期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 22, 期 11, 页码 -出版社
MDPI
DOI: 10.3390/ijms22115768
关键词
Tau; PolDIP2; amyloid
资金
- Swedish Medical Research Council
- JSPS Overseas Research Fellowship [201860287]
- Knut and Alice Wallenberg Foundation [KAW 2019.0307]
- Swedish Research Council [2018-02781]
- Kempe Foundation [JCK-1831]
- Forskningsstrategiska medel
- Medical Faculty, Umea University
- Insamlingsstiftelsen
- Swedish Research Council [2018-02781] Funding Source: Swedish Research Council
The study demonstrates that PolDIP2 interacts with Tau and inhibits Tau aggregation and amyloid fibril growth in vitro, suggesting it as a potential regulator for future Tau-targeting therapeutics.
A central characteristic of Alzheimer's disease (AD) and other tauopathies is the accumulation of aggregated and misfolded Tau deposits in the brain. Tau-targeting therapies for AD have been unsuccessful in patients to date. Here we show that human polymerase delta-interacting protein 2 (PolDIP2) interacts with Tau. With a set of complementary methods, including thioflavin-T-based aggregation kinetic assays, Tau oligomer-specific dot-blot analysis, and single oligomer/fibril analysis by atomic force microscopy, we demonstrate that PolDIP2 inhibits Tau aggregation and amyloid fibril growth in vitro. The identification of PolDIP2 as a potential regulator of cellular Tau aggregation should be considered for future Tau-targeting therapeutics.
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