{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T11:49:10Z","timestamp":1791978550890,"version":"4.4.0"},"reference-count":81,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2023,7,31]],"date-time":"2023-07-31T00:00:00Z","timestamp":1690761600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"JSPS KAKENHI","award":["19K07508 (YC)"],"award-info":[{"award-number":["19K07508 (YC)"]}]},{"name":"JSPS KAKENHI","award":["20K16193 (RM)"],"award-info":[{"award-number":["20K16193 (RM)"]}]},{"name":"JSPS KAKENHI","award":["20K16550 (NU)"],"award-info":[{"award-number":["20K16550 (NU)"]}]},{"name":"JSPS KAKENHI","award":["19K07508 (YC)"],"award-info":[{"award-number":["19K07508 (YC)"]}]},{"name":"JSPS KAKENHI","award":["20K16193 (RM)"],"award-info":[{"award-number":["20K16193 (RM)"]}]},{"name":"JSPS KAKENHI","award":["20K16550 (NU)"],"award-info":[{"award-number":["20K16550 (NU)"]}]},{"name":"JSPS KAKENHI","award":["19K07508 (YC)"],"award-info":[{"award-number":["19K07508 (YC)"]}]},{"name":"JSPS KAKENHI","award":["20K16193 (RM)"],"award-info":[{"award-number":["20K16193 (RM)"]}]},{"name":"JSPS KAKENHI","award":["20K16550 (NU)"],"award-info":[{"award-number":["20K16550 (NU)"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pharmaceutics"],"abstract":"<jats:p>The choroid plexus (CP) plays central roles in regulating the microenvironment of the central nervous system by secreting the majority of cerebrospinal fluid (CSF) and controlling its composition. A monolayer of epithelial cells of CP plays a significant role in forming the blood\u2013CSF barrier to restrict the movement of substances between the blood and ventricles. CP epithelial cells are equipped with transporters for glucose and lactate that are used as energy sources. There are many review papers on glucose transporters in CP epithelial cells. On the other hand, distribution of monocarboxylate transporters (MCTs) in CP epithelial cells has received less attention compared with glucose transporters. Some MCTs are known to transport lactate, pyruvate, and ketone bodies, whereas others transport thyroid hormones. Since CP epithelial cells have significant carrier functions as well as the barrier function, a decline in the expression and function of these transporters leads to a poor supply of thyroid hormones as well as lactate and can contribute to the process of age-associated brain impairment and pathophysiology of neurodegenerative diseases. In this review paper, recent findings regarding the distribution and significance of MCTs in the brain, especially in CP epithelial cells, are summarized.<\/jats:p>","DOI":"10.3390\/pharmaceutics15082062","type":"journal-article","created":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T09:14:40Z","timestamp":1690881280000},"page":"2062","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Distribution of Monocarboxylate Transporters in Brain and Choroid Plexus Epithelium"],"prefix":"10.3390","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6592-3573","authenticated-orcid":false,"given":"Masaki","family":"Ueno","sequence":"first","affiliation":[{"name":"Department of Pathology and Host Defense, Faculty of Medicine, Kagawa University, Takamatsu 761-0793, Kagawa, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoichi","family":"Chiba","sequence":"additional","affiliation":[{"name":"Department of Pathology and Host Defense, Faculty of Medicine, Kagawa University, Takamatsu 761-0793, Kagawa, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryuta","family":"Murakami","sequence":"additional","affiliation":[{"name":"Department of Pathology and Host Defense, Faculty of Medicine, Kagawa University, Takamatsu 761-0793, Kagawa, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yumi","family":"Miyai","sequence":"additional","affiliation":[{"name":"Department of Pathology and Host Defense, Faculty of Medicine, Kagawa University, Takamatsu 761-0793, Kagawa, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Koichi","family":"Matsumoto","sequence":"additional","affiliation":[{"name":"Department of Pathology and Host Defense, Faculty of Medicine, Kagawa University, Takamatsu 761-0793, Kagawa, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Keiji","family":"Wakamatsu","sequence":"additional","affiliation":[{"name":"Department of Pathology and Host Defense, Faculty of Medicine, Kagawa University, Takamatsu 761-0793, Kagawa, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Genta","family":"Takebayashi","sequence":"additional","affiliation":[{"name":"Department of Anesthesiology, Faculty of Medicine, Kagawa University, Takamatsu 761-0793, Kagawa, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naoya","family":"Uemura","sequence":"additional","affiliation":[{"name":"Department of Anesthesiology, Faculty of Medicine, Kagawa University, Takamatsu 761-0793, Kagawa, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ken","family":"Yanase","sequence":"additional","affiliation":[{"name":"Department of Anesthesiology, Faculty of Medicine, Kagawa University, Takamatsu 761-0793, Kagawa, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,7,31]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/2045-8118-8-3","article-title":"Molecular biology of the blood-brain and the blood-cerebrospinal fluid barriers: Similarities and differences","volume":"8","author":"Redzic","year":"2011","journal-title":"Fluids Barriers CNS"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1152\/physrev.00050.2017","article-title":"Blood-Brain Barrier: From Physiology to Disease and Back","volume":"99","author":"Sweeney","year":"2019","journal-title":"Physiol. Rev."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1124\/dmd.119.089516","article-title":"Abundant Expression of OCT2, MATE1, OAT1, OAT3, PEPT2, BCRP, MDR1, and xCT Transporters in Blood-Arachnoid Barrier of Pig and Polarized Localizations at CSF- and Blood-Facing Plasma Membranes","volume":"48","author":"Uchida","year":"2020","journal-title":"Drug Metab. Dispos."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1363","DOI":"10.1007\/s11095-022-03193-2","article-title":"Pharmacoproteomics of Brain Barrier Transporters and Substrate Design for the Brain Targeted Drug Delivery","volume":"39","author":"Huttunen","year":"2022","journal-title":"Pharm. Res."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1083\/jcb.34.1.207","article-title":"Fine structural localization of a blood-brain barrier to exogenous peroxidase","volume":"34","author":"Reese","year":"1967","journal-title":"J. Cell Biol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1083\/jcb.40.3.648","article-title":"Junctions between intimately apposed cell membranes in the vertebrate brain","volume":"40","author":"Brightman","year":"1969","journal-title":"J. Cell Biol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1007\/s00401-018-1815-1","article-title":"Functional morphology of the blood\u2013brain barrier in health and disease","volume":"135","author":"Liebner","year":"2018","journal-title":"Acta Neuropathol."},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Ueno, M., Chiba, Y., Murakami, R., Matsumoto, K., Fujihara, R., Uemura, N., Yanase, K., and Kamada, M. (2019). Disturbance of Intracerebral Fluid Clearance and Blood\u2013Brain Barrier in Vascular Cognitive Impairment. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20102600"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1208\/s12248-017-0110-8","article-title":"SLC and ABC Transporters: Expression, Localization, and Species Differences at the Blood-Brain and the Blood-Cerebrospinal Fluid Barriers","volume":"19","author":"Morris","year":"2017","journal-title":"AAPS J."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Praetorius, J., Blazer-Yost, B., and Damkier, H. (2020). Role of the Choroid Plexus in Health and Disease, Springer.","DOI":"10.1007\/978-1-0716-0536-3"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"C673","DOI":"10.1152\/ajpcell.00041.2017","article-title":"Transport across the choroid plexus epithelium","volume":"312","author":"Praetorius","year":"2017","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1517\/17425247.2016.1171315","article-title":"CSF, blood-brain barrier, and brain drug delivery","volume":"13","author":"Pardridge","year":"2016","journal-title":"Expert Opin. Drug Deliv."},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Wakamatsu, K., Chiba, Y., Murakami, R., Miyai, Y., Matsumoto, K., Kamada, M., Nonaka, W., Uemura, N., Yanase, K., and Ueno, M. (2022). Metabolites and Biomarker Compounds of Neurodegenerative Diseases in Cerebrospinal Fluid. Metabolites, 12.","DOI":"10.3390\/metabo12040343"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"101","DOI":"10.3171\/jns.1993.78.1.0101","article-title":"Colloid cyst of the third ventricle. A comparative immunohisto-chemical study of neuraxis cysts and choroid plexus epithelium","volume":"78","author":"Lach","year":"1993","journal-title":"J. Neurosurg."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1007\/s00428-005-0133-x","article-title":"Podoplanin is expressed in subsets of tumors of the central nervous system","volume":"448","author":"Shibahara","year":"2006","journal-title":"Virchows Arch."},{"key":"ref_16","first-page":"33","article-title":"Cell contact protein beta-catenin in ependymal and epithelial cells of the choroid plexus of the cerebral lateral ventricles","volume":"149","author":"Kirik","year":"2016","journal-title":"Morphology"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/S0065-1281(86)80016-2","article-title":"Detection of cytokeratin(s) in epithelium of human Plexus choroideus by monoclonal antibodies","volume":"78","author":"Kasper","year":"1986","journal-title":"Acta Histochem."},{"key":"ref_18","first-page":"231","article-title":"Intermediate filament proteins in choroid plexus and ependyma and their tumors","volume":"123","author":"Miettinen","year":"1986","journal-title":"Am. J. Pathol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1002\/jcb.240340402","article-title":"Immunohistochemical demonstration of proteinase inhibitor alpha-1-antichymotrypsin in normal human central nervous system","volume":"34","author":"Justice","year":"1987","journal-title":"J. Cell. Biochem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1847","DOI":"10.1152\/physrev.00004.2013","article-title":"Cerebrospinal Fluid Secretion by the Choroid Plexus","volume":"93","author":"Damkier","year":"2013","journal-title":"Physiol. Rev."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.expneurol.2015.02.032","article-title":"A balanced view of choroid plexus structure and function: Focus on adult humans","volume":"267","author":"Spector","year":"2015","journal-title":"Exp. Neurol."},{"key":"ref_22","unstructured":"Johanson, C.E., and Keep, R.F. (2020). Role of the Choroid Plexus in Health and Disease, Springer."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Chiba, Y., Murakami, R., Matsumoto, K., Wakamatsu, K., Nonaka, W., Uemura, N., Yanase, K., Kamada, M., and Ueno, M. (2020). Glucose, Fructose, and Urate Transporters in the Choroid Plexus Epithelium. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21197230"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1007\/s00418-015-1366-7","article-title":"Immunohistochemical analysis of transporters related to clearance of amyloid-\u03b2 peptides through blood\u2013cerebrospinal fluid barrier in human brain","volume":"144","author":"Matsumoto","year":"2015","journal-title":"Histochem. Cell Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1111\/neup.12791","article-title":"Immunohistochemical expression of osteopontin and collagens in choroid plexus of human brains","volume":"42","author":"Wakamatsu","year":"2022","journal-title":"Neuropathology"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/j.mam.2012.05.003","article-title":"The SLC16 gene family\u2014Structure, role and regulation in health and disease","volume":"34","author":"Halestrap","year":"2013","journal-title":"Mol. Asp. Med."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"279","DOI":"10.2220\/biomedres.36.279","article-title":"Cellular distributions of monocarboxylate transporters: A review","volume":"36","author":"Iwanaga","year":"2015","journal-title":"Biomed. Res."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1357","DOI":"10.1210\/me.2007-0112","article-title":"Effective Cellular Uptake and Efflux of Thyroid Hormone by Human Monocarboxylate Transporter 10","volume":"22","author":"Friesema","year":"2008","journal-title":"Mol. Endocrinol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/iub.573","article-title":"The monocarboxylate transporter family-Structure and functional characterization","volume":"64","author":"Halestrap","year":"2012","journal-title":"IUBMB Life"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1471-4159.2005.03168.x","article-title":"Monocarboxylate transporters in the central nervous system: Distribution, regulation and function","volume":"94","author":"Pierre","year":"2005","journal-title":"J. Neurochem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.2174\/13816128113199990462","article-title":"Role of Monocarboxylate Transporters in Drug Delivery to the Brain","volume":"20","author":"Vijay","year":"2014","journal-title":"Curr. Pharm. Des."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"2053","DOI":"10.1074\/jbc.M511577200","article-title":"Modulation of Monocarboxylic Acid Transporter-1 Kinetic Function by the cAMP Signaling Pathway in Rat Brain Endothelial Cells","volume":"281","author":"Smith","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Uhernik, A.L., Li, L., LaVoy, N., Velasquez, M.J., and Smith, J.P. (2014). Regulation of Monocarboxylic Acid Transporter-1 by cAMP Dependent Vesicular Trafficking in Brain Microvascular Endothelial Cells. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0085957"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"C1319","DOI":"10.1152\/ajpcell.2001.280.5.C1319","article-title":"Mouse MCT3 gene is expressed preferentially in retinal pigment and choroid plexus epithelia","volume":"280","author":"Philp","year":"2001","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1038\/jcbfm.2014.206","article-title":"Lactate transport and signaling in the brain: Potential therapeutic targets and roles in body-brain interaction","volume":"35","author":"Bergersen","year":"2015","journal-title":"J. Cereb. Blood Flow. Metab."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1104","DOI":"10.1111\/jnc.13147","article-title":"Quantitative targeted absolute proteomics of rat blood-cerebrospinal fluid barrier transporters: Comparison with a human specimen","volume":"134","author":"Uchida","year":"2015","journal-title":"J. Neurochem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.mam.2012.07.001","article-title":"The SLC2 (GLUT) family of membrane transporters","volume":"34","author":"Mueckler","year":"2013","journal-title":"Mol. Asp. Med."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1152\/physrev.00055.2009","article-title":"Biology of Human Sodium Glucose Transporters","volume":"91","author":"Wright","year":"2011","journal-title":"Physiol. Rev."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/S0165-3806(98)00188-6","article-title":"Monocarboxylate transporter (MCT1) abundance in brains of sucking and adult rats: A quantitative electron microscopic immunogold study","volume":"113","author":"Leino","year":"1999","journal-title":"Brain Res."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.brainres.2012.08.026","article-title":"Regulation of Mct1 by cAMP-dependent internalization in rat brain endothelial cells","volume":"1480","author":"Smith","year":"2012","journal-title":"Brain Res."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1002\/glia.22667","article-title":"Cellular distribution of glucose and monocarboxylate transporters in human brain white matter and multiple sclerosis lesions","volume":"62","author":"Nijland","year":"2014","journal-title":"Glia"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1523\/JNEUROSCI.3516-10.2011","article-title":"Regulation of Oligodendrocyte Development and Myelination by Glucose and Lactate","volume":"31","author":"Rinholm","year":"2011","journal-title":"J. Neurosci."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"135479","DOI":"10.1016\/j.neulet.2020.135479","article-title":"Immunoreactivity of receptor and transporters for lactate located in astrocytes and epithelial cells of choroid plexus of human brain","volume":"741","author":"Murakami","year":"2021","journal-title":"Neurosci. Lett."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.neo.2016.12.011","article-title":"pH, Lactate, and Hypoxia: Reciprocity in Regulating High-Affinity Monocarboxylate Transporter Expression in Glioblastoma","volume":"19","author":"Caruso","year":"2017","journal-title":"Neoplasia"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"C921","DOI":"10.1152\/ajpcell.2000.278.5.C921","article-title":"Monocarboxylic acid transporters, MCT1 and MCT2, in cortical astrocytes in vitro and in vivo","volume":"278","author":"Hanu","year":"2000","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1016\/S0306-4522(00)00294-3","article-title":"Cell-specific localization of monocarboxylate transporters, MCT1 and MCT2, in the adult mouse brain revealed by double immunohistochemical labeling and confocal microscopy","volume":"100","author":"Pierre","year":"2000","journal-title":"Neuroscience"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"1002","DOI":"10.1007\/s12035-021-02651-z","article-title":"Knockdown of Astrocytic Monocarboxylate Transporter 4 in the Motor Cortex Leads to Loss of Dendritic Spines and a Deficit in Motor Learning","volume":"59","author":"Lundquist","year":"2022","journal-title":"Mol. Neurobiol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1042\/bj3500219","article-title":"The low-affinity monocarboxylate transporter MCT4 is adapted to the export of lactate in highly glycolytic cells","volume":"350","author":"Dimmer","year":"2000","journal-title":"Biochem. J."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bbacli.2015.11.001","article-title":"Glioblastomas with copy number gains in EGFR and RNF139 show increased expressions of carbonic anhydrase genes transformed by ENO1","volume":"5","author":"Beckner","year":"2016","journal-title":"BBA Clin."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1093\/hmg\/3.7.1133","article-title":"A novel transmembrane transporter encoded by the XPCT gene in Xq13.2","volume":"3","author":"Carrel","year":"1994","journal-title":"Hum. Mol. Genet."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"40128","DOI":"10.1074\/jbc.M300909200","article-title":"Identification of Monocarboxylate Transporter 8 as a Specific Thyroid Hormone Transporter","volume":"278","author":"Friesema","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.tem.2007.11.003","article-title":"Thyroid hormone transport in and out of cells","volume":"19","author":"Visser","year":"2008","journal-title":"Trends Endocrinol. Metab."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1210\/me.2010-0095","article-title":"Minireview: Thyroid Hormone Transporters: The Knowns and the Unknowns","volume":"25","author":"Visser","year":"2011","journal-title":"Mol. Endocrinol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"98","DOI":"10.3389\/fendo.2014.00098","article-title":"Transport of Thyroid Hormone in Brain","volume":"5","author":"Wirth","year":"2014","journal-title":"Front. Endocrinol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"6251","DOI":"10.1210\/en.2008-0378","article-title":"Expression of the Thyroid Hormone Transporters Monocarboxylate Transporter-8 (SLC16A2) and Organic Ion Transporter-14 (SLCO1C1) at the Blood-Brain Barrier","volume":"149","author":"Roberts","year":"2008","journal-title":"Endocrinology"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"9439","DOI":"10.1523\/JNEUROSCI.6055-08.2009","article-title":"Neuronal 3\u2019,3,5-triiodothyronine (T3) uptake and behavioral phenotype of mice deficient in Mct8, the neuronal T3 transporter mutated in Allan-Herndon-Dudley syndrome","volume":"30","author":"Wirth","year":"2009","journal-title":"J. Neurosci."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1002\/glia.21116","article-title":"Developmental and cell type-specific expression of thyroid hormone transporters in the mouse brain and in primary brain cells","volume":"59","author":"Braun","year":"2011","journal-title":"Glia"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1366","DOI":"10.1089\/thy.2019.0544","article-title":"Spatiotemporal Changes of Cerebral Monocarboxylate Transporter 8 Expression","volume":"30","author":"Wilpert","year":"2020","journal-title":"Thyroid"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"4322","DOI":"10.1210\/jc.2004-2567","article-title":"Neuroanatomical Pathways for Thyroid Hormone Feedback in the Human Hypothalamus","volume":"90","author":"Alkemade","year":"2005","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1701","DOI":"10.1210\/en.2004-1179","article-title":"The Monocarboxylate Transporter 8 Linked to Human Psychomotor Retardation Is Highly Expressed in Thyroid Hormone-Sensitive Neuron Populations","volume":"146","author":"Heuer","year":"2005","journal-title":"Endocrinology"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"E967","DOI":"10.1210\/jc.2010-2750","article-title":"Expression of thyroid hormone trans-porters in the human hypothalamus","volume":"96","author":"Alkemade","year":"2011","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1086\/431313","article-title":"Allan-Herndon-Dudley syndrome and the mono-carboxylate transporter 8 (MCT8) gene","volume":"77","author":"Schwartz","year":"2005","journal-title":"Am. J. Hum. Genet."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"882788","DOI":"10.3389\/fendo.2022.882788","article-title":"Mathematical modeling and simulation of thyroid homeostasis: Implications for the Allan-Herndon-Dudley syndrome","volume":"13","author":"Wolff","year":"2022","journal-title":"Front. Endocrinol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"30096","DOI":"10.1074\/jbc.272.48.30096","article-title":"Comparison of Lactate Transport in Astroglial Cells and Monocarboxylate Transporter 1 (MCT 1) Expressing Xenopus laevis Oocytes. Expression of two different monocarboxylate transporters in astroglial cells and neurons","volume":"272","author":"Rahman","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1111\/j.1471-4159.2008.05650.x","article-title":"Basal and stimulated lactate fluxes in primary cultures of astrocytes are differentially controlled by distinct proteins","volume":"107","author":"Maekawa","year":"2008","journal-title":"J. Neurochem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1002\/glia.22618","article-title":"Oxygen tension controls the expression of the monocarboxylate transporter MCT4 in cultures mouse cortical astrocytes via a hypoxia-inducible factor-1alpha-mediated transcriptional regulation","volume":"62","author":"Rostafio","year":"2014","journal-title":"Glia"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1159\/000017324","article-title":"Evidence Supporting the Existence of an Activity-Dependent Astrocyte-Neuron Lactate Shuttle","volume":"20","author":"Pellerin","year":"1998","journal-title":"Dev. Neurosci."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1097\/MCO.0b013e328312c368","article-title":"Brain energetics (thought needs fond)","volume":"11","author":"Pellerin","year":"2008","journal-title":"Curr. Opin. Clin. Nutr. Metab. Care"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"2481","DOI":"10.1016\/j.bbamcr.2016.03.013","article-title":"Monocarboxylate transporters in the brain and in cancer","volume":"1863","author":"Sboarina","year":"2016","journal-title":"Biochim. Biophys. Acta (BBA)\u2014Mol. Cell Res."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1097\/00004647-199611000-00001","article-title":"Selective Distribution of Lactate Dehydrogenase Isoenzymes in Neurons and Astrocytes of Human Brain","volume":"16","author":"Bittar","year":"1996","journal-title":"J. Cereb. Blood Flow Metab."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Leen, W.G., Willemsen, M.A., Wevers, R.A., and Verbeek, M.M. (2012). Cerebrospinal Fluid Glucose and Lactate: Age-Specific Reference Values and Implications for Clinical Practice. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0042745"},{"key":"ref_72","first-page":"537","article-title":"Biomarkers of Cerebral Glucose Metabolism and Neurodegeneration in Parkinson\u2019s Disease: A Cerebrospinal Fluid-Based Study","volume":"12","author":"Liguori","year":"2022","journal-title":"J. Park. Dis."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/j.neurobiolaging.2021.05.011","article-title":"Brain energy metabolism and neurodegeneration: Hints from CSF lactate levels in dementias","volume":"105","author":"Bonomi","year":"2021","journal-title":"Neurobiol. Aging"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"2784","DOI":"10.1093\/cercor\/bht136","article-title":"Lactate Receptor Sites Link Neurotransmission, Neurovascular Coupling, and Brain Energy Metabolism","volume":"24","author":"Lauritzen","year":"2014","journal-title":"Cereb. Cortex"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1002\/cne.903220405","article-title":"Selective vulnerability of the hippocampal pyramidal neurons to hypothyroidism in male and female rats","volume":"322","author":"Madeira","year":"1992","journal-title":"J. Comp. Neurol."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Bakalov, D., Iliev, P., Sabit, Z., Tafradjiiska-Hadjiolova, R., and Bocheva, G. (2023). Attenuation of Hypothyroidism-Induced Cognitive Impairment by Modulating Serotonin Mediation. Vet. Sci., 10.","DOI":"10.3390\/vetsci10020122"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1177\/13591053221107745","article-title":"Cognitive decline in mid-life: Changes in memory and cognition related to hypothyroidism","volume":"28","author":"Stern","year":"2022","journal-title":"J. Health Psychol."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Ye, Y., Wang, Y., Li, S., Guo, J., Ding, L., and Liu, M. (2022). Association of Hypothyroidism and the Risk of Cognitive Dysfunction: A Meta-Analysis. J. Clin. Med., 11.","DOI":"10.3390\/jcm11226726"},{"key":"ref_79","first-page":"276","article-title":"The Role of Thyroid Dysfunction in Alzheimer\u2019s Disease: A Systematic Review and Meta-Analysis","volume":"10","author":"Salehipour","year":"2023","journal-title":"J. Prev. Alzheimer\u2019s Dis."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"66","DOI":"10.3389\/fnins.2015.00066","article-title":"Transport of thyroid hormones via the choroid plexus into the brain: The roles of transthyretin and thyroid hormone transmembrane transporters","volume":"9","author":"Richardson","year":"2015","journal-title":"Front. Neurosci."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1097\/RMR.0000000000000303","article-title":"Functional Magnetic Resonance Spectroscopy of Lactate in Alzheimer Disease: A Comprehensive Review of Alzheimer Disease Pathology and the Role of Lactate","volume":"32","author":"Shirbandi","year":"2023","journal-title":"Top. Magn. Reson. Imaging"}],"container-title":["Pharmaceutics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4923\/15\/8\/2062\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T20:23:24Z","timestamp":1760127804000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4923\/15\/8\/2062"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,7,31]]},"references-count":81,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2023,8]]}},"alternative-id":["pharmaceutics15082062"],"URL":"https:\/\/doi.org\/10.3390\/pharmaceutics15082062","relation":{},"ISSN":["1999-4923"],"issn-type":[{"value":"1999-4923","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,7,31]]}}}