PortalPublikationenPrion protein oligomers cause neuronal cytoskeletal damage i...

Prion protein oligomers cause neuronal cytoskeletal damage in rapidly progressive Alzheimer's disease

Standard

Prion protein oligomers cause neuronal cytoskeletal damage in rapidly progressive Alzheimer's disease. / Shafiq, Mohsin; Zafar, Saima; Younas, Neelam; Noor, Aneeqa; Puig, Berta; Altmeppen, Hermann Clemens; Schmitz, Matthias; Matschke, Jakob; Ferrer, Isidre; Glatzel, Markus; Zerr, Inga.

in: MOL NEURODEGENER, Jahrgang 16, Nr. 1, 11, 22.02.2021.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Shafiq, M, Zafar, S, Younas, N, Noor, A, Puig, B, Altmeppen, HC, Schmitz, M, Matschke, J, Ferrer, I, Glatzel, M & Zerr, I 2021, 'Prion protein oligomers cause neuronal cytoskeletal damage in rapidly progressive Alzheimer's disease', MOL NEURODEGENER, Jg. 16, Nr. 1, 11. https://doi.org/10.1186/s13024-021-00422-x

APA

Shafiq, M., Zafar, S., Younas, N., Noor, A., Puig, B., Altmeppen, H. C., Schmitz, M., Matschke, J., Ferrer, I., Glatzel, M., & Zerr, I. (2021). Prion protein oligomers cause neuronal cytoskeletal damage in rapidly progressive Alzheimer's disease. MOL NEURODEGENER, 16(1), [11]. https://doi.org/10.1186/s13024-021-00422-x

Vancouver

Shafiq M, Zafar S, Younas N, Noor A, Puig B, Altmeppen HC et al. Prion protein oligomers cause neuronal cytoskeletal damage in rapidly progressive Alzheimer's disease. MOL NEURODEGENER. 2021 Feb 22;16(1). 11. https://doi.org/10.1186/s13024-021-00422-x

Bibtex

@article{32b1a0fe2669467ab4706ecf0a026c3e,
title = "Prion protein oligomers cause neuronal cytoskeletal damage in rapidly progressive Alzheimer's disease",
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.",
author = "Mohsin Shafiq and Saima Zafar and Neelam Younas and Aneeqa Noor and Berta Puig and Altmeppen, {Hermann Clemens} and Matthias Schmitz and Jakob Matschke and Isidre Ferrer and Markus Glatzel and Inga Zerr",
year = "2021",
month = feb,
day = "22",
doi = "10.1186/s13024-021-00422-x",
language = "English",
volume = "16",
journal = "MOL NEURODEGENER",
issn = "1750-1326",
publisher = "BioMed Central Ltd.",
number = "1",

}

RIS

TY - JOUR

T1 - Prion protein oligomers cause neuronal cytoskeletal damage in rapidly progressive Alzheimer's disease

AU - Shafiq, Mohsin

AU - Zafar, Saima

AU - Younas, Neelam

AU - Noor, Aneeqa

AU - Puig, Berta

AU - Altmeppen, Hermann Clemens

AU - Schmitz, Matthias

AU - Matschke, Jakob

AU - Ferrer, Isidre

AU - Glatzel, Markus

AU - Zerr, Inga

PY - 2021/2/22

Y1 - 2021/2/22

N2 - 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.

AB - 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.

U2 - 10.1186/s13024-021-00422-x

DO - 10.1186/s13024-021-00422-x

M3 - SCORING: Journal article

C2 - 33618749

VL - 16

JO - MOL NEURODEGENER

JF - MOL NEURODEGENER

SN - 1750-1326

IS - 1

M1 - 11

ER -