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The GPI-anchoring of PrP: Implications in sorting and pathogenesis

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The GPI-anchoring of PrP: Implications in sorting and pathogenesis. / Puig Martorell, Berta; Altmeppen, Hermann; Glatzel, Markus.

in: PRION, Jahrgang 8, Nr. 1, 01.01.2014, S. 11-18.

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

Harvard

Puig Martorell, B, Altmeppen, H & Glatzel, M 2014, 'The GPI-anchoring of PrP: Implications in sorting and pathogenesis', PRION, Jg. 8, Nr. 1, S. 11-18.

APA

Puig Martorell, B., Altmeppen, H., & Glatzel, M. (2014). The GPI-anchoring of PrP: Implications in sorting and pathogenesis. PRION, 8(1), 11-18.

Vancouver

Puig Martorell B, Altmeppen H, Glatzel M. The GPI-anchoring of PrP: Implications in sorting and pathogenesis. PRION. 2014 Jan 1;8(1):11-18.

Bibtex

@article{9b98079b70574d4ba6dd2e1311dd727e,
title = "The GPI-anchoring of PrP: Implications in sorting and pathogenesis",
abstract = "The cellular prion protein (PrP(C)) is an N-glycosylated GPI-anchored protein usually present in lipid rafts with numerous putative functions. When it changes its conformation to a pathological isoform (then referred to as PrP(Sc)), it is an essential part of the prion, the agent causing fatal and transmissible neurodegenerative prion diseases. There is growing evidence that toxicity and neuronal damage on the one hand and propagation/infectivity on the other hand are two distinct processes of the disease and that the GPI-anchor attachment of PrP(C) and PrP(Sc) plays an important role in protein localization and in neurotoxicity. Here we review how the signal sequence of the GPI-anchor matters in PrP(C) localization, how an altered cellular localization of PrP(C) or differences in GPI-anchor composition can affect prion infection, and we discuss through which mechanisms changes on the anchorage of PrP(C) can modify the disease process.",
author = "{Puig Martorell}, Berta and Hermann Altmeppen and Markus Glatzel",
year = "2014",
month = jan,
day = "1",
language = "English",
volume = "8",
pages = "11--18",
journal = "PRION",
issn = "1933-6896",
publisher = "LANDES BIOSCIENCE",
number = "1",

}

RIS

TY - JOUR

T1 - The GPI-anchoring of PrP: Implications in sorting and pathogenesis

AU - Puig Martorell, Berta

AU - Altmeppen, Hermann

AU - Glatzel, Markus

PY - 2014/1/1

Y1 - 2014/1/1

N2 - The cellular prion protein (PrP(C)) is an N-glycosylated GPI-anchored protein usually present in lipid rafts with numerous putative functions. When it changes its conformation to a pathological isoform (then referred to as PrP(Sc)), it is an essential part of the prion, the agent causing fatal and transmissible neurodegenerative prion diseases. There is growing evidence that toxicity and neuronal damage on the one hand and propagation/infectivity on the other hand are two distinct processes of the disease and that the GPI-anchor attachment of PrP(C) and PrP(Sc) plays an important role in protein localization and in neurotoxicity. Here we review how the signal sequence of the GPI-anchor matters in PrP(C) localization, how an altered cellular localization of PrP(C) or differences in GPI-anchor composition can affect prion infection, and we discuss through which mechanisms changes on the anchorage of PrP(C) can modify the disease process.

AB - The cellular prion protein (PrP(C)) is an N-glycosylated GPI-anchored protein usually present in lipid rafts with numerous putative functions. When it changes its conformation to a pathological isoform (then referred to as PrP(Sc)), it is an essential part of the prion, the agent causing fatal and transmissible neurodegenerative prion diseases. There is growing evidence that toxicity and neuronal damage on the one hand and propagation/infectivity on the other hand are two distinct processes of the disease and that the GPI-anchor attachment of PrP(C) and PrP(Sc) plays an important role in protein localization and in neurotoxicity. Here we review how the signal sequence of the GPI-anchor matters in PrP(C) localization, how an altered cellular localization of PrP(C) or differences in GPI-anchor composition can affect prion infection, and we discuss through which mechanisms changes on the anchorage of PrP(C) can modify the disease process.

M3 - SCORING: Journal article

C2 - 24509692

VL - 8

SP - 11

EP - 18

JO - PRION

JF - PRION

SN - 1933-6896

IS - 1

ER -