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Hsp90 co-chaperones, FKBP52 and Aha1, promote tau pathogenesis in aged wild-type mice by Marangelie Criado-Marrero; Niat T. Gebru; Danielle M. Blazier; Lauren A. Gould; Jeremy D. Baker; David Beaulieu-Abdelahad; Laura J. Blair is a Medicine article available to read on EtoBox.
What is Hsp90 co-chaperones, FKBP52 and Aha1, promote tau pathogenesis in aged wild-type mice about?
The microtubule associated protein tau is an intrinsically disordered phosphoprotein that accumulates under pathological conditions leading to formation of neurofibrillary tangles, a hallmark of Alzheimer’s disease (AD). The mechanisms that initiate the accumulation of phospho-tau aggregates and filamentous deposits are largely unknown. In the past, our work and others’ have shown that molecular chaperones play a crucial role in maintaining protein homeostasis and that imbalance in their levels or activity can drive tau pathogenesis. We have found two co-chaperones of the 90 kDa heat shock protein (Hsp90), FK506-binding protein 52 (FKBP52) and the activator of Hsp90 ATPase homolog 1 (Aha1), promote tau aggregation in vitro and in the brains of tau transgenic mice. Based on this, we hypothesized that increased levels of these chaperones could promote tau misfolding and accumulation in the brains of aged wild-type mice. We tested this hypothesis by overexpressing Aha1, FKBP52, or mCherry (control) proteins in the hippocampus of 9-month-old wild-type mice. After 7 months of expression, mice were evaluated for cognitive and pathological changes. Our results show that FKBP52 overexpress
Who reads Hsp90 co-chaperones, FKBP52 and Aha1, promote tau pathogenesis in aged wild-type mice?
It is typically read by researchers, students, and practitioners in Medicine.
- Author
- Marangelie Criado-Marrero; Niat T. Gebru; Danielle M. Blazier; Lauren A. Gould; Jeremy D. Baker; David Beaulieu-Abdelahad; Laura J. Blair
- Publisher
- Springer Science and Business Media LLC
- Published
- 2021
- Language
- EN
- Field
- Medicine (Health Sciences)