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Neurodegenerative diseases, including Alzheimer's disease (AD), are closely related to the build-up of tau proteins that are abnormally aggregation in the brain.
unbinded micro-tube-related protein tau (MAPT) is physiologically present in the form of soluble non-structural proteins, but under pathogenic conditions, tau accumulates in AD and other tau diseases into insoluble β-folded amyloid-rich primary fiber encases.
note that these packages are extensively translated and modified, with significant excessive phosphorylation.
in AD, the accumulation of tau in neurogenic fibrous tangles (NFTs) was significantly associated with cognitive impairment, brain atrophy, and neuron loss.
, it is also recognized that tau encases may remain stable in human neurons for decades.
recent evidence that neuron function was not impaired in tau genetically modified mice with NFT pathology.
Although little is known about the mechanisms of tau accumulation and tau-related neurodegenerative lesions, genetics, models, and pathology studies support tau's therapeutic targeting in neurodegenerative diseases, but information on tau envelin formation and removal dynamics remains limited.
This study used the expression of the P301L/S320F tau protein in human wild type, P301L and pre-aggregated human wild type, P301L and pre-aggregated Dendra2 marker of rAAV vectors, and evaluated the dynamics of tau enumeration in organ-type brain chip culture (BSC) models using long-term optical pulse markers without adding exogenous tau raw fiber seeds.
studies have shown that tau encases are usually formed in the Tau disease BSC model at 12-96h.
unexpectedly, tau in the package has a significant turnover, with an average half-life of about 1 week when the package is newly formed.
When BSC containing the wrapper ages over a long period of time in culture, the tau encaser continues to turn around, but after 1 month and 2 months of culture, its half-life increases to 2 weeks and 3 weeks, respectively.
a single tau encaser can be long-lived and can last for months in these BSC models, even longer in the human brain.
, however, the data in this paper show that the tau wrapper is not static, but has a dynamic structure with perceptible turnover.
, understanding the cellular processes that mediate this encased transformation may lead to new treatment strategies that may reverse the formation of pathological tau encases.
Croft, C.L., Goodwin, M.S., Ryu, D.H. et al. Photodynamic studies reveal rapid formation and appreciable turnover of tau inclusions. Acta Neuropathol 141, 359–381 (2021). MedSci Original Source: MedSci Original Copyright Notice: All text, images and audio and video materials on this website that indicate "Source: Mets Medicine" or "Source: MedSci Original" are owned by Mets Medicine and are not authorized to be reproduced by any media, website or individual, and are authorized to be reproduced with the words "Source: Mets Medicine".
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