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Tau Phosphorylation Rates Measured by Mass Spectrometry Differ in the Intracellular Brain vs. Extracellular Cerebrospinal Fluid Compartments and Are Differentially Affected by Alzheimer’s Disease
Open accessAbstract
Tau protein aggregation into neurofibrillary tangles in the central nervous system contributes to the etiology of certain neurodegenerative disorders, including Alzheimer's disease (AD). Though the mechanism of tau destabilization is not fully understood yet, tau protein has been found to be hyperphosphorylated in tau aggregates. To investigate this further, we developed a highly sensitive and specific mass spectrometry (MS) method using parallel reaction monitoring (PRM) to identify tau phosphorylation sites. This method enables us to compare the abundance of phosphorylation sites in tau proteins in the brain and cerebrospinal fluid (CSF) in humans with and without AD. We detected 29 distinct phosphorylated tau (p-tau) sites in full-length tau from soluble human brain lysate and 12 sites on truncated tau in CSF, mainly in the mid-domain. Brain soluble tau phosphorylation sites are localized on three domains including a proline-rich mid-domain, the C-terminus, and a cluster on the N-terminal projection domain not previously characterized. Some phosphorylation sites increased in CSF, while others decreased compared to brain. Notably, phosphorylation on T205 and S208, recognized by AT8 antibody defining Braak stages of brain tau aggregation, were not detected in normal brain soluble tau but were found in the CSF. Comparison of the p-tau rates from the brain and the CSF indicated that the abundance of phosphorylated sites varied in a site-specific manner. CSF tau proteins from non-AD participants were significantly hyperphosphorylated on T111, T205, S208, T217 and T231. In AD CSF, hyperphosphorylation on these sites was exacerbated, and phosphorylation on T153 and T175 specifically were detected. This supports the hypothesis that tau hyperphosphorylation could be a physiological process amplified by AD pathology. Conversely, we found that S202 was hypophosphorylated in CSF and was not hyperphosphorylated in AD, demonstrating that p-tau isoforms could have different metabolisms depending on which sites are phosphorylated. These site-specific p-tau rates are independent of tau concentration and distinct of current CSF tau and p-tau assays measuring tau isoforms levels. Targeted MS multiplexing ability and high-throughput capacity lets us envision the use of these new p-tau measurements as promising biomarkers for AD diagnosis and tracking therapeutic responses.
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“a recent mass spectrometry–based study found increased degree of phosphorylation at position 217 compared with position 181 in CSF from patients with AD (9).”
From Aβ deposition is associated with increases in soluble and phosphorylated tau that precede a positive tau PET in Alzheimer's disease (2020) · cites this paper as [9]
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Citations
Cites
Staging of alzheimer's disease-related neurofibrillary changes
Braak, H., & Braak, E. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00021-6 · Cited by 2,357
Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251
Peterson, A. C., Russell, J. D., Bailey, D. J., Westphall, M. S., & Coon, J. J. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o112.020131 · Cited by 1,288
PET Imaging of Tau Deposition in the Aging Human Brain
Schöll, M., Lockhart, S. N., Schonhaut, D. R., O’Neil, J. P., Janabi, M., Ossenkoppele, R., Baker, S. L., Vogel, J. W., Faria, J., Schwimmer, H. D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.028 · Cited by 1,214
Tau pathology in Alzheimer disease and other tauopathies
Iqbal, K., del C. Alonso, A., Chen, S., Chohan, M. O., El-Akkad, E., Gong, C.-X., Khatoon, S., Li, B., Liu, F., Rahman, A., et al. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.008 · Cited by 1,037
Augustinack, J. C., Schneider, A., Mandelkow, E.-M., & Hyman, B. T. (2002) · Acta Neuropathologica · doi:10.1007/s004010100423 · Cited by 998
Alonso, A. D. C., Zaidi, T., Novak, M., Grundke-Iqbal, I., & Iqbal, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121119298 · Cited by 827
Biernat, J., Gustke, N., Drewes, G., Mandelkow, E., & Mandelkow, E. (1993) · Neuron · doi:10.1016/0896-6273(93)90279-z · Cited by 796
Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779
Neuronal activity regulates extracellular tau in vivo
Yamada, K., Holth, J. K., Liao, F., Stewart, F. R., Mahan, T. E., Jiang, H., Cirrito, J. R., Patel, T. K., Hochgräfe, K., Mandelkow, E., et al. (2014) · The Journal of Experimental Medicine · doi:10.1084/jem.20131685 · Cited by 606
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Items 101–156 of 156
Faldu, K. G., & Shah, J. (2022) · Expert Review of Molecular Diagnostics · doi:10.1080/14737159.2022.2104639 · Cited by 10
Biofluid biomarkers for Alzheimer’s disease
Wang, S., Xie, S., Zheng, Q., Zhang, Z., Wang, T., & Zhang, G. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1380237 · Cited by 9
Molecular mechanisms of aging in the pathogenesis of Alzheimer’s disease
Kakkar, A., Singh, H., Singh, B. K., Chauhan, K., Chopra, S., Chopra, H., & Mishra, A. K. (2026) · Discover Neuroscience · doi:10.1186/s13064-026-00243-y · Cited by 9
Untangling the tau microtubule-binding region
Toombs, J., & Zetterberg, H. (2020) · Brain · doi:10.1093/brain/awaa468 · Cited by 8
Distribution of Big Tau Isoforms in the Human Central and Peripheral Nervous System
Koppisetti, R. K., Barthélemy, N. R., Horie, K., Ly, C. V., Roberts, K. F., Koutarapu, S., Perrin, R. J., Franklin, E. E., Pedicone, C., Orrick, J., et al. (2026) · Annals of Neurology · doi:10.1002/ana.78300 · Cited by 7
Self-citationUnambiguous Tracking of Protein Phosphorylation by Fast High‐Resolution FOSY NMR**
Lesovoy, D. M., Georgoulia, P. S., Diercks, T., Matečko‐Burmann, I., Burmann, B. M., Bocharov, E. V., Bermel, W., & Orekhov, V. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202102758 · Cited by 7
Subjective hearing loss is not associated with an increased risk of Alzheimer's disease dementia
Lad, M., Taylor, J., & Griffiths, T. D. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e30423 · Cited by 7
Kinase inhibition in Alzheimer’s disease
Bagheri, S., & Saboury, A. A. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91287-7.00003-x · Cited by 6
Hajjar, L. E., Bridot, C., Nguyen, M., Cantrelle, F., Landrieu, I., & Smet‐Nocca, C. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3629-9_15 · Cited by 6
Wu, L., Wang, Z., Lad, S., Dougharty, D. T., Madhavan, S. S., Marcus, M., Henderson, F. E., Ray, W. K., Tan, C., Siedlak, S. L., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2019.12.31.876946 · Cited by 6
Das, S., Awasthi, A., Rawal, R. K., & Bhatia, R. (2026) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-025-05549-x · Cited by 6
Making tau amyloid models in vitro: a crucial and underestimated challenge
Broc, J., Piersson, C., & Fichou, Y. (2025) · FEBS Letters · doi:10.1002/1873-3468.70022 · Cited by 5
P-tau231 as a Diagnostic Biomarker for Alzheimer's Disease and Mild Cognitive Impairment
Nabizadeh, F., Salehi, N., Ramezannezhad, E., Sadeghmousavi, S., & Khalili, E. (2022) · Annals of Indian Academy of Neurology · doi:10.4103/aian.aian_77_22 · Cited by 6
Effects of Neighboring Phosphorylation Events on the Affinities of pT181-Tau Antibodies
Min, S., Mohallem, R., Aryal, U. K., Kinzer‐Ursem, T. L., & Rochet, J. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c04081 · Cited by 4
Patel, R., Cheng, R., Cardona, C. L., Angeles, E., Singh, G., Miller, S., Ashok, A., Teich, A. F., Piriz, A. L., Maldonado, A., et al. (2026) · Glia · doi:10.1002/glia.70165 · Cited by 5
Soluble form of the APP fragment, sAPPβ, positively regulates tau secretion
Sato, H., Kasuga, K., Isoo, N., Hayashi, T., Ikeuchi, T., Hori, Y., & Tomita, T. (2023) · Neuroscience Research · doi:10.1016/j.neures.2023.03.002 · Cited by 4
Multi-omics integration in disease research
Ceballos, M. W. G., Sy, F., Akbar, A., & Taofiq, A. (2025) · Progress in brain research · doi:10.1016/bs.pbr.2025.08.012 · Cited by 4
Development of New Blood Immunoassay and Biomarkers for Tau in the Diagnosis of Alzheimer’s Disease
Li, X., Zeng, H., Durairaj, P., Wen, W., Li, T., Zhao, Y., Liu, Y., Liu, X., Qiu, Y., Xing, J., et al. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00301 · Cited by 3
Yang, W., Yu, Q., Wang, N., Lam, K. K. Y., Lin, Z., & Xian, Y. (2025) · NeuroMolecular Medicine · doi:10.1007/s12017-025-08860-2 · Cited by 4
Sindi, G., Ismael, S., Uddin, R., Slepchenko, K. G., Colvin, R. A., & Lee, D. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.02.597022 · Cited by 3
Analysis of Brain Protein Stability Changes in a Mouse Model of Alzheimer’s Disease
Tang, Y., Park, H.-J., Li, S., & Fitzgerald, M. C. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c00406 · Cited by 2
A novel pThr217 tau monoclonal antibody reveals neuropathological heterogeneity in tauopathies
Paterno, G., Bell, B. M., Gorion, K.-M. M., Quintin, S. S., Prokop, S., & Giasson, B. I. (2025) · Scientific Reports · doi:10.1038/s41598-025-04291-y · Cited by 2
Reveglia, P., Nasso, R., Angiolillo, A., Lecce, L., Paolillo, C., Tullio, S. D., Gelzo, M., Costanzo, A. D., Matrone, C., & Corso, G. (2021) · Biomolecules · doi:10.3390/biom11091297 · Cited by 2
Li, S., Luo, Z., Meng, S., Qiu, X., Zheng, F., Dai, W., Zhang, X., Sui, W., Yan, Q., Tang, D., et al. (2021) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.202000069 · Cited by 2
Novel Conformation-Dependent Tau Antibodies Are Modulated by Adjacent Phosphorylation Sites
Paterno, G., Torrellas, J., Bell, B. M., Gorion, K.-M. M., Quintin, S. S., Hery, G. P., Prokop, S., & Giasson, B. I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813676 · Cited by 2
Barthélemy, N. R., Saef, B. A., Li, Y., Gordon, B. A., He, Y., Horie, K., Stomrud, E., Salvadó, G., Janelidze, S., Sato, C., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-2175929/v1 · Cited by 2
Self-citationUnambiguous Tracking of Protein Phosphorylation by Fast High‐Resolution FOSY NMR**
Lesovoy, D. M., Georgoulia, P. S., Diercks, T., Matečko‐Burmann, I., Burmann, B. M., Bocharov, E. V., Bermel, W., & Orekhov, V. (2021) · Angewandte Chemie · doi:10.1002/ange.202102758 · Cited by 1
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Tanveer, A., & Yadav, D. (2022) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815040913122010012 · Cited by 1
Kemppainen, S., Aramburu-Núñez, M., Koivisto, H., Posado-Fernández, A., Felix-Garcia, M. R., Nurminen, K., Häkli, S., Abellí‐Deulofeu, E., Kaisto, M., Custodia, A., et al. (2025) · Experimental Neurology · doi:10.1016/j.expneurol.2025.115315 · Cited by 1
Neurotheranostics in Alzheimer's Disease: Current concepts and experimental strategies
Yanagisawa, D., Ohgita, T., Kawashima, H., Yoshikawa, H., Saito, H., Tooyama, I., & Takata, K. (2026) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2026.109084 · Cited by 1
Schneeweis, A. K., & Pak, D. T. S. (2023) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2023.106475 · Cited by 1
Jacquemin, C., Villain, N., Azevedo, R., Boluda, S., Thévenot, E., Fenaille, F., Lamari, F., & Bécher, F. (2024) · European Journal of Mass Spectrometry · doi:10.1177/14690667231218912 · Cited by 1
Aguilar-Pineda, J. A., Vera-López, K. J., Shrivastava, P., Nieto-Montesinos, R., Chávez‐Fumagalli, M. Á., Dávila-Del-Carpio, G., Valdez, B. G., Miller, C. L., Malhotra, R. K., Lindsay, M. E., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.13.439741 · Cited by 1
Bazan, N. G., Bhattacharjee, S., Kala-Bhattacharjee, S., Ledet, A. J., & Mukherjee, P. K. (2023) · Research Square · doi:10.21203/rs.3.rs-3185942/v1 · Cited by 1
Confirmation de biomarqueurs pour le pronostic du sepsis et développement de tests rapides
Dubois, C. (2019) · theses.fr (ABES) · doi:10.70675/4101c43dzc2b3z4ae2zb315z16d8d8252081 · Cited by 1
Sasmita, A. O. (2024) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-10403
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Arastoo, M., Penny, L. K., Lofthouse, R. A., Hitchcock, A., Moelders, A., Szalma, S., Porter, A. J., Palliyil, S., Harrington, C. R., & Wischik, C. M. (2025) · Scientific Reports · doi:10.1038/s41598-025-25864-x
Horie, K., Barthélemy, N. R., Mallipeddi, N., Li, Y., Franklin, E. E., Perrin, R. J., Bateman, R. J., & Sato, C. (2020) · Figshare · doi:10.6084/m9.figshare.12886049
Self-citationAdditional file 6 of Tau protein profiling in tauopathies: a human brain study
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Additional file 5 of Tau protein profiling in tauopathies: a human brain study
Lantero‐Rodriguez, J., Camporesi, E., Montoliu‐Gaya, L., Gobom, J., Piotrowska, D., Olsson, M., Matečko‐Burmann, I., Becker, B., Brinkmalm, A., Burmann, B. M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26751389
Additional file 3 of Tau protein profiling in tauopathies: a human brain study
Lantero‐Rodriguez, J., Camporesi, E., Montoliu‐Gaya, L., Gobom, J., Piotrowska, D., Olsson, M., Matečko‐Burmann, I., Becker, B., Brinkmalm, A., Burmann, B. M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26751383
Barthélemy, N. R., Bateman, R. J., Hirtz, C., Marin, P., Bécher, F., Sato, C., Gabelle, A., & Lehmann, S. (2020) · Figshare · doi:10.6084/m9.figshare.11998815
Self-citationBarthélemy, N. R., Bateman, R. J., Hirtz, C., Marin, P., Bécher, F., Sato, C., Gabelle, A., & Lehmann, S. (2020) · Figshare · doi:10.6084/m9.figshare.11998812
Self-citationAdditional file 8 of Tau protein profiling in tauopathies: a human brain study
Lantero‐Rodriguez, J., Camporesi, E., Montoliu‐Gaya, L., Gobom, J., Piotrowska, D., Olsson, M., Matečko‐Burmann, I., Becker, B., Brinkmalm, A., Burmann, B. M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26751398
Additional file 1 of Tau protein profiling in tauopathies: a human brain study
Lantero‐Rodriguez, J., Camporesi, E., Montoliu‐Gaya, L., Gobom, J., Piotrowska, D., Olsson, M., Matečko‐Burmann, I., Becker, B., Brinkmalm, A., Burmann, B. M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26333190
Lantero‐Rodriguez, J., Vrillon, A., Fernández‐Lebrero, A., Ortiz‐Romero, P., Snellman, A., Montoliu‐Gaya, L., Brum, W. S., Cognat, E., Dumurgier, J., Puig‐Pijoan, A., et al. (2023) · Figshare · doi:10.6084/m9.figshare.22625720
Additional file 7 of Tau protein profiling in tauopathies: a human brain study
Lantero‐Rodriguez, J., Camporesi, E., Montoliu‐Gaya, L., Gobom, J., Piotrowska, D., Olsson, M., Matečko‐Burmann, I., Becker, B., Brinkmalm, A., Burmann, B. M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26751395
Additional file 2 of Tau protein profiling in tauopathies: a human brain study
Lantero‐Rodriguez, J., Camporesi, E., Montoliu‐Gaya, L., Gobom, J., Piotrowska, D., Olsson, M., Matečko‐Burmann, I., Becker, B., Brinkmalm, A., Burmann, B. M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26333445
Additional file 4 of Tau protein profiling in tauopathies: a human brain study
Lantero‐Rodriguez, J., Camporesi, E., Montoliu‐Gaya, L., Gobom, J., Piotrowska, D., Olsson, M., Matečko‐Burmann, I., Becker, B., Brinkmalm, A., Burmann, B. M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26751386
Gobom, J., Benedet, A. L., Mattsson, N., Montoliu‐Gaya, L., Schultz, N., Ashton, N. J., Janelidze, S., Servaes, S., Sauer, M., Pascoal, T. A., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26553350
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Ledesma-Aparicio, J., Caro-Gómez, L. A., Padilla-Godínez, F. J., Hernández‐González, O., Soto-Rojas, L. O., Reyes‐Grajeda, J. P., Arias-Carrión, Ó., Palomero‐Rivero, M., Bertrand, B., Muñóz-Garay, C., et al. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1841131
Mukherjee, S., Barthélemy, N. R., Atri, T. E., Wang, Q., Yen, D. P., He, Y., Coyle, R. A., Ovod, V., Franklin, E. E., Xiong, C., et al. (2026) · medRxiv · doi:10.64898/2026.09.22.26363432
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Metadata
- Authors
- Barthélemy, N. R., Mallipeddi, N., Moiseyev, P., Sato, C., & Bateman, R. J.
- Affiliations
- Washington University in St. Louis (US)
- Corresponding author
- Barthélemy, Nicolas R.
- Bateman, Randall J.
- Venue
- Frontiers in Aging Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2019-05-21
- Volume
- 11
- Pages
- 121-121
- ISSN
- 1663-4365 (ISSN-L)
- PMC
- PMC6537657
- OpenAlex
- W2945823364
- Cited by
- 152
- References
- 34
- Citations by year
- 2026: 10 · 2025: 15 · 2024: 24 · 2023: 19 · 2022: 22 · 2021: 32 · 2020: 25 · 2019: 5
- FWCI
- 14.41
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Aging Neuroscience (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Digital Commons@Becker (Washington University School of Medicine) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Alzheimer’s Association (AARF-16-443265)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau phosphorylation, Alzheimer's disease, cerebrospinal fluid, brain, parallel reaction monitoring, tau phosphorylation sites, neurofibrillary tangles, tau isoforms, AT8 antibody, Braak stages, biomarkers, tau aggregation, site-specific phosphorylation, targeted mass spectrometry
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