ArticleFrontiers in aging neuroscience2017
Expression of Tau Pathology-Related Proteins in Different Brain Regions: A Molecular Basis of Tau Pathogenesis.
Article in Frontiers in aging neuroscience, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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25 citing papers in PubMed, 58 citations in OpenAlex.
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- Divergent actions of physiological and pathological amyloid-β on synapses in live human brain slice cultures.Nature communications · 2025Article
- Impact of Peptide Transport and Memory Function in the Brain.Nutrients · 2024Review
- Sleep deprivation soon after recovery from synthetic torpor enhances tau protein dephosphorylation in the rat brain.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2024Article
- Therapies for Tau-associated neurodegenerative disorders: targeting molecules, synapses, and cells.Neural regeneration research · 2023Article
- The mitochondrial protein TSPO in Alzheimer's disease: relation to the severity of AD pathology and the neuroinflammatory environment.Journal of neuroinflammation · 2023Article
- Machine learning application for classification of Alzheimer's disease stages usingBiomedical engineering online · 2023Article
- APOE in the bullseye of neurodegenerative diseases: impact of the APOE genotype in Alzheimer's disease pathology and brain diseases.Molecular neurodegeneration · 2022Review
- Pathological and neurophysiological outcomes of seeding human-derived tau pathology in the APP-KI NL-G-F and NL-NL mouse models of Alzheimer's Disease.Acta neuropathologica communications · 2022Article
- The propagation mechanisms of extracellular tau in Alzheimer's disease.Journal of neurology · 2022Review
- Mapping the gene network landscape of Alzheimer's disease through integrating genomics and transcriptomics.PLoS computational biology · 2022Article
- Mouse and Human Tau Expression in Different Brain Areas.Journal of Alzheimer's disease reports · 2022Article
- Characterization of Early Alzheimer's Disease-Like Pathological Alterations in Non-Human Primates with Aging: A Pilot Study.Journal of Alzheimer's disease : JAD · 2022Article
- Phosphorylated Tau protein in the myenteric plexus of the ileum and colon of normothermic rats and during synthetic torpor.Cell and tissue research · 2021Article
- Morphine and HIV-1 Tat interact to cause region-specific hyperphosphorylation of tau in transgenic mice.Neuroscience letters · 2021Article
- Human Tau Isoforms and Proteolysis for Production of Toxic Tau Fragments in Neurodegeneration.Frontiers in neuroscience · 2021Review
- Protein phosphorylation profiling of peripheral nerve regeneration after autologous nerve grafting.Molecular and cellular biochemistry · 2020Article
- Molecular crosstalk between cancer and neurodegenerative diseases.Cellular and molecular life sciences : CMLS · 2020Review
- Characterization ofMolecules (Basel, Switzerland) · 2020Article
- In Vivo Validation of a Small Molecule Inhibitor of Tau Self-Association in htau Mice.Journal of Alzheimer's disease : JAD · 2020Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubule-associated protein tau is hyperphosphorylated and aggregated in affected neurons in Alzheimer disease (AD) brains. The tau pathology starts from the entorhinal cortex (EC), spreads to the hippocampus and frontal and temporal cortices, and finally to all isocortex areas, but the cerebellum is spared from tau lesions. The molecular basis of differential vulnerability of different brain regions to tau pathology is not understood. In the present study, we analyzed brain regional expressions of tau and tau pathology-related proteins. We found that tau was hyperphosphorylated at multiple sites in the frontal cortex (FC), but not in the cerebellum, from AD brain. The level of tau expression in the cerebellum was about 1/4 of that seen in the frontal and temporal cortices in human brain. In the rat brain, the expression level of tau with three microtubule-binding repeats (3R-tau) was comparable in the hippocampus, EC, FC, parietal-temporal cortex (PTC), occipital-temporal cortex (OTC), striatum, thalamus, olfactory bulb (OB) and cerebellum. However, the expression level of 4R-tau was the highest in the EC and the lowest in the cerebellum. Tau phosphatases, kinases, microtubule-related proteins and other tau pathology-related proteins were also expressed in a region-specific manner in the rat brain. These results suggest that higher levels of tau and tau kinases in the EC and low levels of these proteins in the cerebellum may accounts for the vulnerability and resistance of these representative brain regions to the development of tau pathology, respectively. The present study provides the regional expression profiles of tau and tau pathology-related proteins in the brain, which may help understand the brain regional vulnerability to tau pathology in neurodegenerative tauopathies.
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