Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
Abstract
We have determined the sequences of isoforms of human tau protein, which differ from previously reported forms by insertions of 29 or 58 amino acids in the amino-terminal region. Complementary DNA cloning shows that the insertions occur in combination with both three and four tandem repeats. RNAase protection assays indicate that transcripts encoding isoforms with the insertions are expressed in an adult-specific manner. Transcripts encoding four tandem repeats are also expressed in an adult-specific manner, whereas mRNAs encoding three tandem repeats are expressed throughout life, including in fetal brain. The levels of transcripts encoding the 29 or 58 amino acid inserts were not significantly changed in cerebral cortex from patients with Alzheimer's disease. Antisera raised against synthetic peptides corresponding to these different human tau isoforms demonstrate that multiple tau protein isoforms are incorporated into the neurofibrillary tangles of Alzheimer's disease.
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Alternative splice variation including exons 2, 3, and 10 generates up to six differing tau isoform variants in the human brain.
“Alternative splice variation including exons 2, 3, and 10 generates up to six differing tau isoform variants in the human brain [106, 107].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [106]
Tau protein is a microtubule-associated protein widely distributed in the central nervous system and maintains and regulates neuronal morphology and function.
“Tau protein is a microtubule-associated protein that is widely distributed in the central nervous system and maintains and regulates neuronal morphology and function.”
From Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review (2024) · cites this paper as [3]
In AD and PART, tau aggregates are a mixture of three-repeat and four-repeat tau isoforms, whereas four-repeat sequences dominate in PSP and CBD and three-repeat sequences predominate in Pick disease.
“In AD and PART, the tau aggregates are a mixture of three-repeat and four-repeat tau isoforms, whereas four-repeat sequences dominate in PSP and CBD and three-repeat sequences predominate in Pick disease14,18,19,21.”
From Tau-targeting therapies for Alzheimer disease (2018) · cites this paper as [19]
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References 32 · Cited by 2,492
- Authors
- Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1989-10
- Volume
- 3
- Issue
- 4
- Pages
- 519-526
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2159377066
- Cited by
- 2,492
- References
- 32
- Citations by year
- 2026: 83 · 2025: 103 · 2024: 112 · 2023: 122 · 2022: 124 · 2021: 148 · 2020: 109 · 2019: 108 · 2018: 104 · 2017: 76 · 2016: 60 · 2015: 70 · 2014: 64 · 2013: 57 · 2012: 74
- FWCI
- 21.18
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, tau isoforms, Alzheimer's disease, neurofibrillary tangles, tandem repeats, alternative splicing, cerebral cortex, microtubule-associated proteins
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Humans, Immunologic Techniques, Isomerism, Microtubule-Associated Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Neurofibrils, RNA, Messenger, Staining and Labeling, tau Proteins
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