Prion protein oligomers cause neuronal cytoskeletal damage in rapidly progressive Alzheimer’s disease
2021 | journal article; research paper. A publication with affiliation to the University of Göttingen.
Jump to: Cite & Linked | Documents & Media | Details | Version history
Cite this publication
Prion protein oligomers cause neuronal cytoskeletal damage in rapidly progressive Alzheimer’s disease
Shafiq, M.; Zafar, S.; Younas, N.; Noor, A.; Puig, B.; Altmeppen, H. C. & Schmitz, M. et al. (2021)
Molecular Neurodegeneration, 16(1) art. 11. DOI: https://doi.org/10.1186/s13024-021-00422-x
Documents & Media
13024_2021_Article_422.pdf2.09 MBAdobe PDFSupplementary information155.1 kBMicrosoft Word XMLSupplementary information15.43 kBMicrosoft Excel XMLSupplementary information22.54 kBMicrosoft Excel XMLSupplementary information101.67 kBMicrosoft Excel XMLSupplementary information3.86 MBMicrosoft Excel XMLSupplementary information2.92 MBMicrosoft Excel XMLSupplementary information684.88 kBMicrosoft Excel XMLs13024-021-00422-x.pdf2.09 MBUnknown
Details
- Authors
- Shafiq, Mohsin; Zafar, Saima; Younas, Neelam; Noor, Aneeqa; Puig, Berta; Altmeppen, Hermann Clemens; Schmitz, Matthias; Matschke, Jakob; Ferrer, Isidre; Zerr, Inga; Glatzel, Markus
- Abstract
- Abstract Background High-density oligomers of the prion protein (HDPs) have previously been identified in brain tissues of patients with rapidly progressive Alzheimer’s disease (rpAD). The current investigation aims at identifying interacting partners of HDPs in the rpAD brains to unravel the pathological involvement of HDPs in the rapid progression. Methods HDPs from the frontal cortex tissues of rpAD brains were isolated using sucrose density gradient centrifugation. Proteins interacting with HDPs were identified by co-immunoprecipitation coupled with mass spectrometry. Further verifications were carried out using proteomic tools, immunoblotting, and confocal laser scanning microscopy. Results We identified rpAD-specific HDP-interactors, including the growth arrest specific 2-like 2 protein (G2L2). Intriguingly, rpAD-specific disturbances were found in the localization of G2L2 and its associated proteins i.e., the end binding protein 1, α-tubulin, and β-actin. Discussion The results show the involvement of HDPs in the destabilization of the neuronal actin/tubulin infrastructure. We consider this disturbance to be a contributing factor for the rapid progression in rpAD.
- Issue Date
- 2021
- Journal
- Molecular Neurodegeneration
- Organization
- Klinik für Neurologie
- eISSN
- 1750-1326
- Language
- English
- Sponsor
- Open-Access-Finanzierung durch die Universitätsmedizin Göttingen 2021