Tau Kinetics in Neurons and the Human Central Nervous System
We developed stable isotope labeling and mass spectrometry approaches to measure the kinetics of multiple isoforms and fragments of tau in the human central nervous system (CNS) and in human induced pluripotent stem cell (iPSC)-derived neurons. Newly synthesized tau is truncated and released from hu...
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| Published in | Neuron (Cambridge, Mass.) Vol. 97; no. 6; pp. 1284 - 1298.e7 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
21.03.2018
Elsevier Limited |
| Subjects | |
| Online Access | Get full text |
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| Abstract | We developed stable isotope labeling and mass spectrometry approaches to measure the kinetics of multiple isoforms and fragments of tau in the human central nervous system (CNS) and in human induced pluripotent stem cell (iPSC)-derived neurons. Newly synthesized tau is truncated and released from human neurons in 3 days. Although most tau proteins have similar turnover, 4R tau isoforms and phosphorylated forms of tau exhibit faster turnover rates, suggesting unique processing of these forms that may have independent biological activities. The half-life of tau in control human iPSC-derived neurons is 6.74 ± 0.45 days and in human CNS is 23 ± 6.4 days. In cognitively normal and Alzheimer’s disease participants, the production rate of tau positively correlates with the amount of amyloid plaques, indicating a biological link between amyloid plaques and tau physiology.
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•Multiple forms of tau exist in the human brain, CSF, and iPSC-derived neurons•Newly synthesized tau is truncated and actively released by human neurons•Fibrillogenic forms of tau have shorter half-lives than non-fibrillogenic forms•Tau production rate positively correlates with amyloid plaque burden
Sato et al. show that stable isotope labeling kinetics enable measurement of tau in the CNS and in iPSC-derived neurons. Specific forms of tau are uniquely processed in neurons and tau production rates correlate with amyloid accumulation in human subjects. |
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| AbstractList | We developed stable isotope labeling and mass spectrometry approaches to measure the kinetics of multiple isoforms and fragments of tau in the human central nervous system (CNS) and in human induced pluripotent stem cell (iPSC)-derived neurons. Newly synthesized tau is truncated and released from human neurons in 3 days. Although most tau proteins have similar turnover, 4R tau isoforms and phosphorylated forms of tau exhibit faster turnover rates, suggesting unique processing of these forms that may have independent biological activities. The half-life of tau in control human iPSC-derived neurons is 6.74 ± 0.45 days and in human CNS is 23 ± 6.4 days. In cognitively normal and Alzheimer’s disease participants, the production rate of tau positively correlates with the amount of amyloid plaques, indicating a biological link between amyloid plaques and tau physiology.
[Display omitted]
•Multiple forms of tau exist in the human brain, CSF, and iPSC-derived neurons•Newly synthesized tau is truncated and actively released by human neurons•Fibrillogenic forms of tau have shorter half-lives than non-fibrillogenic forms•Tau production rate positively correlates with amyloid plaque burden
Sato et al. show that stable isotope labeling kinetics enable measurement of tau in the CNS and in iPSC-derived neurons. Specific forms of tau are uniquely processed in neurons and tau production rates correlate with amyloid accumulation in human subjects. We developed stable isotope labeling and mass spectrometry approaches to measure the kinetics of multiple isoforms and fragments of tau in the human central nervous system (CNS) and in human induced pluripotent stem cell (iPSC)-derived neurons. Newly synthesized tau is truncated and released from human neurons in 3 days. Although most tau proteins have similar turnover, 4R tau isoforms and phosphorylated forms of tau exhibit faster turnover rates, suggesting unique processing of these forms that may have independent biological activities. The half-life of tau in control human iPSC-derived neurons is 6.74 ± 0.45 days and in human CNS is 23 ± 6.4 days. In cognitively normal and Alzheimer's disease participants, the production rate of tau positively correlates with the amount of amyloid plaques, indicating a biological link between amyloid plaques and tau physiology. We developed stable isotope labeling and mass spectrometry approaches to measure the kinetics of multiple isoforms and fragments of tau in the human central nervous system (CNS) and in human induced pluripotent stem cell (iPSC)-derived neurons. Newly synthesized tau is truncated and released from human neurons in 3 days. Although most tau proteins have similar turnover, 4R tau isoforms and phosphorylated forms of tau exhibit faster turnover rates, suggesting unique processing of these forms that may have independent biological activities. The half-life of tau in control human iPSC-derived neurons is 6.74 ± 0.45 days and in human CNS is 23 ± 6.4 days. In cognitively normal and Alzheimer's disease participants, the production rate of tau positively correlates with the amount of amyloid plaques, indicating a biological link between amyloid plaques and tau physiology.We developed stable isotope labeling and mass spectrometry approaches to measure the kinetics of multiple isoforms and fragments of tau in the human central nervous system (CNS) and in human induced pluripotent stem cell (iPSC)-derived neurons. Newly synthesized tau is truncated and released from human neurons in 3 days. Although most tau proteins have similar turnover, 4R tau isoforms and phosphorylated forms of tau exhibit faster turnover rates, suggesting unique processing of these forms that may have independent biological activities. The half-life of tau in control human iPSC-derived neurons is 6.74 ± 0.45 days and in human CNS is 23 ± 6.4 days. In cognitively normal and Alzheimer's disease participants, the production rate of tau positively correlates with the amount of amyloid plaques, indicating a biological link between amyloid plaques and tau physiology. We developed stable isotope labeling and mass spectrometry approaches to measure the kinetics of multiple isoforms and fragments of tau in the human central nervous system (CNS) and in human induced pluripotent stem cell (iPSC)-derived neurons. Newly synthesized tau is truncated and released from human neurons in 3 days. Although most tau proteins have similar turnover, 4R tau isoforms and phosphorylated forms of tau exhibit faster turnover rates, suggesting unique processing of these forms that may have independent biological activities. The half-life of tau in control human iPSCderived neurons is 6.74 ± 0.45 days and in human CNS is 23 ± 6.4 days. In cognitively normal and Alzheimer’s disease participants, the production rate of tau positively correlates with the amount of amyloid plaques, indicating a biological link between amyloid plaques and tau physiology. Sato et al. show that stable isotope labeling kinetics enable measurement of tau in the CNS and in iPSC-derived neurons. Specific forms of tau are uniquely processed in neurons and tau production rates correlate with amyloid accumulation in human subjects. SummaryWe developed stable isotope labeling and mass spectrometry approaches to measure the kinetics of multiple isoforms and fragments of tau in the human central nervous system (CNS) and in human induced pluripotent stem cell (iPSC)-derived neurons. Newly synthesized tau is truncated and released from human neurons in 3 days. Although most tau proteins have similar turnover, 4R tau isoforms and phosphorylated forms of tau exhibit faster turnover rates, suggesting unique processing of these forms that may have independent biological activities. The half-life of tau in control human iPSC-derived neurons is 6.74 ± 0.45 days and in human CNS is 23 ± 6.4 days. In cognitively normal and Alzheimer’s disease participants, the production rate of tau positively correlates with the amount of amyloid plaques, indicating a biological link between amyloid plaques and tau physiology. |
| Author | Patterson, Bruce W. Sullivan, Melissa Kirmess, Kristopher M. Bateman, Randall J. Kanaan, Nicholas M. Crisp, Matthew J. Mawuenyega, Kwasi G. Baker-Nigh, Alaina Benzinger, Tammie L.S. Miller, Timothy M. Gordon, Brian A. Karch, Celeste M. Sato, Chihiro Barthélemy, Nicolas R. Jockel-Balsarotti, Jennifer Kasten, Tom Yarasheski, Kevin E. |
| AuthorAffiliation | 1 Department of Neurology, Washington University School of Medicine, St. Louis, MO 63110, USA 4 Michigan State University, College of Human Medicine, Department of Translational Science and Molecular Medicine, Grand Rapids, MI 49503, USA 6 Department of Psychiatry, Washington University School of Medicine, St. Louis, MO 63110, USA 2 Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA 5 Hope Center for Neurological Disorders, Washington University School of Medicine, St. Louis, MO 63110, USA 7 Charles F. and Joanne Knight Alzheimer’s Disease Research Center, Washington University School of Medicine, St. Louis, MO 63110, USA 3 Department of Radiology, Washington University School of Medicine, St. Louis, MO 63110, USA 8 These authors contributed equally 9 Lead Contact |
| AuthorAffiliation_xml | – name: 9 Lead Contact – name: 5 Hope Center for Neurological Disorders, Washington University School of Medicine, St. Louis, MO 63110, USA – name: 8 These authors contributed equally – name: 2 Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA – name: 6 Department of Psychiatry, Washington University School of Medicine, St. Louis, MO 63110, USA – name: 3 Department of Radiology, Washington University School of Medicine, St. Louis, MO 63110, USA – name: 1 Department of Neurology, Washington University School of Medicine, St. Louis, MO 63110, USA – name: 7 Charles F. and Joanne Knight Alzheimer’s Disease Research Center, Washington University School of Medicine, St. Louis, MO 63110, USA – name: 4 Michigan State University, College of Human Medicine, Department of Translational Science and Molecular Medicine, Grand Rapids, MI 49503, USA |
| Author_xml | – sequence: 1 givenname: Chihiro surname: Sato fullname: Sato, Chihiro email: satochihiro@wustl.edu organization: Department of Neurology, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 2 givenname: Nicolas R. surname: Barthélemy fullname: Barthélemy, Nicolas R. organization: Department of Neurology, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 3 givenname: Kwasi G. surname: Mawuenyega fullname: Mawuenyega, Kwasi G. organization: Department of Neurology, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 4 givenname: Bruce W. surname: Patterson fullname: Patterson, Bruce W. organization: Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 5 givenname: Brian A. surname: Gordon fullname: Gordon, Brian A. organization: Department of Radiology, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 6 givenname: Jennifer surname: Jockel-Balsarotti fullname: Jockel-Balsarotti, Jennifer organization: Department of Neurology, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 7 givenname: Melissa surname: Sullivan fullname: Sullivan, Melissa organization: Department of Neurology, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 8 givenname: Matthew J. surname: Crisp fullname: Crisp, Matthew J. organization: Department of Neurology, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 9 givenname: Tom surname: Kasten fullname: Kasten, Tom organization: Department of Neurology, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 10 givenname: Kristopher M. surname: Kirmess fullname: Kirmess, Kristopher M. organization: Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 11 givenname: Nicholas M. surname: Kanaan fullname: Kanaan, Nicholas M. organization: Michigan State University, College of Human Medicine, Department of Translational Science and Molecular Medicine, Grand Rapids, MI 49503, USA – sequence: 12 givenname: Kevin E. surname: Yarasheski fullname: Yarasheski, Kevin E. organization: Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 13 givenname: Alaina surname: Baker-Nigh fullname: Baker-Nigh, Alaina organization: Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 14 givenname: Tammie L.S. surname: Benzinger fullname: Benzinger, Tammie L.S. organization: Department of Radiology, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 15 givenname: Timothy M. surname: Miller fullname: Miller, Timothy M. organization: Department of Neurology, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 16 givenname: Celeste M. surname: Karch fullname: Karch, Celeste M. email: karchc@wustl.edu organization: Hope Center for Neurological Disorders, Washington University School of Medicine, St. Louis, MO 63110, USA – sequence: 17 givenname: Randall J. surname: Bateman fullname: Bateman, Randall J. email: batemanr@wustl.edu organization: Department of Neurology, Washington University School of Medicine, St. Louis, MO 63110, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29566794$$D View this record in MEDLINE/PubMed |
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| Keywords | SILK amyloid Alzheimer’s disease induced pluripotent stem cell stable isotope labeling kinetics production rate tau positron emission tomography phosphorylation human isoform PET |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 AUTHOR CONTRIBUTIONS R.J.B., T.M.M., C.S., and C.M.K. conceived the project. R.J.B., C.S., M.J.C., T.M.M., J.J.-B., M.S., and B.W.P. designed the long-term labeling protocol. J.J.-B. and M.S. recruited the participants. C.S., N.R.B., K.G.M., T.K., and R.J.B. designed and developed the tau SILK method. B.W.P. designed and performed compartmental modeling. K.M.K., K.E.Y., A.B.-N., and B.W.P. conducted the plasma and CSF free 13C6-leucine quantitation. B.A.G. and T.L.S.B. obtained amyloid and tau PET imaging. N.M.K. generated Tau1, Tau12, Tau5, and Tau7 antibodies. C.M.K. generated the iPSC lines and C.S., C.M.K., and N.R.B. designed and performed iPSC-derived neuron SILK experiments. N.R.B. designed and performed MS experiments. N.R.B. and C.S. analyzed and interpreted data and prepared figures. C.S., R.J.B., N.R.B., C.M.K., K.G.M., B.W.P., N.M.K., T.K., T.M.M., and K.E.Y. wrote the paper. |
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| SubjectTerms | Aged Aged, 80 and over Alzheimer Disease - cerebrospinal fluid Alzheimer Disease - metabolism Alzheimer Disease - pathology Alzheimer's disease Amino Acid Sequence amyloid Biomarkers - cerebrospinal fluid Brain Brain - metabolism Brain - pathology Cell Line Cells, Cultured Central nervous system Central Nervous System - metabolism Central Nervous System - pathology Dementia Female human Humans Immunoglobulins induced pluripotent stem cell Induced Pluripotent Stem Cells - metabolism Induced Pluripotent Stem Cells - pathology isoform Isoforms Kinetics Labeling Male Mass spectroscopy Middle Aged Neurons Pathology Peptides PET phosphorylation Physiology Pluripotency positron emission tomography production rate Proteins Senile plaques SILK stable isotope labeling kinetics Stem cells tau Tau protein tau Proteins - cerebrospinal fluid tau Proteins - metabolism |
| Title | Tau Kinetics in Neurons and the Human Central Nervous System |
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