral vasculature and promote cancer progression
Rocha, B. G. S., Picoli, C. C., Gonçalves, B. Ô. P., da Silva, W. N., Costa, A. C., Moraes, M. M., Costa, P. A. C., Santos, G. S. P., Almeida, M. R., Silva, L. M., et al. (2022) · Angiogenesis · doi:10.1007/s10456-022-09858-1 · Cited by 24
Liu, Y.-J., Guo, J.-J., Matoga, M., Korotkova, M., Jakobsson, P.-J., & Aguzzi, A. (2024) · Nature Neuroscience · doi:10.1038/s41593-024-01663-x · Cited by 19
“However, accumulating evidence suggest that this cell lineage may have additional functions other than producing myelin sheath 31–33 , and may be actively involved in neurodegenerative processes 7,34 .”
Self-citationEmamnejad, R., Pagnin, M., & Petratos, S. (2024) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2024.105788 · Cited by 25
“This limitation includes the uptake of glucose and other metabolites, confirming the metabolic support role of OLs (Lee et al., 2012).”
Luo, F., Zhang, J., Burke, K., Romito‐DiGiacomo, R. R., Miller, R. H., & Yang, Y. (2018) · Experimental Neurology · doi:10.1016/j.expneurol.2018.05.001 · Cited by 23
“Oligodendrocyte lineage cells also provide trophic and metabolic support for neurons and other CNS cells (Lee et al., 2012; Nave, 2010).”
24S-hydroxycholesterol affects redox homeostasis in human glial U-87 MG cells
Cigliano, L., Spagnuolo, M. S., Napolitano, G., Iannotta, L., Fasciolo, G., Barone, D., & Venditti, P. (2019) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2019.02.013 · Cited by 23
Oligodendrocyte-specific ATF4 inactivation does not influence the development of EAE
Yue, Y., Stanojlović, M., Lin, Y., Karsenty, G., & Lin, W. (2019) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1415-6 · Cited by 23
Differential transcript usage in the Parkinson’s disease brain
Dick, F., Nido, G. S., Alves, G. W., Tysnes, O., Nilsen, G. H., Dölle, C., & Tzoulis, C. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1009182 · Cited by 23
“MCT1 disruption causes axonal dysfunction and neurodegeneration in cell and animal models and MCT1 levels have been found to be decreased in patients and mouse models of ALS [22, 23].”
Bartos, L. M., Kunte, S. T., Beumers, P., Xiang, X., Wind-Mark, K., Ziegler, S. I., Bartenstein, P., Choi, H., Lee, D. S., Haass, C., et al. (2022) · Journal of Nuclear Medicine · doi:10.2967/jnumed.122.264171 · Cited by 23
“Given the growing evidence for an astrocyte–neuron lactate shuttle (11,12), it will be of interest to reveal whether increasing neuronal activity (13) can stimulate glial (18)F-FDG uptake, which could be addressed using scRadiotracing.”
BackgroundCerebral Creatine Deficiency Affects the Timing of Oligodendrocyte Myelination
Rosko, L. M., Gentile, T., Smith, V. N., Manavi, Z., Melchor, G. S., Hu, J., Shults, N. V., Albanese, C., Lee, Y., Rodriguez, O. C., et al. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.2120-21.2022 · Cited by 23
“It remains unknown whether oligodendrocyte-derived creatine regulates oligodendrocyte function cell-autonomously, or can be distributed to other cell types in the brain, thereby affecting neighboring cells non–cell-autonomously (Fünfschilling et al., 2012; Lee et al., 2012).”
BackgroundSelf-citationAdvances of Genome Editing with CRISPR/Cas9 in Neurodegeneration: The Right Path towards Therapy
Klinkovskij, A., Shepelev, M. V., Isaakyan, Y. A., Aniskin, D., & Ulasov, I. V. (2023) · Biomedicines · doi:10.3390/biomedicines11123333 · Cited by 24
Lisak, R. P., Nedelkoska, L., & Benjamins, J. A. (2014) · Glia · doi:10.1002/glia.22639 · Cited by 23
Agenesis and Hypomyelination of Corpus Callosum in Mice Lacking Nsun5, an RNA Methyltransferase
Yuan, Z., Chen, P., Zhang, T., Shen, B., & Chen, L. (2019) · Cells · doi:10.3390/cells8060552 · Cited by 23
“The formation of myelin provides essential signals for the growth of axons as well as long-term structural integrity [48].”
BackgroundHeterogeneity of Oligodendrocytes and Their Precursor Cells
Hayashi, C., & Suzuki, N. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9636-7_5 · Cited by 23
Thümmler, K., Rom, E., Zeis, T., Lindner, M., Brunner, S. P., Cole, J. J., Arseni, D., Mücklisch, S., Edgar, J. M., Schaeren‐Wiemers, N., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0864-6 · Cited by 25
Evolution of glial wrapping: A new hypothesis
Rey, S., Zalc, B., & Klämbt, C. (2020) · Developmental Neurobiology · doi:10.1002/dneu.22739 · Cited by 24
“Such metabolic coupling is also observed between axons and myelin forming glial cells (Fünfschilling et al., 2012; Lee et al., 2012; Saab et al., 2016).”
BackgroundWerkman, I. L., Kövilein, J., de Jonge, J. C., & Baron, W. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15113 · Cited by 23
“Remyelination is a regenerative process in which new myelin membranes are formed and which is not only essential to recover saltatory conduction, but also to prevent neurodegeneration (Franklin and ffrench-Constant 2008; Fünfschilling et al., 2012; Irvine & Blakemore, 2008; Lee et al., 2012).”
BackgroundTau-Mediated Dysregulation of Neuroplasticity and Glial Plasticity
Koller, E. J., & Chakrabarty, P. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00151 · Cited by 23
When glia meet induced pluripotent stem cells (iPSCs)
Li, L., & Shi, Y. (2020) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2020.103565 · Cited by 24
Yan, Z., Chen, C., Rosso, G., Qian, Y., & Fan, C. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.746074 · Cited by 23
“In short, Schwann cells metabolically support axonal regeneration, however, where do Schwann cells get metabolic substrate is not completely understood A similar phenomenon occurs in the central nervous system (CNS) where astrocytes and oligodendrocytes - the glial cells in CNS - transfer lactate to neuronal axons and…”
BackgroundSupport of Nerve Conduction by Respiring Myelin Sheath: Role of Connexons
Ravera, S., Bartolucci, M., Adriano, E., Garbati, P., Ferrando, S., Ramoino, P., Calzia, D., Morelli, A. M., Balestrino, M., & Panfoli, I. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9216-0 · Cited by 23
Rezania, K., & Roos, R. P. (2012) · Neurologic Clinics · doi:10.1016/j.ncl.2012.09.014 · Cited by 23
Myelin-based inhibitors of oligodendrocyte myelination: clues from axonal growth and regeneration
Mei, F., Chong, S. Y. C., & Chan, J. R. (2013) · Neuroscience Bulletin · doi:10.1007/s12264-013-1319-x · Cited by 26
The challenges of axon survival: Introduction to the special issue on axonal degeneration
Coleman, M. P. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.06.007 · Cited by 22
Remyelination: A Potential Therapeutic Strategy for Alzheimer’s Disease?
Sun, J., Zhou, H., Bai, F., Zhang, Z., & Ren, Q. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170036 · Cited by 22
Reducing monocarboxylate transporter MCT1 worsens experimental diabetic peripheral neuropathy
Jha, M. K., Ament, X. H., Yang, F. W., Liu, Y., Polydefkis, M. J., Pellerin, L., & Morrison, B. M. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113415 · Cited by 22
Self-citationBiomarkers Utility: At the Borderline between Cardiology and Neurology
Chetran, A., Stafie, C. S., Mitu, O., Ciobanu, E. C., Iliescu-Halițchi, D., Costache, A. D., Bobric, C., Troase, R., Mitu, I., Huzum, B., et al. (2021) · Journal of Cardiovascular Development and Disease · doi:10.3390/jcdd8110139 · Cited by 25
“Oligodendrocytes are myelin-producing cells that also support axon survival and function, preventing neurodegeneration [123].”
BackgroundA metabolic biomarker predicts Parkinson’s disease at the early stages in patients and animal models
Mallet, D., Dufourd, T., Decourt, M., Carcenac, C., Bossù, P., Verlin, L., Fernagut, P., Benoit‐Marand, M., Spalletta, G., Barbier, E., et al. (2022) · DOAJ (DOAJ: Directory of Open Access Journals) · Cited by 22
Asante, I., Louie, S. G., & Yassine, H. N. (2022) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14907 · Cited by 23
Central nervous system regeneration--where are we?
Williams, A. (2013) · QJM · doi:10.1093/qjmed/hct260 · Cited by 23
Xu, X., Fan, S., He, Y., Ke, X., Song, C., Xiao, Y., Zhang, W.-H., Zhang, J.-Y., Yin, X., Kato, N., et al. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0003-3 · Cited by 25
Fluoride Alteration of [3H]Glucose Uptake in Wistar Rat Brain and Peripheral Tissues
Rogalska, A., Kuter, K. Z., Żelazko, A., Głogowska-Gruszka, A., Świętochowska, E., & Nowak, P. G. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9709-x · Cited by 22
Tang, X., Lan, M., Zhang, M., & Yao, Z. (2017) · Nitric Oxide · doi:10.1016/j.niox.2017.04.004 · Cited by 22
Skaper, S. D., Barbierato, M., Facci, L., Borri, M., Contarini, G., Zusso, M., & Giusti, P. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0722-0 · Cited by 22
Radiation-induced Demyelination and Remyelination in the Central Nervous System: A Literature Review
Helson, L. (2018) · Anticancer Research · doi:10.21873/anticanres.12818 · Cited by 22
A novel myelin protein zero transgenic zebrafish designed for rapid readout of in vivo myelination
Preston, M., Finseth, L. T., Bourne, J. N., & Macklin, W. B. (2019) · Glia · doi:10.1002/glia.23559 · Cited by 23
Eykens, C., Rossaert, E., Duqué, S. I., Rué, L., Bento‐Abreu, A., Hersmus, N., Lenaerts, A., Kerstens, A., Corthout, N., Munck, S., et al. (2021) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2021.01.006 · Cited by 24
“MCT4 to astrocytes,(17,18) MCT1 is primarily expressed in oligodendrocytes.(11) This transporter is essential to meet the local energy requirements of neurons, since nutrients can only access motor neurons at the nodes of Ranvier or at the motor neuron cell body.”
BackgroundBoggs, J. M. (2014) · Advances in neurobiology · doi:10.1007/978-1-4939-1154-7_12 · Cited by 22
The role of TSC1 and TSC2 proteins in neuronal axons
Karalis, V., Wood, D., Teaney, N. A., & Sahin, M. (2024) · Molecular Psychiatry · doi:10.1038/s41380-023-02402-7 · Cited by 21
Gyetvai, G., Hughes, T., Wedmore, F., Roe, C., Heikal, L., Ghezzi, P., & Mengozzi, M. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01394 · Cited by 20
“In addition, active mitochondrial metabolism has been recently described in mature OLs, previously thought to produce almost exclusively lactate to support neuron and axon survival (37, 74, 75).”
BackgroundDing, R., Tan, Y., Du, A., Wen, G., Ren, X., Yao, H., Ren, W., Liu, H., Wang, X., Yu, H. Q., et al. (2020) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2020.00060 · Cited by 21
Ravera, S., Morelli, A. M., & Panfoli, I. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104883 · Cited by 21
Chen, Y., Lin, Q., Liao, X., Zhou, C., & Yong He, A. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2013232118 · Cited by 22
“As mentioned previously, brain AG supports axonal growth and synapse activity (9, 19, 20, 26, 70).”
BackgroundDamiano, S., Rosa, G. L., Sozio, C., Cavaliere, G., Trinchese, G., Raia, M., Paternò, R., Mollica, M. P., Avvedimento, V. E., & Santillo, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052621 · Cited by 22
Restoration of spinal cord injury: From endogenous repairing process to cellular therapy
Wu, Y., Tang, Z., Zhang, J., Wang, Y., & Liu, S. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.1077441 · Cited by 21
“, 1997) that impair the conduction of nerve impulses (Funfschilling et al., 2012; Lee et al., 2012) can be seen in a few weeks after SCI.”
BackgroundEmerging mitochondrial‐mediated mechanisms involved in oligodendrocyte development
Gil, M., & Gama, V. (2022) · Journal of Neuroscience Research · doi:10.1002/jnr.25151 · Cited by 24
Lactate: a prospective target for therapeutic intervention in psychiatric disease
Cai, Y., Guo, H., Han, T., & Wang, H. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.387969 · Cited by 23
“…and oligodendrocytes can transport lactate into the extracellular matrix via monocarboxylate transporters (MCTs); they have also found that extracellular lactate can either enter neurons via MCT2 or by directly binding to the lactate receptor (Lee et al., 2012; Magistretti and Allaman, 2018).”
BackgroundTurner, M. P., Hubbard, N. A., Sivakolundu, D. K., Himes, L. M., Hutchison, J. L., Hart, J., Spence, J. S., Frohman, E. M., Frohman, T. C., Okuda, D. T., et al. (2018) · NeuroImage · doi:10.1016/j.neuroimage.2017.12.081 · Cited by 23
“Several studies have provided evidence for the appropriateness of gamma functions (e.g., Friston et al., 1998; Maus et al., 2012; cf. Lindquist and Wager, 2007; Lindquist et al., 2009).”
Zhang, Z., Chen, W., Zhao, Y., & Yang, Y. A. (2018) · Neuroscience Bulletin · doi:10.1007/s12264-018-0229-3 · Cited by 20
Andrés‐Benito, P., Domínguez-González, M., & Ferrer, I. (2018) · Prion · doi:10.1080/19336896.2018.1500076 · Cited by 20
“of MCT1 in organotypic cultures of the spinal cord in glucose-deprived media is toxic to neurons; the effects on neurons are reversed with the addition of lactate into the medium [29]; moreover, reduction of MCT1”
BackgroundAppikatla, S., Bessert, D. A., Lee, I., Hüttemann, M., Mullins, C. M., Somayajulu‐Nitu, M., Yao, F., & Skoff, R. P. (2013) · Glia · doi:10.1002/glia.22591 · Cited by 21
Angamo, E. A., Rösner, J., Liotta, A., Kovács, R., & Heinemann, U. (2016) · Journal of Neurophysiology · doi:10.1152/jn.00327.2016 · Cited by 21
Shan, F., Zhang, N., Yao, X., Li, Y., Wang, Z., Zhang, C., & Wang, Y. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01497-x · Cited by 20
“In the nervous system, glial cells actively uptake glycose, produce the energic substrates via glycolysis, for example, the lactate, and then provide the energy supply for the neuron and the axons through a coupling mechanism [53, 54].”
BackgroundSelf-citationThomas, E. V., Fenton, W. A., McGrath, J. M., & Horwich, A. L. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1701465114 · Cited by 23
Angamo, E. A., Haq, R. U., Rösner, J., Gabriel, S., Gerevich, Z., Heinemann, U., & Kovács, R. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091835 · Cited by 20
“Lactate release mediated by oligodendricytic MCT1 was shown to be critical for maintenance of axonal functions [15].”
BackgroundRevisiting lactate dynamics in cancer—a metabolic expertise or an alternative attempt to survive?
Mendes, C., & Serpa, J. (2020) · Journal of Molecular Medicine · doi:10.1007/s00109-020-01965-0 · Cited by 20
“was found to be embryonically lethal due to neuronal defects [249].”
BackgroundPOLR3-Related Leukodystrophy: Exploring Potential Therapeutic Approaches
Perrier, S., Michell‐Robinson, M. A., & Bernard, G. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.631802 · Cited by 23
Adult Hippocampal Neurogenesis: One Lactate to Rule Them All
Nicola, R., & Okun, E. (2021) · NeuroMolecular Medicine · doi:10.1007/s12017-021-08658-y · Cited by 21
“MCT1 deficiency induces myelination-independent axonal degeneration, an effect that can be rescued by exogenous lactate supplementation (Lee et al. 2012) (Fig.”
BackgroundMicheva, K. D., Király, M., Perez, M. M., & Madison, D. V. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.0871-21.2021 · Cited by 23
Endocannabinoid signaling in oligodendroglia
Molina‐Holgado, E., Esteban, P. F., Arévalo‐Martín, Á., Moreno‐Luna, R., Molina‐Holgado, F., & García‐Ovejero, D. (2022) · Glia · doi:10.1002/glia.24180 · Cited by 20
“energy substrates such as lactate (Fünfschilling et al., 2012; Lee et al., 2012): reviewed in Nave (2010).”
BackgroundMarangon, D., Audano, M., Pedretti, S., Fumagalli, M., Mitro, N., Lecca, D., Caruso, D., & Abbracchio, M. P. (2022) · Cells · doi:10.3390/cells11152369 · Cited by 20
“The ability of OLs to import lactate or release it extracellularly is mediated by monocarboxylate transporter 1 (MCT1), responsible for the passive transport of lactate and hydrogen towards the cytoplasm or the extracellular environment in response to its concentrations in the two compartments [47,52].”
BackgroundRossi, G., Ordazzo, G., Vanni, N. N., Castoldi, V., Iannielli, A., Silvestre, D. D., Bellini, E. N., Bernardo, L., Giannelli, S. G., Luoni, M., et al. (2023) · eLife · doi:10.7554/elife.81779 · Cited by 19
Bachmann, H., Vandemoortele, B., Vermeirssen, V., Carrette, E., Vonck, K. E. J., Boon, P., Raedt, R., & Laureys, G. (2024) · Brain stimulation · doi:10.1016/j.brs.2024.04.012 · Cited by 24
“Remyelination insulates axons from a hostile microenvironment and restores their conductive properties and metabolic interaction with oligodendrocytes [22 – 24].”
Fukushima, S., Nishikawa, K., Furube, E., Muneoka, S., Ono, K., Takebayashi, H., & Miyata, S. (2015) · Brain Research · doi:10.1016/j.brainres.2015.09.011 · Cited by 21
The non-cell-autonomous component of ALS: new in vitro models and future challenges
Ferraiuolo, L. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140168 · Cited by 21
Fibre sub‐type specific conduction reveals metabolic function in mouse sciatic nerve
Rich, L. R., & Brown, A. M. (2018) · The Journal of Physiology · doi:10.1113/jp275680 · Cited by 25
“2012), which inevitably confer unique metabolic demands on each fibre sub-type, based principally upon the consequences of ion channel distribution (Ritchie, 1995), and the emerging metabolic roles purported for myelinating cells (Lee et al. 2012; Morrison et al. 2015).”
BackgroundGuo, D., Hu, H., & Pan, S. (2019) · Medical Hypotheses · doi:10.1016/j.mehy.2019.109522 · Cited by 20
Huang, Y., Song, Y. J., Isaac, M., Miretzky, S., Patel, A., McAuliffe, W. G., & Dreyfus, C. F. (2020) · ASN NEURO · doi:10.1177/1759091420957464 · Cited by 19
“…(OLGs) are critical for the proper functioning of the central nervous system (CNS), with the responsibility of synthesizing myelin sheaths that allow for the rapid conductance of nerve signals and metabolic support (e.g., Waxman and Foster, 1980; Lee et al., 2012; Ronzano et al., 2020).”
BackgroundImpact of Fatty Acid-Binding Proteins in α-Synuclein-Induced Mitochondrial Injury in Synucleinopathy
Cheng, A., Jia, W., Kawahata, K., & Fukunaga, K. (2021) · Biomedicines · doi:10.3390/biomedicines9050560 · Cited by 19
“Neurodegenerative disorders (NDDs) are characterized by the progressive deterioration of neurons, followed by degeneration of the structure and function of axons, dendrites, and synapses, and finally leading to neuronal death [1] or dysfunction of myelination [2].”
BackgroundVerheijen, M. H. G., Peviani, M., Hendricusdottir, R., Bell, E. M., Lammens, M. M. Y., Smit, A. B., Bendotti, C., & van Minnen, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087255 · Cited by 20
Marzban, H., Kong, J., Mehr, S. E., Vriend, J. P., Li, J., Guan, T., Chung, S., Mirzaei, N., Marzban, A., Shojaei, S., et al. (2016) · Current Molecular Pharmacology · doi:10.2174/1874467209666160112125446 · Cited by 20
Bao, Y., Yang, L., Chen, Y., Zhang, B., Li, H., Tang, W., Geng, D., & Li, Y. (2018) · European Radiology · doi:10.1007/s00330-018-5506-z · Cited by 21
Self-citationBergner, C. G., Genc, N., Hametner, S., Franz, J., van der Meer, F., Mitkovski, M., Weber, M. S., Stoltenburg‐Didinger, G., Kühl, J., Köhler, W., et al. (2021) · Glia · doi:10.1002/glia.24042 · Cited by 23
“This was attributed to the tight structural and metabolic interactions within the axon-myelin unit (Fünfschilling et al., 2012; Lee et al., 2012; Stadelmann, Timmler, Barrantes-Freer, & Simons, 2019).”
BackgroundHoriuchi, M., Watanabe, S., Komine, O., Takahashi, E., Kaneko, K., Itohara, S., Shimada, M., Ogi, T., & Yamanaka, K. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01893-x · Cited by 22
“Oligodendrocytes, which produce myelin to enable saltatory conduction and provide metabolic support to axons [34], are critical for maintaining neuronal function.”
Meisingset, T. W., Ricca, A., Neri, M., Sonnewald, U., & Gritti, A. (2013) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2013.64 · Cited by 19
Becker, H. M. (2014) · Neuromethods · doi:10.1007/978-1-4939-1059-5_2 · Cited by 19
Bioenergetic Impairment in the Neuro-Glia-Vascular Unit: An Emerging Physiopathology during Aging
Yuan, M., Wang, Y., Wang, S., Huang, Z., Jin, F., Zou, Q., Li, J., Pu, Y., & Cai, Z. (2021) · Aging and Disease · doi:10.14336/ad.2021.04017 · Cited by 20
“In addition, MCT1-knockout oligodendrocytes in transgenic mice have decreased metabolism and axonopathy [121].”
BackgroundSleep Disturbance and Alzheimer’s Disease: The Glial Connection
Sunkaria, A., & Bhardwaj, S. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03578-0 · Cited by 19
Dysfunction of the oligodendrocytes in amyotrophic lateral sclerosis
Gong, Z., Ba, L., & Zhang, M. (2022) · Journal of Biomedical Research · doi:10.7555/jbr.36.20220009 · Cited by 21
Akinlaja, Y. O., & Nishiyama, A. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1418100 · Cited by 23
“Oligodendrocytes express monocarboxylate transporter 1 (Lee et al., 2012), which enables lactate uptake from the extracellular space, and its loss in oligodendrocytes causes axonal degeneration without signi fi cant demyelination or oligodendrocyte damage (Lee et al., 2012; Philips et al., 2021).”
BackgroundOláh, J., Tőkési, N., Lehotzky, A., Orosz, F., & Ovádi, J. (2013) · Cytoskeleton · doi:10.1002/cm.21137 · Cited by 19
Xiong, M., Chen, L.-X., Ma, S., Yang, Y., & Zhou, W. (2013) · Developmental Neuroscience · doi:10.1159/000346324 · Cited by 19
Role of myelin sheath energy metabolism in neurodegenerative diseases
Ravera, S., & Panfoli, I. (2015) · Neural Regeneration Research · doi:10.4103/1673-5374.167749 · Cited by 19
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
