Gatt, S. Enzymic hydrolysis and synthesis of ceramides. J. Biol. Chem. 238, 3131–3133 (1963).
Li, C. M. et al. The human acid ceramidase gene (ASAH): structure, chromosomal location, mutation analysis, and expression. Genomics 62, 223–231 (1999).
van Eijk, M., Ferraz, M. J., Boot, R. G. & Aerts, J. Lyso-glycosphingolipids: presence and consequences. Essays Biochem 64, 565–578 (2020).
Tsuboi, K. et al. Involvement of acid ceramidase in the degradation of bioactive N-acylethanolamines. Biochimica et. Biophysica Acta (BBA) – Mol. Cell Biol. Lipids 1866, 158972 (2021).
Sugita, M., Dulaney, J. T. & Moser, H. W. Ceramidasedeficiency in Farber’s disease (lipogranulomatosis). Science 178, 1100–1102 (1972).
Fujiwaki, T. et al. Tissue accumulation of sulfatide and GM3 ganglioside in a patient with variant Farber disease. Clin. Chim. Acta 234, 23–36 (1995).
Yu, F. P. S., Amintas, S., Levade, T. & Medin, J. A. Acid ceramidase deficiency: Farber disease and SMA-PME. Orphanet J. Rare Dis. 13, 121 (2018).
Elsea, S. H. et al. ASAH1 pathogenic variants associated with acid ceramidase deficiency: Farber disease and spinal muscular atrophy with progressive myoclonic epilepsy. Hum. Mutat. 41, 1469–1487 (2020).
Fiumara, A., Nigro, F., Pavone, L. & Moser, H. W. Farber disease with prolonged survival. J. Inherit. Metab. Dis. 16, 915–916 (1993).
Goudie, C. et al. Hematopoietic stem cell transplant does not prevent neurological deterioration in infants with Farber disease: Case report and literature review. JIMD Rep. 46, 46–51 (2019).
Zhou, J. et al. Spinal muscular atrophy associated with progressive myoclonic epilepsy is caused by mutations in ASAH1. Am. J. Hum. Genet 91, 5–14 (2012).
Haluk, T. & Judith, M. Spinal muscular atrophy associated with progressive myoclonus epilepsy. Epileptic Disord. 18, 128–134 (2016).
Shervin Badv, R., Nilipour, Y., Rahimi-Dehgolan, S., Rashidi-Nezhad, A. & Ghahvechi Akbari, M. A novel case report of spinal muscular atrophy with progressive myoclonic epilepsy from Iran. Int Med Case Rep. J. 12, 155–159 (2019).
Filosto, M. et al. ASAH1 variant causing a mild SMA phenotype with no myoclonic epilepsy: a clinical, biochemical and molecular study. Eur. J. Hum. Genet 24, 1578–1583 (2016).
Rubboli, G. et al. Spinal muscular atrophy associated with progressive myoclonic epilepsy: A rare condition caused by mutations in ASAH1. Epilepsia 56, 692–698 (2015).
Teoh, H. L. et al. Polyarticular arthritis and spinal muscular atrophy in acid ceramidase deficiency. Pediatrics 138, e20161068 (2016).
Ame van der Beek, N. et al. A new case of SMA phenotype without epilepsy due to biallelic variants in ASAH1. Eur. J. Hum. Genet 27, 337–339 (2019).
Jankovic, J. & Rivera, V. M. Hereditary myoclonus and progressive distal muscular atrophy. Ann. Neurol. 6, 227–231 (1979).
Lance, J. W. & Evans, W. A. Progressive myoclonic epilepsy, nerve deafness and spinal muscular atrophy. Clin. Exp. Neurol. 20, 141–151 (1984).
Liyanage, D. S., Pathberiya, L. S., Gooneratne, I. K., Vithanage, K. K. & Gamage, R. Association of type IV spinal muscular atrophy (SMA) with myoclonic epilepsy within a single family. Int. Arch. Med. 7, 42 (2014).
Taglioli, M., Bartolini, S., Volpi, G., Alberti, G. & Ambrosetto, G. [Progressive familial myoclonic epilepsy with bulbo-spinal amyotrophy. Clinical, electrophysiological study, and biopsy of a case]. Riv. Neurol. 60, 201–206 (1990).
Giráldez, B. G. et al. Uniparental disomy as a cause of spinal muscular atrophy and progressive myoclonic epilepsy: Phenotypic homogeneity due to the homozygous c.125C>T mutation in ASAH1. Neuromuscul. Disord. 25, 222–224 (2015).
Dyment, D. A. et al. Evidence for clinical, genetic and biochemical variability in spinal muscular atrophy with progressive myoclonic epilepsy. Clin. Genet. 86, 558–563 (2014).
Lefebvre, S. et al. Identification and characterization of a spinal muscular atrophy-determining gene. Cell 80, 155–165 (1995).
Kolb, S. J. & Kissel, J. T. Spinal muscular atrophy: a timely review. Arch. Neurol. 68, 979–984 (2011).
Querin, G. et al. The spinal and cerebral profile of adult spinal-muscular atrophy: A multimodal imaging study. NeuroImage: Clin. 21, 101618 (2019).
Yonekawa, T., Komaki, H., Saito, Y., Sugai, K. & Sasaki, M. Peripheral nerve abnormalities in pediatric patients with spinal muscular atrophy. Brain Dev. 35, 165–171 (2013).
Chedrawi, A. K. et al. Novel V97G ASAH1 mutation found in Farber disease patients: unique appearance of the disease with an intermediate severity, and marked early involvement of central and peripheral nervous system. Brain Dev. 34, 400–404 (2012).
Molz, G. Farbersche Krankheit. Virchows Arch. A 344, 86–99 (1968).
Körver, S., Vergouwe, M., Hollak, C. E. M., van Schaik, I. N. & Langeveld, M. Development and clinical consequences of white matter lesions in Fabry disease: a systematic review. Mol. Genet. Metab. 125, 205–216 (2018).
Davies, E. H., Seunarine, K. K., Banks, T., Clark, C. A. & Vellodi, A. Brain white matter abnormalities in paediatric Gaucher Type I and Type III using diffusion tensor imaging. J. Inherit. Metab. Dis. 34, 549–553 (2011).
Di Rocco, M. et al. Different molecular mechanisms leading to white matter hypomyelination in infantile onset lysosomal disorders. Neuropediatrics 36, 265–269 (2005).
Resende, L. L., Paiva, A. R. Bd, Kok, F., Leite, Cd. C. & Lucato, L. T. Adult leukodystrophies: A step-by-step diagnostic approach. RadioGraphics 39, 153–168 (2019).
Eliyahu, E., Park, J.-H., Shtraizent, N., He, X. & Schuchman, E. H. Acid ceramidase is a novel factor required for early embryo survival. FASEB J. 21, 1403–1409 (2007).
Li, C.-M. et al. Insertional mutagenesis of the mouse acid ceramidase gene leads to early embryonic lethality in homozygotes and progressive lipid storage disease in heterozygotes. Genomics 79, 218–224 (2002).
Alayoubi, A. M. et al. Systemic ceramide accumulation leads to severe and varied pathological consequences. EMBO Mol. Med. 5, 827–842 (2013).
Yu, F. P. S. et al. Chronic lung injury and impaired pulmonary function in a mouse model of acid ceramidase deficiency. Am. J. Physiol. Lung Cell Mol. Physiol. 314, L406–L420 (2018).
Yu, F. P. S. et al. Hepatic pathology and altered gene transcription in a murine model of acid ceramidase deficiency. Lab Invest. 99, 1572–1592 (2019).
Dworski, S. et al. Markedly perturbed hematopoiesis in acid ceramidase deficient mice. Haematologica 100, e162–e165 (2015).
Sikora, J. et al. Acid ceramidase deficiency in mice results in a broad range of central nervous system abnormalities. Am. J. Pathol. 187, 864–883 (2017).
Yu, F. P. S. et al. Acid ceramidase deficiency in mice leads to severe ocular pathology and visual impairment. Am. J. Pathol. 189, 320–338 (2019).
Rybova, J., Kuchar, L., Sikora, J., McKillop, W. M. & Medin, J. A. Skin inflammation and impaired adipogenesis in a mouse model of acid ceramidase deficiency. J. Inherit. Metab. Dis. 45, 1175–1190 (2022).
Dyment, D. A., Bennett, S. A. L., Medin, J. A. & Levade, T. In GeneReviews((R)) (eds M. P. Adam et al.) (2018).
Yu, F. P. S., Dworski, S. & Medin, J. A. Deletion of MCP-1 impedes pathogenesis of acid ceramidase deficiency. Sci. Rep. 8, 1808–1808 (2018).
Beckmann, N. et al. Pathological manifestations of Farber disease in a new mouse model. Biol. Chem. 399, 1183–1202 (2018).
Nagy, A. et al. Dissecting the role of N-myc in development using a single targeting vector to generate a series of alleles. Curr. Biol. 8, 661–664 (1998).
Meyers, E. N., Lewandoski, M. & Martin, G. R. An Fgf8 mutant allelic series generated by Cre- and Flp-mediated recombination. Nat. Genet. 18, 136–141 (1998).
Hayashi, S., Tenzen, T. & McMahon, A. P. Maternal inheritance of Cre activity in a Sox2Cre deleter strain. genesis 37, 51–53 (2003).
Li, Y. et al. Genetic ablation of acid ceramidase in Krabbe disease confirms the psychosine hypothesis and identifies a new therapeutic target. Proc. Natl. Acad. Sci. USA 116, 20097–20103 (2019).
Dworski, S. et al. Acid Ceramidase Deficiency is characterized by a unique plasma cytokine and ceramide profile that is altered by therapy. Biochimica et. Biophysica Acta (BBA) – Mol. Basis Dis. 1863, 386–394 (2017).
Sturm, R. M. & Cheng, E. Y. Bladder wall thickness in the assessment of neurogenic bladder: a translational discussion of current clinical applications. Ann. Transl. Med. 4, 32–32 (2016).
Öztürk Akcora, B., Vassilios Gabriël, A., Ortiz-Perez, A. & Bansal, R. Pharmacological inhibition of STAT3 pathway ameliorates acute liver injury in vivo via inactivation of inflammatory macrophages and hepatic stellate cells. FASEB BioAdv. 2, 77–89 (2020).
Samoriski, G. M. & Applegate, C. D. Repeated generalized seizures induce time-dependent changes in the behavioral seizure response independent of continued seizure induction. J. Neurosci. 17, 5581–5590 (1997).
Ferland, R. J. The repeated flurothyl seizure model in mice. Bio. Protoc. 7 https://doi.org/10.21769/BioProtoc.2309 (2017).
Sarna, J. R. et al. Patterned Purkinje cell degeneration in mouse models of Niemann-Pick type C disease. J. Comp. Neurol. 456, 279–291 (2003).
Sarna, J., Miranda, S. R. P., Schuchman, E. H. & Hawkes, R. Patterned cerebellar Purkinje cell death in a transgenic mouse model of Niemann Pick type A/B disease. Eur. J. Neurosci. 13, 1873–1880 (2001).
Praggastis, M. et al. A murine Niemann-Pick C1 I1061T knock-in model recapitulates the pathological features of the most prevalent human disease allele. J. Neurosci. 35, 8091–8106 (2015).
Chen, Y., Liu, Y., Sullards, M. C. & Merrill, A. H. An introduction to sphingolipid metabolism and analysis by new technologies. NeuroMolecular Med. 12, 306–319 (2010).
O’Brien, J. S. & Sampson, E. L. Lipid composition of the normal human brain: gray matter, white matter, and myelin. J. Lipid Res. 6, 537–544 (1965).
Fitzner, D. et al. Cell-type- and brain-region-resolved mouse brain lipidome. Cell Rep. 32, 108132 (2020).
Novakova, L. et al. Sulfatide isoform pattern in cerebrospinal fluid discriminates progressive MS from relapsing-remitting MS. J. Neurochem. 146, 322–332 (2018).
Nijeholt, G. J. et al. Post-mortem high-resolution MRI of the spinal cord in multiple sclerosis: a correlative study with conventional MRI, histopathology and clinical phenotype. Brain 124, 154–166 (2001).
Calabrese, E. et al. Postmortem diffusion MRI of the entire human spinal cord at microscopic resolution. Neuroimage Clin. 18, 963–971 (2018).
You, Y. et al. Demyelination precedes axonal loss in the transneuronal spread of human neurodegenerative disease. Brain 142, 426–442 (2019).
Kornek, B. et al. Multiple sclerosis and chronic autoimmune encephalomyelitis: a comparative quantitative study of axonal injury in active, inactive, and remyelinated lesions. Am. J. Pathol. 157, 267–276 (2000).
Mar, S. & Noetzel, M. Axonal damage in leukodystrophies. Pediatr. Neurol. 42, 239–242 (2010).
Irvine, K. A. & Blakemore, W. F. Remyelination protects axons from demyelination-associated axon degeneration. Brain 131, 1464–1477 (2008).
Lecommandeur, E. et al. Decrease in myelin-associated lipids precedes neuronal loss and glial activation in the CNS of the sandhoff mouse as determined by metabolomics. Metabolites 11, 18 (2020).
Mei, F. et al. Accelerated remyelination during inflammatory demyelination prevents axonal loss and improves functional recovery. Elife 5, e18246 (2016).
Wang, X. et al. Macrophages in spinal cord injury: phenotypic and functional change from exposure to myelin debris. Glia 63, 635–651 (2015).
Dorrier, C. E. et al. CNS fibroblasts form a fibrotic scar in response to immune cell infiltration. Nat. Neurosci. 24, 234–244 (2021).
D’Ambrosi, N. & Apolloni, S. Fibrotic scar in neurodegenerative diseases. Front Immunol. 11, 1394–1394 (2020).
Shibata, M. et al. Caspases determine the vulnerability of oligodendrocytes in the ischemic brain. J. Clin. Invest 106, 643–653 (2000).
Dominguez, E., Rivat, C., Pommier, B., Mauborgne, A. & Pohl, M. JAK/STAT3 pathway is activated in spinal cord microglia after peripheral nerve injury and contributes to neuropathic pain development in rat. J. Neurochem. 107, 50–60 (2008).
Herrmann, J. E. et al. STAT3 is a critical regulator of astrogliosis and scar formation after spinal cord injury. J. Neurosci. 28, 7231–7243 (2008).
Bley, A. et al. The natural history of Canavan disease: 23 new cases and comparison with patients from literature. Orphanet J. Rare Dis. 16, 227–227 (2021).
Sonnino, S. & Chigorno, V. Ganglioside molecular species containing C18- and C20-sphingosine in mammalian nervous tissues and neuronal cell cultures. Biochimica et. Biophysica Acta (BBA) – Rev. Biomembranes 1469, 63–77 (2000).
Vutukuri, R. et al. S1P d20:1, an endogenous modulator of S1P d18:1/S1P2-dependent signaling. FASEB J. 34, 3932–3942 (2020).
Tredici, G., Buccellato, F. R., Cavaletti, G. & Scalabrino, G. Subacute combined degeneration in totally gastrectomized rats: an ultrastructural study. J. Submicrosc. Cytol. Pathol. 30, 165–173 (1998).
Sun, H. Y., Lee, J. W., Park, K. S., Wi, J. Y. & Kang, H. S. Spine MR imaging features of subacute combined degeneration patients. Eur. Spine J. 23, 1052–1058 (2014).
Qudsiya, Z. & De Jesus, O. In StatPearls (2021).
Wolffenbuttel, B. H. R., Wouters, H. J. C. M., Heiner-Fokkema, M. R. & van der Klauw, M. M. The Many Faces of Cobalamin (Vitamin B(12)) Deficiency. Mayo Clin. Proc. Innov. Qual. Outcomes 3, 200–214 (2019).
Nielsen, M. J., Rasmussen, M. R., Andersen, C. B. F., Nexø, E. & Moestrup, S. K. Vitamin B12 transport from food to the body’s cells—a sophisticated, multistep pathway. Nat. Rev. Gastroenterol. Hepatol. 9, 345–354 (2012).
Hannibal, L. et al. Hampered Vitamin B12 metabolism in Gaucher disease. J. Inborn Errors Metab. Screen. 5, 2326409817692359 (2017).
Savage, D. G., Lindenbaum, J., Stabler, S. P. & Allen, R. H. Sensitivity of serum methylmalonic acid and total homocysteine determinations for diagnosing cobalamin and folate deficiencies. Am. J. Med. 96, 239–246 (1994).
Misra, U. K., Kalita, J., Kumar, G. & Kapoor, R. Bladder dysfunction in subacute combined degeneration. J. Neurol. 255, 1881–1888 (2008).
McCombe, P. A., Gordon, T. P. & Jackson, M. W. Bladder dysfunction in multiple sclerosis. Expert Rev. Neurotherapeutics 9, 331–340 (2009).
Taweel, W. A. & Seyam, R. Neurogenic bladder in spinal cord injury patients. Res Rep. Urol. 7, 85–99 (2015).
Sato, S. & Hughes, R. C. Regulation of secretion and surface expression of Mac-2, a galactoside-binding protein of macrophages. J. Biol. Chem. 269, 4424–4430 (1994).
Reichert, F. & Rotshenker, S. Galectin-3 (MAC-2) Controls microglia phenotype whether amoeboid and phagocytic or branched and non-phagocytic by regulating the cytoskeleton. Front. Cel. Neurosci. 13, https://doi.org/10.3389/fncel.2019.00090 (2019).
Bonsack, F. & Sukumari-Ramesh, S. Differential cellular expression of galectin−1 and galectin-3 after intracerebral hemorrhage. Front Cell Neurosci. 13, 157 (2019).
Rotshenker, S. The role of Galectin-3/MAC-2 in the activation of the innate-immune function of phagocytosis in microglia in injury and disease. J. Mol. Neurosci. 39, 99–103 (2009).
Morizawa, Y. M. et al. Reactive astrocytes function as phagocytes after brain ischemia via ABCA1-mediated pathway. Nat. Commun. 8, 28 (2017).
Ajuebor, M. N. et al. Endogenous monocyte chemoattractant protein-1 recruits monocytes in the zymosan peritonitis model. J. Leukoc. Biol. 63, 108–116 (1998).
Lampron, A. et al. Inefficient clearance of myelin debris by microglia impairs remyelinating processes. J. Exp. Med. 212, 481–495 (2015).
Ferreira, C. R. & Gahl, W. A. Lysosomal storage diseases. Transl. Sci. Rare Dis. 2, 1–71 (2017).
Johnson, T. B. et al. Therapeutic landscape for Batten disease: current treatments and future prospects. Nat. Rev. Neurol. 15, 161–178 (2019).
Vitner, E. B., Farfel-Becker, T., Eilam, R., Biton, I. & Futerman, A. H. Contribution of brain inflammation to neuronal cell death in neuronopathic forms of Gaucher’s disease. Brain 135, 1724–1735 (2012).
Gan, J. J. et al. Acid ceramidase deficiency associated with spinal muscular atrophy with progressive myoclonic epilepsy. Neuromuscul. Disord. 25, 959–963 (2015).
Adang, L. A. et al. Revised consensus statement on the preventive and symptomatic care of patients with leukodystrophies. Mol. Genet. Metab. 122, 18–32 (2017).
Kobayashi, D. T. et al. SMA-MAP: a plasma protein panel for spinal muscular atrophy. PLoS One 8, e60113–e60113 (2013).
Eberhardt, O. & Topka, H. Myoclonic disorders. Brain Sci. 7, 103 (2017).
Souza, A. D. & Moloi, M. W. Involuntary movements due to vitamin B12 deficiency. Neurological Res. 36, 1121–1128 (2014).
Alroughani, R. A., Ahmed, S. F., Khan, R. A. & Al-Hashel, J. Y. Spinal segmental myoclonus as an unusual presentation of multiple sclerosis. BMC Neurol. 15, 15–15 (2015).
Marrie, R. A. et al. Unusual imaging findings in progressive myoclonus epilepsy. Epilepsia 42, 430–432 (2001).
Tian, W. T. et al. Progressive myoclonus epilepsy without renal failure in a Chinese family with a novel mutation in SCARB2 gene and literature review. Seizure 57, 80–86 (2018).
Hagen, M. C. et al. Encephalopathy with neuroserpin inclusion bodies presenting as progressive myoclonus epilepsy and associated with a novel mutation in the Proteinase Inhibitor 12 gene. Brain Pathol. 21, 575–582 (2011).
Pant, D. C. et al. Loss of the sphingolipid desaturase DEGS1 causes hypomyelinating leukodystrophy. J. Clin. Investig. 129, 1240–1256 (2019).
Karsai, G. et al. DEGS1-associated aberrant sphingolipid metabolism impairs nervous system function in humans. J. Clin. Investig. 129, 1229–1239 (2019).
Dolgin, V. et al. DEGS1 variant causes neurological disorder. Eur. J. Hum. Genet. 27, 1668–1676 (2019).
Edvardson, S. et al. Deficiency of the alkaline ceramidase ACER3 manifests in early childhood by progressive leukodystrophy. J. Med Genet 53, 389–396 (2016).
Papandrea, D., Anderson, T. M., Herron, B. J. & Ferland, R. J. Dissociation of seizure traits in inbred strains of mice using the flurothyl kindling model of epileptogenesis. Exp. Neurol. 215, 60–68 (2009).
Engel, J. Seizures and epilepsy. Second edition. edn, (Oxford University Press, 2013).
Caviness, J. N. & Brown, P. Myoclonus: current concepts and recent advances. Lancet Neurol. 3, 598–607 (2004).
Jana, A. & Pahan, K. Oxidative stress kills human primary oligodendrocytes via neutral sphingomyelinase: implications for multiple sclerosis. J. Neuroimmune Pharm. 2, 184–193 (2007).
Lee, J.-T. et al. Amyloid-beta peptide induces oligodendrocyte death by activating the neutral sphingomyelinase-ceramide pathway. J. Cell Biol. 164, 123–131 (2004).
Chami, M. et al. Acid sphingomyelinase deficiency enhances myelin repair after acute and chronic demyelination. PLoS One 12, e0178622–e0178622 (2017).
van Doorn, R. et al. Fingolimod attenuates ceramide-induced blood–brain barrier dysfunction in multiple sclerosis by targeting reactive astrocytes. Acta Neuropathologica 124, 397–410 (2012).
Davis, D. L. et al. Dynamics of sphingolipids and the serine palmitoyltransferase complex in rat oligodendrocytes during myelination. J. lipid Res. 61, 505–522 (2020).
Yu, Z. F. et al. Pivotal role for acidic sphingomyelinase in cerebral ischemia-induced ceramide and cytokine production, and neuronal apoptosis. J. Mol. Neurosci. 15, 85–97 (2000).
Fischer, H. et al. Ceramide as a TLR4 agonist; a putative signalling intermediate between sphingolipid receptors for microbial ligands and TLR4. Cell. Microbiol. 9, 1239–1251 (2007).
Church, J. S., Kigerl, K. A., Lerch, J. K., Popovich, P. G. & McTigue, D. M. TLR4 Deficiency Impairs Oligodendrocyte Formation in the Injured Spinal Cord. J. Neurosci. 36, 6352–6364 (2016).
Mohassel, P. et al. Childhood amyotrophic lateral sclerosis caused by excess sphingolipid synthesis. Nat. Med. 27, 1197–1204 (2021).
Cutler, R. G., Pedersen, W. A., Camandola, S., Rothstein, J. D. & Mattson, M. P. Evidence that accumulation of ceramides and cholesterol esters mediates oxidative stress–induced death of motor neurons in amyotrophic lateral sclerosis. Ann. Neurol. 52, 448–457 (2002).
Davis, D. L., Gable, K., Suemitsu, J., Dunn, T. M. & Wattenberg, B. W. The ORMDL/Orm-serine palmitoyltransferase (SPT) complex is directly regulated by ceramide: Reconstitution of SPT regulation in isolated membranes. J. Biol. Chem. 294, 5146–5156 (2019).
Clarke, B. A. et al. The Ormdl genes regulate the sphingolipid synthesis pathway to ensure proper myelination and neurologic function in mice. Elife 8, e51067 (2019).
Momoi, T., Ben-Yoseph, Y. & Nadler, H. L. Substrate-specificities of acid and alkaline ceramidases in fibroblasts from patients with Farber disease and controls. Biochem J. 205, 419–425 (1982).
Sugita, M., Williams, M., Dulaney, J. T. & Moser, H. W. Ceramidase and ceramide synthesis in human kidney and cerebellum. Description of a new alkaline ceramidase. Biochim Biophys. Acta 398, 125–131 (1975).
Krishnamurthy, K., Dasgupta, S. & Bieberich, E. Development and characterization of a novel anti-ceramide antibody. J. Lipid Res. 48, 968–975 (2007).
Cowart, L. A., Szulc, Z., Bielawska, A. & Hannun, Y. A. Structural determinants of sphingolipid recognition by commercially available anti-ceramide antibodies. J. Lipid Res 43, 2042–2048 (2002).
Andreyev, A. Y. et al. Subcellular organelle lipidomics in TLR-4-activated macrophages. J. lipid Res. 51, 2785–2797 (2010).
Grösch, S., Schiffmann, S. & Geisslinger, G. Chain length-specific properties of ceramides. Prog. Lipid Res. 51, 50–62 (2012).
Cruickshanks, N. et al. Differential regulation of autophagy and cell viability by ceramide species. Cancer Biol. Ther. 16, 733–742 (2015).
Muralidharan, S. et al. A reference map of sphingolipids in murine tissues. Cell Rep. 35, 109250 (2021).
Olsen, A. S. B. & Færgeman, N. J. Sphingolipids: membrane microdomains in brain development, function and neurological diseases. Open Biol. 7, 170069 (2017).
Mayo, L. et al. Regulation of astrocyte activation by glycolipids drives chronic CNS inflammation. Nat. Med. 20, 1147–1156 (2014).
Taguchi, A. et al. A symptomatic Fabry disease mouse model generated by inducing globotriaosylceramide synthesis. Biochem J. 456, 373–383 (2013).
Shen, J. S. et al. Blocking hyperactive androgen receptor signaling ameliorates cardiac and renal hypertrophy in Fabry mice. Hum. Mol. Genet 24, 3181–3191 (2015).
Hirahara, Y. et al. Sulfatide species with various fatty acid chains in oligodendrocytes at different developmental stages determined by imaging mass spectrometry. J. Neurochem. 140, 435–450 (2017).
Bhat, O. M. et al. Arterial Medial Calcification through Enhanced small Extracellular Vesicle Release in Smooth Muscle-Specific Asah1 Gene Knockout Mice. Sci. Rep. 10, 1645 (2020).
Bedia, C., Camacho, L., Abad, J. L., Fabrias, G. & Levade, T. A simple fluorogenic method for determination of acid ceramidase activity and diagnosis of Farber disease. J. Lipid Res. 51, 3542–3547 (2010).
Carson, F. L. & Cappellano, C. H. Histotechnology. (ASCP Press, 2009).
Schneider, C. A., Rasband, W. S. & Eliceiri, K. W. NIH Image to ImageJ: 25 years of image analysis. Nat. Methods 9, 671–675 (2012).
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265–275 (1951).
Saville, J. T. & Fuller, M. Sphingolipid dyshomeostasis in the brain of the mouse model of mucopolysaccharidosis type IIIA. Mol. Genet. Metab. 129, 111–116 (2020).
Saville, J. T., Thai, H. N., Lehmann, R. J., Derrick-Roberts, A. L. & Fuller, M. Subregional brain distribution of simple and complex glycosphingolipids in the mucopolysaccharidosis type I (Hurler syndrome) mouse: impact of diet. J. Neurochem 141, 287–295 (2017).
Tinklenberg, J. et al. Treatment with ActRIIB-mFc produces myofiber growth and improves lifespan in the Acta1 H40Y murine model of nemaline myopathy. Am. J. Pathol. 186, 1568–1581 (2016).
Ravenscroft, G. et al. Mouse models of dominant ACTA1 disease recapitulate human disease and provide insight into therapies. Brain 134, 1101–1115 (2011).
Chaplan, S. R., Bach, F. W., Pogrel, J. W., Chung, J. M. & Yaksh, T. L. Quantitative assessment of tactile allodynia in the rat paw. J. Neurosci. Methods 53, 55–63 (1994).
Garrison, S. R., Kramer, A. A., Gerges, N. Z., Hillery, C. A. & Stucky, C. L. Sickle cell mice exhibit mechanical allodynia and enhanced responsiveness in light touch cutaneous mechanoreceptors. Mol. Pain. 8, 62–62 (2012).
Avants, B. B. et al. The Insight ToolKit image registration framework. Front Neuroinform 8, 44 (2014).