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Roles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration

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Roles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration. / Altmeppen, Hermann C; Prox, Johannes; Puig Martorell, Berta; Dohler, Frank; Falker, Clemens; Krasemann, Susanne; Glatzel, Markus.

in: FEBS J, Jahrgang 280, Nr. 18, 01.09.2013, S. 4338-47.

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

Harvard

Altmeppen, HC, Prox, J, Puig Martorell, B, Dohler, F, Falker, C, Krasemann, S & Glatzel, M 2013, 'Roles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration', FEBS J, Jg. 280, Nr. 18, S. 4338-47. https://doi.org/10.1111/febs.12196

APA

Altmeppen, H. C., Prox, J., Puig Martorell, B., Dohler, F., Falker, C., Krasemann, S., & Glatzel, M. (2013). Roles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration. FEBS J, 280(18), 4338-47. https://doi.org/10.1111/febs.12196

Vancouver

Altmeppen HC, Prox J, Puig Martorell B, Dohler F, Falker C, Krasemann S et al. Roles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration. FEBS J. 2013 Sep 1;280(18):4338-47. https://doi.org/10.1111/febs.12196

Bibtex

@article{8349107ef73648a48aba6f81eeadb790,
title = "Roles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration",
abstract = "The cellular prion protein (PrP(C)) plays important roles in neurodegenerative diseases. First, it is the well-established substrate for the conformational conversion into its pathogenic isoform (PrP(Sc)) giving rise to progressive and fatal prion diseases. Moreover, several recent reports highlight important roles of PrP(C) in other neurodegenerative conditions such as Alzheimer's disease. Since PrP(C) is subject to proteolytic processing, here we discuss the two main cleavage events under physiological conditions, α-cleavage and shedding. We focus on how these cleavages and the resulting fragments may impact prion diseases as well as other neurodegenerative proteinopathies. Finally, we discuss the recently identified sheddase of PrP(C), namely the metalloprotease ADAM10, with regard to therapeutic potential against neurodegenerative diseases.",
keywords = "ADAM Proteins, Alzheimer Disease, Amyloid Precursor Protein Secretases, Amyloid beta-Peptides, Cell Line, Humans, Membrane Proteins, PrPC Proteins, PrPSc Proteins, Prion Diseases, Protein Conformation, Protein Folding, Protein Processing, Post-Translational, Proteolysis, Signal Transduction",
author = "Altmeppen, {Hermann C} and Johannes Prox and {Puig Martorell}, Berta and Frank Dohler and Clemens Falker and Susanne Krasemann and Markus Glatzel",
note = "{\textcopyright} 2013 The Authors Journal compilation {\textcopyright} 2013 FEBS.",
year = "2013",
month = sep,
day = "1",
doi = "10.1111/febs.12196",
language = "English",
volume = "280",
pages = "4338--47",
journal = "FEBS J",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "18",

}

RIS

TY - JOUR

T1 - Roles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration

AU - Altmeppen, Hermann C

AU - Prox, Johannes

AU - Puig Martorell, Berta

AU - Dohler, Frank

AU - Falker, Clemens

AU - Krasemann, Susanne

AU - Glatzel, Markus

N1 - © 2013 The Authors Journal compilation © 2013 FEBS.

PY - 2013/9/1

Y1 - 2013/9/1

N2 - The cellular prion protein (PrP(C)) plays important roles in neurodegenerative diseases. First, it is the well-established substrate for the conformational conversion into its pathogenic isoform (PrP(Sc)) giving rise to progressive and fatal prion diseases. Moreover, several recent reports highlight important roles of PrP(C) in other neurodegenerative conditions such as Alzheimer's disease. Since PrP(C) is subject to proteolytic processing, here we discuss the two main cleavage events under physiological conditions, α-cleavage and shedding. We focus on how these cleavages and the resulting fragments may impact prion diseases as well as other neurodegenerative proteinopathies. Finally, we discuss the recently identified sheddase of PrP(C), namely the metalloprotease ADAM10, with regard to therapeutic potential against neurodegenerative diseases.

AB - The cellular prion protein (PrP(C)) plays important roles in neurodegenerative diseases. First, it is the well-established substrate for the conformational conversion into its pathogenic isoform (PrP(Sc)) giving rise to progressive and fatal prion diseases. Moreover, several recent reports highlight important roles of PrP(C) in other neurodegenerative conditions such as Alzheimer's disease. Since PrP(C) is subject to proteolytic processing, here we discuss the two main cleavage events under physiological conditions, α-cleavage and shedding. We focus on how these cleavages and the resulting fragments may impact prion diseases as well as other neurodegenerative proteinopathies. Finally, we discuss the recently identified sheddase of PrP(C), namely the metalloprotease ADAM10, with regard to therapeutic potential against neurodegenerative diseases.

KW - ADAM Proteins

KW - Alzheimer Disease

KW - Amyloid Precursor Protein Secretases

KW - Amyloid beta-Peptides

KW - Cell Line

KW - Humans

KW - Membrane Proteins

KW - PrPC Proteins

KW - PrPSc Proteins

KW - Prion Diseases

KW - Protein Conformation

KW - Protein Folding

KW - Protein Processing, Post-Translational

KW - Proteolysis

KW - Signal Transduction

U2 - 10.1111/febs.12196

DO - 10.1111/febs.12196

M3 - SCORING: Journal article

C2 - 23413979

VL - 280

SP - 4338

EP - 4347

JO - FEBS J

JF - FEBS J

SN - 1742-464X

IS - 18

ER -