Cleavage of Tau by calpain in Alzheimer's disease: the quest for the toxic 17 kD fragment
Abstract
The amyloid cascade hypothesis of Alzheimer's disease (AD) posits that the generation of β-amyloid (Aβ) triggers Tau neurofibrillary pathology. Recently a "17 kD" calpain-induced Tau fragment, comprising residues 45-230 (molecular weight [MW], 18.7 kD), was proposed to mediate Aβ-induced toxicity. Here, we demonstrate that the "17 kD" fragment is actually much smaller, containing residues 125-230 (molecular weight, 10.7 kD). Inducing Tau phosphorylation by okadaic acid or mimicking phosphorylation by Glu mutations at the epitopes of Alzheimer-diagnostic antibodies AT100/AT8/PHF1 could not prevent the generation of this fragment. The fragment can be induced not only by Aβ oligomers, but also by other cell stressors, e.g., thapsigargin (a Ca(2+)-ATPase inhibitor) or glutamate (an excitatory neurotransmitter). However, overexpression of neither Tau(45-230) nor Tau(125-230) fragment is toxic to Chinese hamster ovary (CHO) cells, neuroblastoma cells (N2a) or primary hippocampal neurons. Finally, the calpain-induced fragment can be observed both in Alzheimer's disease brains and in control normal human brains. We conclude that the 17 kD Tau fragment is not a mediator of Aβ-induced toxicity, leaving open the possibility that upstream calpain activation might cause both Tau fragmentation and toxicity.
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Calpain-2 cleaves tau at Arg230.
“while calpain-2 cleaves tau at Arg230 [202–206].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [205]
Calpain-1 cleaves tau at Lys44, Arg230, Arg242, Gly323, and Gly326.
“Calpain-1 cleaves tau at Lys44, Arg230, Arg242, Gly323, and Gly326”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [205]
Tau45-230 is neurotoxic, and can induce synaptic and cognitive impairment.
“a recent study utilizing tau45–230 transgenic mice indicates that tau45–230 is neurotoxic, and can induce synaptic and cognitive impairment [204, 205, 209].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [205]
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- Authors
- Garg, S., Timm, T., Mandelkow, E.-M., Mandelkow, E., & Wang, Y.
- Affiliations
- Max Planck Unit for Structural Molecular Biology (DE)
- Center of Advanced European Studies and Research (DE)
- Corresponding author
- Mandelkow, Eckhard
- Wang, Yipeng
- Venue
- Neurobiology of Aging
- Publisher
- Elsevier BV
- Published
- 2011-01
- Volume
- 32
- Issue
- 1
- Pages
- 1-14
- ISSN
- 0197-4580 (ISSN-L)
- OpenAlex
- W2169388089
- Cited by
- 103
- References
- 58
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 1 · 2023: 7 · 2022: 5 · 2021: 6 · 2020: 8 · 2019: 5 · 2018: 7 · 2017: 5 · 2016: 10 · 2015: 6 · 2014: 12 · 2013: 8 · 2012: 9
- FWCI
- 5.85
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neurobiology of Aging (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- DZNE Pub (submittedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau protein, calpain, Alzheimer's disease, tau phosphorylation, amyloid-beta, amyloid hypothesis, neurofibrillary tangles, thapsigargin, glutamate excitotoxicity, tau cleavage, neurotoxicity
- MeSH terms
- Adducins, Aged, Aged, 80 and over, Alzheimer Disease, Animals, Calmodulin-Binding Proteins, Calpain, Cell Count, Cerebral Cortex, Cricetulus, Embryo, Mammalian, Enzyme Inhibitors, Cricetinae, Humans, Molecular Weight, Mutation, Neurons, Peptide Fragments, Peptides, Phosphorylation, Transfection, Amyloid beta-Peptides, tau Proteins, Glutamic Acid, Thapsigargin, In Situ Nick-End Labeling, Green Fluorescent Proteins, Rats
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