Increased ceramide in brains with Alzheimer's and other neurodegenerative diseases
Open accessAbstract
Ceramide has been suggested to participate in the neuronal cell death that leads to Alzheimer's disease (AD), but its role is not yet well-understood. We compared the levels of six ceramide subspecies, which differ in the length of their fatty acid moieties, in brains from patients who suffered from AD, other neuropathological disorders, or both. We found elevated levels of Cer16, Cer18, Cer20, and Cer24 in brains from patients with any of the tested neural defects. Moreover, ceramide levels were highest in patients with more than one neuropathologic abnormality. Interestingly, the range of values was higher among brains with neural defects than in controls, suggesting that the regulation of ceramide synthesis is normally under tight control, and that this tight control may be lost during neurodegeneration. These changes, however, did not alter the ratio between the tested ceramide species. To explore the mechanisms underlying this dysregulation, we evaluated the expression of four genes connected to ceramide metabolism: ASMase, NSMase 2, GALC, and UGCG. The patterns of gene expression were complex, but overall, ASMase, NSMase 2, and GALC were upregulated in specimens from patients with neuropathologic abnormalities in comparison with age-matched controls. Such findings suggest these genes as attractive candidates both for diagnostic purposes and for intervening in neurodegenerative processes.
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
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?
Glucosylceramide synthesis is downregulated in AD brains.
“a process downregulated in AD brains34.”
From APOE4 to APOE2 allelic switching in mice improves Alzheimer’s disease-related metabolic signatures, neuropathology and cognition (2025) · cites this paper as [34]
The Discussion reports downregulated expression of UGCG, the enzyme that synthesizes glucosylceramide from ceramide, and cites lower UGCG activity in AD frontal cortex. But the Results report variable UGCG expression across the paper’s AD samples, including four with higher expression; the paper does not directly establish that glucosylceramide synthesis is generally downregulated in AD brains. (LLM, conf=0.84)
Experimental — accuracy not yet measuredIncreased levels of Cer16, Cer18, Cer20, and Cer24 are found in the brains of patients with Alzheimer's disease.
“Specifically, increased levels of Cer16, Cer18, Cer20, and Cer24 are found in the brains from patients with AD. 26”
From Protective mechanisms against Alzheimer's disease in APOE3‐Christchurch homozygous astrocytes (2025) · cites this paper as [26]
Ceramide is increased in human brains as a function of age and in Alzheimer's disease, suggesting that a common mechanism could drive age-related early endosome defects in neurons and the RPE.
“Recent studies show that ceramide is increased in human brains as a function of age (Park et al., 2018) and in Alzheimer’s disease (Filippov et al., 2012), suggesting that a common mechanism could drive age-related early endosome defects in neurons and the RPE.”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Filippov 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.
Cites
Cutler, R. G., Kelly, J., Storie, K., Pedersen, W. A., Tammara, A., Hatanpaa, K. J., Troncoso, J. C., & Mattson, M. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305799101 · Cited by 1,135 · see citing works
Ceramide in apoptosis: an overview and current perspectives
Pettus, B. J., Chalfant, C. E., & Hannun, Y. A. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(02)00331-1 · Cited by 788 · see citing works
Evidence for a membrane defect in Alzheimer disease brain.
Nitsch, R. M., Blusztajn, J. K., Pittas, A. G., Slack, B. E., Growdon, J. H., & Wurtman, R. J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.5.1671 · Cited by 536 · see citing works
Deregulation of sphingolipid metabolism in Alzheimer’s disease
He, X., Huang, Y., Li, B., Gong, C.-X., & Schuchman, E. H. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.05.010 · Cited by 516 · see citing works
Characterization of Ceramide Synthase 2
Laviad, E. L., Albee, L. D., Pankova-Kholmyansky, I., Epstein, S., Park, H. J., Merrill, A. H., & Futerman, A. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707386200 · Cited by 468 · see citing works
Hofmann, K., Tomiuk, S., Wolff, G., & Stoffel, W. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.11.5895 · Cited by 309 · see citing works
Imgrund, S., Hartmann, D., Farwanah, H., Eckhardt, M., Sandhoff, R., Degen, J., Gieselmann, V., Sandhoff, K., & Willecke, K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.031971 · Cited by 299 · see citing works
Roles and regulation of secretory and lysosomal acid sphingomyelinase
Jenkins, R. W., Canals, D., & Hannun, Y. A. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.01.026 · Cited by 276 · see citing works
Katsel, P., Li, C., & Haroutunian, V. H. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9297-x · Cited by 240 · see citing works
Jana, A., Hogan, E. L., & Pahan, K. (2009) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2008.12.010 · Cited by 233 · see citing works
Ceramide synthases 2, 5, and 6 confer distinct roles in radiation-induced apoptosis in HeLa cells
Mesicek, J., Lee, H., Feldman, T., Jiang, X., Skobeleva, A., Berdyshev, E. V., Haimovitz‐Friedman, A., FUKS, Z. Y., & Kolesnick, R. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.04.006 · Cited by 229 · see citing works
Jennemann, R., Sandhoff, R., Wang, S., Kiss, É., Gretz, N., Zuliani, C., Martín-Villalba, A., Jäger, R., Schorle, H., Kenzelmann, M., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500893102 · Cited by 179 · see citing works
Mammalian Neutral Sphingomyelinases: Regulation and Roles in Cell Signaling Responses
Wu, B. X., Clarke, C. J., & Hannun, Y. A. (2010) · NeuroMolecular Medicine · doi:10.1007/s12017-010-8120-z · Cited by 151 · see citing works
Sphingolipid metabolism in neural cells
van Echten‐Deckert, G., & Herget, T. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.06.009 · Cited by 144 · see citing works
High activity of acid sphingomyelinase in major depression
Kornhuber, J., Medlin, A., Bleich, S., Jendrossek, V., Henkel, A. W., Wiltfang, J., & Gulbins, E. (2005) · Journal of Neural Transmission · doi:10.1007/s00702-005-0374-5 · Cited by 143 · see citing works
The Liver-Brain Axis of Alcohol-Mediated Neurodegeneration: Role of Toxic Lipids
de la Monte, S. M., Longato, L., Tong, M., DeNucci, S. M., & Wands, J. R. (2009) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph6072055 · Cited by 137 · see citing works
Sphingolipid metabolites in neural signalling and function
Colombaioni, L., & Garcia‐Gil, M. (2004) · Brain Research Reviews · doi:10.1016/j.brainresrev.2004.07.014 · Cited by 119 · see citing works
Dementia syndromes: evaluation and treatment
Scott, K. R., & Barrett, A. M. (2007) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.7.4.407 · Cited by 107 · see citing works
Kasumov, T., Huang, H., Chung, Y., Zhang, R., McCullough, A. J., & Kirwan, J. P. (2010) · Analytical Biochemistry · doi:10.1016/j.ab.2010.02.023 · Cited by 98 · see citing works
Zimmermann, C., Ginis, I., Furuya, K., Klimanis, D., Ruetzler, C. A., Spatz, M., & Hallenbeck, J. M. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02028-5 · Cited by 92 · see citing works
Marks, N., Berg, M. J., Saito, M., & Saito, M. (2007) · Brain Research · doi:10.1016/j.brainres.2007.10.066 · Cited by 41 · see citing works
Haynes, T.-A. S., Duerksen-Hughes, P. J., Filippova, M., Filippov, V. A., & Zhang, K. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.03.045 · Cited by 15 · see citing works
Self-citationZhang, K., Haynes, T.-A. S., Filippova, M., Filippov, V. A., & Duerksen-Hughes, P. J. (2011) · Analytical Methods · doi:10.1039/c1ay05022b · Cited by 10 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Lipids and Alzheimer’s Disease
Kao, Y.-C., Ho, P.-C., Tu, Y.-K., Jou, I.-M., & Tsai, K.-J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041505 · Cited by 485 · see citing works
Yin, F. (2023) · The FEBS Journal · doi:10.1111/febs.16344 · Cited by 441 · see citing works
The cell biology of the retinal pigment epithelium
Lakkaraju, A., Umapathy, A., Tan, L. X., Daniele, L., Philp, N. J., Boesze-Battaglia, K., & Williams, D. S. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100846 · Cited by 422 · see citing works
Involvement of Lipids in Alzheimer’s Disease Pathology and Potential Therapies
Chew, H., Solomon, V. A., & Fonteh, A. N. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00598 · Cited by 353 · see citing works
Repairing mitochondrial dysfunction in disease
Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337 · see citing works
Sphingolipids: membrane microdomains in brain development, function and neurological diseases
Olsen, A. S. B., & Færgeman, N. J. (2017) · Open Biology · doi:10.1098/rsob.170069 · Cited by 312 · see citing works
Circulating microRNAs as potential biomarkers for psychiatric and neurodegenerative disorders
van den Berg, M. M. J., Krauskopf, J., Ramaekers, J. G., Kleinjans, J. C. S., Prickaerts, J., & Briedé, J. J. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101732 · Cited by 253 · see citing works
Dinkins, M. B., Enasko, J., Hernandez, C. M., Wang, G., Kong, J., Helwa, I., Liu, Y., Terry, A. V., & Bieberich, E. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.1429-16.2016 · Cited by 243 · see citing works
Jazvinšćak Jembrek, M., Hof, P. R., & Šimić, G. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/346783 · Cited by 244 · see citing works
Pera, M., Larrea, D., Guardia‐Laguarta, C., Montesinos, J., VELASCO, K. R., Agrawal, R. R., Xu, Y., Chan, R., Paolo, G. D., Mehler, M. F., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796797 · Cited by 235 · see citing works
Ceramides as Novel Disease Biomarkers
Kurz, J., Parnham, M. J., Geißlinger, G., & Schiffmann, S. (2018) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2018.10.009 · Cited by 189 · see citing works
Lipid metabolism and storage in neuroglia: role in brain development and neurodegenerative diseases
Yang, D., Wang, X., Zhang, L., Fang, Y., Zheng, Q., Liu, X., Yu, W., Chen, S., Ying, J., & Hua, F. (2022) · Cell & Bioscience · doi:10.1186/s13578-022-00828-0 · Cited by 179 · see citing works
Klosinski, L. P., Yao, J., Yin, F., Fonteh, A. N., Harrington, M. G., Christensen, T. A., Trushina, E. V., & Brinton, R. D. (2015) · EBioMedicine · doi:10.1016/j.ebiom.2015.11.002 · Cited by 164 · see citing works
Loss of the neuroprotective factor sphingosine 1-phosphate early in Alzheimer’s disease pathogenesis
Couttas, T. A., Kain, N., Daniels, B., Lim, X. Y., Shepherd, C., Kril, J., Pickford, R., Li, H., Garner, B., & Don, A. S. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-9 · Cited by 161 · see citing works
Secretory sphingomyelinase in health and disease
Kornhuber, J., Rhein, C., Müller, C. P., & Mühle, C. (2015) · Biological Chemistry · doi:10.1515/hsz-2015-0109 · Cited by 145 · see citing works
Role of Ceramidases in Sphingolipid Metabolism and Human Diseases
Parveen, F., Bender, D. A., Law, S., Mishra, V. K., Chen, C.-C., & Ke, L. (2019) · Cells · doi:10.3390/cells8121573 · Cited by 145 · see citing works
Fingolimod for the treatment of neurological diseases—state of play and future perspectives
Brunkhorst, R., Vutukuri, R., & Pfeilschifter, W. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00283 · Cited by 142 · see citing works
Lipidomics in translational research and the clinical significance of lipid-based biomarkers
Stephenson, D., Hoeferlin, L. A., & Chalfant, C. E. (2017) · Translational research · doi:10.1016/j.trsl.2017.06.006 · Cited by 136 · see citing works
Role of Sphingolipid Metabolism in Neurodegeneration
Alaamery, M., Albesher, N., Aljawini, N., Alsuwailm, M., Massadeh, S., Wheeler, M. A., Chao, C., & Quintana, F. J. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15044 · Cited by 129 · see citing works
The pleiotropic effects of omega-3 docosahexaenoic acid on the hallmarks of Alzheimer's disease
Belkouch, M., Hachem, M., Elgot, A., Van, A. L., Picq, M., Guichardant, M., Lagarde, M., & Bernoud‐Hubac, N. (2016) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.03.002 · Cited by 128 · see citing works
Sepsis-Associated Encephalopathy: The Blood–Brain Barrier and the Sphingolipid Rheostat
Kuperberg, S. J., & Wadgaonkar, R. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00597 · Cited by 125 · see citing works
A plural role for lipids in motor neuron diseases: energy, signaling and structure
Schmitt, F., Hussain, G., Dupuis, L., Loeffler, J., & Henriques, A. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00025 · Cited by 120 · see citing works
Asle‐Rousta, M., Kolahdooz, Z., Oryan, S., Ahmadiani, A., & Dargahi, L. (2013) · Journal of Molecular Neuroscience · doi:10.1007/s12031-013-9979-6 · Cited by 112 · see citing works
Grimm, M. O. W., Michaelson, D. M., & Hartmann, T. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r076331 · Cited by 110 · see citing works
APP Function and Lipids: A Bidirectional Link
Grimm, M. O. W., Mett, J., Grimm, H. S., & Hartmann, T. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00063 · Cited by 104 · see citing works
The interactions of p53 with tau and Aß as potential therapeutic targets for Alzheimer’s disease
Jembrek, M. J., Slade, N., Hof, P. R., & Šimić, G. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.05.001 · Cited by 99 · see citing works
Kim, M. G., Nevado‐Holgado, A. J., Whiley, L., Snowden, S. G., Soininen, H. S., Kłoszewska, I., Mecocci, P., Tsolaki, M., Vellas, B. J., Thambisetty, M., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160645 · Cited by 97 · see citing works
Microglia modulate stable wakefulness via the thalamic reticular nucleus in mice
Liu, H., Wang, X., Chen, L., Chen, L., Tsirka, S. E., Ge, S., & Xiong, Q. (2021) · Nature Communications · doi:10.1038/s41467-021-24915-x · Cited by 95 · see citing works
Disentangling Mitochondria in Alzheimer’s Disease
Johri, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111520 · Cited by 96 · see citing works
Ceramides and depression: A systematic review
Dinoff, A., Herrmann, N., & Lanctôt, K. L. (2017) · Journal of Affective Disorders · doi:10.1016/j.jad.2017.02.008 · Cited by 95 · see citing works
Neurodegenerative Pathways in Alzheimer’s Disease: A Review
Ramachandran, A. K., Das, S., Joseph, A., Shenoy, G. G., Alex, A. T., & Mudgal, J. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200807130637 · Cited by 94 · see citing works
Jianming, W., & Ling, L. (2016) · The Journal of Biomedical Research · doi:10.7555/jbr.30.20150131 · Cited by 87 · see citing works
Sphingolipids in Alzheimer's disease, how can we target them?
Crivelli, S. M., Giovagnoni, C., Visseren, L., Scheithauer, A.-L., de Wit, N. M., den Hoedt, S., Losen, M. H., Mulder, M. T., Walter, J., de Vries, H. E., et al. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2019.12.003 · Cited by 85 · see citing works
The Impact of Cholesterol, DHA, and Sphingolipids on Alzheimer’s Disease
Grimm, M. O. W., Zimmer, V. C., Lehmann, J., Grimm, H. S., & Hartmann, T. (2013) · BioMed Research International · doi:10.1155/2013/814390 · Cited by 81 · see citing works
Defective Sphingosine-1-phosphate metabolism is a druggable target in Huntington’s disease
Pardo, A. D., Amico, E., Basit, A., Armirotti, A., Joshi, P. K., Neely, M. D., Vuono, R., Castaldo, S., Digilio, A. F., Scalabrì, F., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-05709-y · Cited by 81 · see citing works
Kaur, G., Tan, L. X., Rathnasamy, G., La Cunza, N., Germer, C. J., Toops, K. A., Fernandes, M., Blenkinsop, T. A., & Lakkaraju, A. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1805039115 · Cited by 79 · see citing works
Li, H., Tan, Y., Cheng, X. M., Zhang, Z., Huang, J., Hui, S., Zhu, L., Liu, Y., Zhao, D. S., Liu, Z., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.990307 · Cited by 77 · see citing works
Cardiolipin promotes electron transport between ubiquinone and complex I to rescue PINK1 deficiency
Vos, M. H., Geens, A., Böhm, C., Deaulmerie, L., Swerts, J., Rossi, M., Craessaerts, K., Leites, E. P., Seibler, P., Raković, A., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201511044 · Cited by 77 · see citing works
Integrative metabolomics science in Alzheimer’s disease: Relevance and future perspectives
Lista, S., González‐Domínguez, R., López‐Ortiz, S., González‐Domínguez, Á., Menéndez, H., Martín-Hernández, J., Lucía, A., Emanuele, E., Centonze, D., Imbimbo, B. P., et al. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101987 · Cited by 75 · see citing works
Sphingolipid Metabolism: A New Therapeutic Opportunity for Brain Degenerative Disorders
Pardo, A. D., & Maglione, V. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00249 · Cited by 73 · see citing works
Stojakovic, A., Trushin, S., Sheu, A., Khalili, L., Chang, S.-Y., Li, X., Christensen, T., Salisbury, J. L., Geroux, R. E., Gateno, B., et al. (2021) · Communications Biology · doi:10.1038/s42003-020-01584-y · Cited by 72 · see citing works
Melchiorri, D., Merlo, S., Micallef, B., Borg, J.-J., & Dráfi, F. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1196413 · Cited by 72 · see citing works
Couttas, T. A., Kain, N., Tran, C., Chatterton, Z., Kwok, J. B., & Don, A. S. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171054 · Cited by 70 · see citing works
Lipids in Pathophysiology and Development of the Membrane Lipid Therapy: New Bioactive Lipids
Torres, M., Parets, S., Fernández-Díaz, J., Beteta-Göbel, R., Rodríguez-Lorca, R., Román, R., Lladó, V., Rosselló, C. A., Fernández‐García, P., & Escribá, P. V. (2021) · Membranes · doi:10.3390/membranes11120919 · Cited by 70 · see citing works
Tan, L. X., Germer, C. J., Cunza, N. L., & Lakkaraju, A. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101781 · Cited by 69 · see citing works
Deciphering cellular transcriptional alterations in Alzheimer’s disease brains
Wang, X., Allen, M., Li, S., Quicksall, Z., Patel, T., Carnwath, T., Reddy, J. S., Carrasquillo, M. M., Lincoln, S., Nguyen, T., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00392-6 · Cited by 68 · see citing works
Ceramides and sphingomyelinases in senile plaques
Panchal, M., Gaudin, M., Lazar, A. N., Salvati, E., Rivals, I., Ayciriex, S., Dauphinot, L., Dargère, D., Auzeil, N., Masserini, M., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.01.010 · Cited by 68 · see citing works
Dinkins, M. B., Dasgupta, S., Wang, G., Zhu, G., He, Q., Kong, J. N., & Bieberich, E. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150088 · Cited by 68 · see citing works
He, S., Xu, Z., & Han, X. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00803-6 · Cited by 62 · see citing works
Angerer, T. B., Pour, M. D., Malmberg, P., & Fletcher, J. S. (2015) · Analytical Chemistry · doi:10.1021/ac504774y · Cited by 66 · see citing works
Ceramide Metabolism and Parkinson’s Disease—Therapeutic Targets
Custodia, A., Aramburu-Núñez, M., Correa‐Paz, C., Posado-Fernández, A., Gómez-Larrauri, A., Castillo, J., Gómez‐Muñoz, A., Sobrino, T., & Ouro, A. (2021) · Biomolecules · doi:10.3390/biom11070945 · Cited by 63 · see citing works
Lipidomics of Bioactive Lipids in Alzheimer’s and Parkinson’s Diseases: Where Are We?
Chiurchiù, V., Tiberi, M., Matteocci, A., Fazio, F., Siffeti, H., Saracini, S., Mercuri, N. B., & Sancesario, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116235 · Cited by 65 · see citing works
Lucaciu, A., Brunkhorst, R., Pfeilschifter, J. M., Pfeilschifter, W., & Subburayalu, J. (2020) · Cells · doi:10.3390/cells9061515 · Cited by 65 · see citing works
Microglia in juvenile neuronal ceroid lipofuscinosis are primed toward a pro‐inflammatory phenotype
Xiong, J., & Kielian, T. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12385 · Cited by 64 · see citing works
Nie, Y., Chu, C., Qin, Q., Shen, H., Wen, L., Tang, Y., & Qu, M. (2023) · Brain Pathology · doi:10.1111/bpa.13202 · Cited by 63 · see citing works
Lu, S., Zhu, X., Zeng, P., Hu, L., Huang, Y., Guo, X., Chen, Q., Wang, Y., Lai, L., Xue, A., et al. (2024) · Environmental Pollution · doi:10.1016/j.envpol.2024.125098 · Cited by 61 · see citing works
CSF proteomics in autosomal dominant Alzheimer’s disease highlights parallels with sporadic disease
van der Ende, E. L., Veld, S. G. J. G. I. ‘., Hanskamp, I., van der Lee, S. J., Dijkstra, J. I. R., Hok‐A‐Hin, Y. S., Blujdea, E. R., Swieten, J. C. V., Irwin, D. J., Chen‐Plotkin, A. S., et al. (2023) · Brain · doi:10.1093/brain/awad213 · Cited by 55 · see citing works
Body Mass Index in Multiple Sclerosis modulates ceramide-induced DNA methylation and disease course
Castro, K., Ntranos, A., Amatruda, M., Petracca, M., Kosa, P. F., Chen, E. Y.-S., Morstein, J., Trauner, D. H., Watson, C. T., Kiebish, M. A., et al. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.03.087 · Cited by 59 · see citing works
Zhu, C., Huai, Q., Zhang, X., Dai, H., Li, X., & Wang, H. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.78525 · Cited by 59 · see citing works
Elevated plasma ceramide levels in post-menopausal women: a cross-sectional study
Vozella, V., Basit, A., Piras, F., Realini, N., Armirotti, A., Bossù, P., Assogna, F., Sensi, S. L., Spalletta, G., & Piomelli, D. (2019) · Aging · doi:10.18632/aging.101719 · Cited by 58 · see citing works
Could plasma sphingolipids be diagnostic or prognostic biomarkers for Alzheimer’s disease?
Mielke, M. M., & Haughey, N. J. (2012) · Clinical Lipidology · doi:10.2217/clp.12.59 · Cited by 56 · see citing works
The lysosomal storage disease continuum with ageing-related neurodegenerative disease
Lloyd‐Evans, E., & Haslett, L. J. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.07.005 · Cited by 57 · see citing works
Song, Z., Xu, Y., Zhang, L., Zhou, L., Zhang, Y., Han, Y., Li, X., Yü, P., Qu, Y., Zhao, W., et al. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.565479 · Cited by 55 · see citing works
Ji, F., Sreenivasmurthy, S. G., Wei, J., Shao, X., Luan, H., Zhu, L., Song, J., Liu, L., Li, M., & Cai, Z. (2019) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2019.06.015 · Cited by 55 · see citing works
Membrane raft domains and remodeling in aging brain
Colin, J., Gregory-Pauron, L., Lanhers, M.-C., Claudepierre, T., Corbier, C., Yen, F. T., Malaplate-Armand, C., & Oster, T. (2016) · Biochimie · doi:10.1016/j.biochi.2016.08.014 · Cited by 55 · see citing works
Ceramides are fuel gauges on the drive to cardiometabolic disease
Wilkerson, J. L., Tatum, S. M., Holland, W. L., & Summers, S. A. (2024) · Physiological Reviews · doi:10.1152/physrev.00008.2023 · Cited by 59 · see citing works
Sun, Y., Wei, K., Liao, X., Wang, J., Gao, L., & Pang, B. (2025) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2025.5580 · Cited by 57 · see citing works
Michno, W., Kaya, I., Nyström, S., Guérard, L., Nilsson, K. P. R., Hammarström, P., Blennow, K., Zetterberg, H., & Hanrieder, J. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b01361 · Cited by 53 · see citing works
Parkinson's disease pathogenesis, evolution and alternative pathways: A review
Alexoudi, A., Alexoudi, I., & Gatzonis, S. D. (2018) · Revue Neurologique · doi:10.1016/j.neurol.2017.12.003 · Cited by 52 · see citing works
Subventricular zone lipidomic architecture loss in Huntington's disease
Hunter, M., Demarais, N. J., Faull, R. L. M., Grey, A. C., & Curtis, M. A. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14468 · Cited by 52 · see citing works
Sphingolipids accumulate in aged muscle, and their reduction counteracts sarcopenia
Laurila, P., Wohlwend, M., de Lima, T. I., Luan, P., Herzig, S., Zanou, N., Crisol, B., Sleiman, M. S. B., Porcu, E., Gallart‐Ayala, H., et al. (2022) · Nature Aging · doi:10.1038/s43587-022-00309-6 · Cited by 51 · see citing works
Ayub, M., Jin, H.-K., & Bae, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147353 · Cited by 51 · see citing works
Sphingolipid metabolism in brain insulin resistance and neurological diseases
Mei, M., Liu, M., Mei, Y., Zhao, J., & Li, Y. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1243132 · Cited by 50 · see citing works
Acid Ceramidase Deficiency in Mice Results in a Broad Range of Central Nervous System Abnormalities
Sikora, J., Dworski, S., Jones, E. E., Kamani, M. A., Micsenyi, M. C., Sawada, T., Faouder, P. L., Bertrand‐Michel, J., Dupuy, A., Dunn, C. K., et al. (2017) · American Journal Of Pathology · doi:10.1016/j.ajpath.2016.12.005 · Cited by 50 · see citing works
Bouscary, A., Quessada, C., René, F., Spedding, M., Turner, B. J., Henriques, A., Ngo, S. T., & Loeffler, J. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.10.008 · Cited by 47 · see citing works
Lipidomic Profiles in Diabetes and Dementia
Huynh, K., Martins, R. N., & Meikle, P. J. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161215 · Cited by 47 · see citing works
The role of mitochondrial defects and oxidative stress in Alzheimer’s disease
Islam, B. U., Jabir, N. R., & Tabrez, S. S. M. (2019) · Journal of drug targeting · doi:10.1080/1061186x.2019.1584808 · Cited by 48 · see citing works
Zhang, F., Wei, J., Li, X., Ma, C., & Gao, Y. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180412 · Cited by 47 · see citing works
Death-associated protein kinase 1 as a therapeutic target for Alzheimer's disease
Zhang, T., Kim, B. M., & Lee, T. H. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-023-00395-5 · Cited by 47 · see citing works
Type 2 Diabetes and Alzheimer’s Disease: The Emerging Role of Cellular Lipotoxicity
Marrano, N., Biondi, G., Borrelli, A., Rella, M., Zambetta, T., Gioia, L. D., Caporusso, M., Logroscino, G., Perrini, S., Giorgino, F., et al. (2023) · Biomolecules · doi:10.3390/biom13010183 · Cited by 44 · see citing works
Inhibition of sphingolipid de novo synthesis counteracts muscular dystrophy
Laurila, P., Luan, P., Wohlwend, M., Zanou, N., Crisol, B., de Lima, T. I., Goeminne, L. J. E., Gallart‐Ayala, H., Shong, M., Ivanišević, J., et al. (2022) · Science Advances · doi:10.1126/sciadv.abh4423 · Cited by 43 · see citing works
Zhan, X., Cox, C. D., Ander, B. P., Liu, D., Stamova, B. S., Jin, L., Jickling, G. C., & Sharp, F. R. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-143072 · Cited by 41 · see citing works
The silence of the fats: A MAM’s story about Alzheimer
Agrawal, R. R., Montesinos, J., Larrea, D., Área-Gómez, E., & Pera, M. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105062 · Cited by 41 · see citing works
The Role of Sphingolipids and Specialized Pro-Resolving Mediators in Alzheimer’s Disease
de Wit, N. M., Mol, K., Rodríguez‐Lorenzo, S., de Vries, H. E., & Kooij, G. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.620348 · Cited by 39 · see citing works
Synapses, Microglia, and Lipids in Alzheimer’s Disease
Paasila, P. J., Aramideh, J. A., Sutherland, G. T., & Graeber, M. B. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.778822 · Cited by 38 · see citing works
Crivelli, S. M., Quadri, Z., Vekaria, H. J., Zhu, Z., Tripathi, P., Elsherbini, A. M., Zhang, L., Sullivan, P. G., & Bieberich, E. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01633-7 · Cited by 39 · see citing works
Membrane lipid raft homeostasis is directly linked to neurodegeneration
Moll, T., Marshall, J. N. G., Soni, N., Zhang, S., Cooper‐Knock, J., & Shaw, P. J. (2021) · Essays in Biochemistry · doi:10.1042/ebc20210026 · Cited by 37 · see citing works
Lipid Metabolic Alterations in the ALS–FTD Spectrum of Disorders
Godoy-Corchuelo, J. M., Fernández-Beltrán, L. C., Ali, Z., Gil-Moreno, M. J., López-Carbonero, J. I., Guerrero-Sola, A., Larrad-Sainz, A., Matias-Guiu, J., Matias-Guiu, J. A., Cunningham, T. J., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10051105 · Cited by 35 · see citing works
Characterization of Acid Sphingomyelinase Activity in Human Cerebrospinal Fluid
Mühle, C., Huttner, H. B., Walter, S., Reichel, M., Canneva, F., Lewczuk, P., Gulbins, E., & Kornhuber, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062912 · Cited by 35 · see citing works
Suppression of tau propagation using an inhibitor that targets the DK-switch of nSMase2
Bilousova, T. V., Elias, C. J., Miyoshi, E., Alam, M. P., Zhu, C., Campagna, J. J., Vadivel, K., Jagodzinska, B. M., Gylys, K. H., & John, V. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.03.209 · Cited by 35 · see citing works
Tallon, C., Bell, B. J., Malvankar, M. M., Deme, P., Nogueras‐Ortiz, C. J., Eren, E., Thomas, A. G., Hollinger, K. R., Pal, A., Mustapić, M., et al. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00383-9 · Cited by 34 · see citing works
Alterations in neuronal metabolism contribute to the pathogenesis of prion disease
Bourgognon, J.-M., Spiers, J. G., Scheiblich, H., Antonov, A., Bradley, S. J., Tobin, A. B., & Steinert, J. R. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0148-x · Cited by 34 · see citing works
Teitsdottir, U. D., Halldórsson, S., Rolfsson, Ó., Lund, S. H., Jónsdóttir, M. K., Snædal, J., & Petersen, P. H. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-200964 · Cited by 37 · see citing works
Zhu, C., Bilousova, T. V., Focht, S., Jun, M., Elias, C. J., Melnik, M., Chandra, S., Campagna, J. J., Cohn, W., Hatami, A., et al. (2021) · Molecular Brain · doi:10.1186/s13041-021-00776-9 · Cited by 33 · see citing works
Kawade, N., & Yamanaka, K. (2023) · FEBS Open Bio · doi:10.1002/2211-5463.13661 · Cited by 32 · see citing works
Bilousova, T. V., Simmons, B. J., Knapp, R. R., Elias, C. J., Campagna, J. J., Melnik, M., Chandra, S., Focht, S., Zhu, C., Vadivel, K., et al. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00311 · Cited by 32 · see citing works
Sergi, D., Zauli, E., Tisato, V., Secchiero, P., Zauli, G., & Cervellati, C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054403 · Cited by 32 · see citing works
Metabolomic Study of Hibernating Syrian Hamster Brains: In Search of Neuroprotective Agents
González-Riaño, C., León‐Espinosa, G., Regalado-Reyes, M., Garcı́a, A., DeFelipe, J., & Barbas, C. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00816 · Cited by 31 · see citing works
Yamada, C., Akkaoui, J., Ho, A., Duarte, C. L., Deth, R. C., Kawai, T., Nichols, F. C., Lakshmana, M. K., & Movilă, A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.591571 · Cited by 31 · see citing works
Tobeh, N. S., & Bruce, K. D. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1259012 · Cited by 31 · see citing works
- Authors
- Filippov, V., Song, M. A., Zhang, K., Vinters, H. V., Tung, S., Kirsch, W. M., Yang, J., & Duerksen-Hughes, P. J.
- Affiliations
- Loma Linda University (US)
- University of California, Los Angeles (US)
- Hangzhou Normal University (CN)
- Corresponding author
- Duerksen-Hughes, Penelope J.
- ORCID
- Venue
- Journal of Alzheimer s Disease
- Publisher
- SAGE Publications
- Published
- 2012-03-30
- Volume
- 29
- Issue
- 3
- Pages
- 537-547
- ISSN
- 1387-2877 (ISSN-L)
- 1875-8908
- PMC
- PMC3643694
- OpenAlex
- W2145962946
- Cited by
- 264
- References
- 23
- Citations by year
- 2026: 12 · 2025: 28 · 2024: 28 · 2023: 29 · 2022: 27 · 2021: 22 · 2020: 26 · 2019: 11 · 2018: 17 · 2017: 21 · 2016: 14 · 2015: 8 · 2014: 10 · 2013: 10 · 2012: 1
- FWCI
- 3.73
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Alzheimer s Disease (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (P50AG016570, P50-AG 16570)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
- Health Sciences › Medicine › Physiology › Lysosomal Storage Disorders Research
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- ceramide, Alzheimer's disease
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Brain, Ceramides, Chromatography, High Pressure Liquid, Female, Galactosylceramidase, Gene Expression Regulation, Humans, Male, RNA, Messenger, Sphingomyelin Phosphodiesterase, Case-Control Studies, Neurodegenerative Diseases, Tandem Mass Spectrometry
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