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Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice

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Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice. / Puig Martorell, Berta; Altmeppen, Hermann C; Ulbrich, Sarah; Linsenmeier, Luise; Krasemann, Susanne; Chakroun, Karima; Acevedo-Morantes, Claudia Y; Wille, Holger; Tatzelt, Jörg; Glatzel, Markus.

In: SCI REP-UK, Vol. 6, 2016, p. 24970.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Puig Martorell, B, Altmeppen, HC, Ulbrich, S, Linsenmeier, L, Krasemann, S, Chakroun, K, Acevedo-Morantes, CY, Wille, H, Tatzelt, J & Glatzel, M 2016, 'Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice', SCI REP-UK, vol. 6, pp. 24970. https://doi.org/10.1038/srep24970

APA

Puig Martorell, B., Altmeppen, H. C., Ulbrich, S., Linsenmeier, L., Krasemann, S., Chakroun, K., Acevedo-Morantes, C. Y., Wille, H., Tatzelt, J., & Glatzel, M. (2016). Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice. SCI REP-UK, 6, 24970. https://doi.org/10.1038/srep24970

Vancouver

Puig Martorell B, Altmeppen HC, Ulbrich S, Linsenmeier L, Krasemann S, Chakroun K et al. Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice. SCI REP-UK. 2016;6:24970. https://doi.org/10.1038/srep24970

Bibtex

@article{daaf522f64274e4cace99b6466d8a935,
title = "Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice",
abstract = "Misfolding of proteins in the biosynthetic pathway in neurons may cause disturbed protein homeostasis and neurodegeneration. The prion protein (PrP(C)) is a GPI-anchored protein that resides at the plasma membrane and may be misfolded to PrP(Sc) leading to prion diseases. We show that a deletion in the C-terminal domain of PrP(C) (PrPΔ214-229) leads to partial retention in the secretory pathway causing a fatal neurodegenerative disease in mice that is partially rescued by co-expression of PrP(C). Transgenic (Tg(PrPΔ214-229)) mice show extensive neuronal loss in hippocampus and cerebellum and activation of p38-MAPK. In cell culture under stress conditions, PrPΔ214-229 accumulates in the Golgi apparatus possibly representing transit to the Rapid ER Stress-induced ExporT (RESET) pathway together with p38-MAPK activation. Here we describe a novel pathway linking retention of a GPI-anchored protein in the early secretory pathway to p38-MAPK activation and a neurodegenerative phenotype in transgenic mice.",
author = "{Puig Martorell}, Berta and Altmeppen, {Hermann C} and Sarah Ulbrich and Luise Linsenmeier and Susanne Krasemann and Karima Chakroun and Acevedo-Morantes, {Claudia Y} and Holger Wille and J{\"o}rg Tatzelt and Markus Glatzel",
year = "2016",
doi = "10.1038/srep24970",
language = "English",
volume = "6",
pages = "24970",
journal = "SCI REP-UK",
issn = "2045-2322",
publisher = "NATURE PUBLISHING GROUP",

}

RIS

TY - JOUR

T1 - Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice

AU - Puig Martorell, Berta

AU - Altmeppen, Hermann C

AU - Ulbrich, Sarah

AU - Linsenmeier, Luise

AU - Krasemann, Susanne

AU - Chakroun, Karima

AU - Acevedo-Morantes, Claudia Y

AU - Wille, Holger

AU - Tatzelt, Jörg

AU - Glatzel, Markus

PY - 2016

Y1 - 2016

N2 - Misfolding of proteins in the biosynthetic pathway in neurons may cause disturbed protein homeostasis and neurodegeneration. The prion protein (PrP(C)) is a GPI-anchored protein that resides at the plasma membrane and may be misfolded to PrP(Sc) leading to prion diseases. We show that a deletion in the C-terminal domain of PrP(C) (PrPΔ214-229) leads to partial retention in the secretory pathway causing a fatal neurodegenerative disease in mice that is partially rescued by co-expression of PrP(C). Transgenic (Tg(PrPΔ214-229)) mice show extensive neuronal loss in hippocampus and cerebellum and activation of p38-MAPK. In cell culture under stress conditions, PrPΔ214-229 accumulates in the Golgi apparatus possibly representing transit to the Rapid ER Stress-induced ExporT (RESET) pathway together with p38-MAPK activation. Here we describe a novel pathway linking retention of a GPI-anchored protein in the early secretory pathway to p38-MAPK activation and a neurodegenerative phenotype in transgenic mice.

AB - Misfolding of proteins in the biosynthetic pathway in neurons may cause disturbed protein homeostasis and neurodegeneration. The prion protein (PrP(C)) is a GPI-anchored protein that resides at the plasma membrane and may be misfolded to PrP(Sc) leading to prion diseases. We show that a deletion in the C-terminal domain of PrP(C) (PrPΔ214-229) leads to partial retention in the secretory pathway causing a fatal neurodegenerative disease in mice that is partially rescued by co-expression of PrP(C). Transgenic (Tg(PrPΔ214-229)) mice show extensive neuronal loss in hippocampus and cerebellum and activation of p38-MAPK. In cell culture under stress conditions, PrPΔ214-229 accumulates in the Golgi apparatus possibly representing transit to the Rapid ER Stress-induced ExporT (RESET) pathway together with p38-MAPK activation. Here we describe a novel pathway linking retention of a GPI-anchored protein in the early secretory pathway to p38-MAPK activation and a neurodegenerative phenotype in transgenic mice.

U2 - 10.1038/srep24970

DO - 10.1038/srep24970

M3 - SCORING: Journal article

C2 - 27117504

VL - 6

SP - 24970

JO - SCI REP-UK

JF - SCI REP-UK

SN - 2045-2322

ER -