PortalPublikationenThe sheddase ADAM10 is a potent modulator of prion disease

The sheddase ADAM10 is a potent modulator of prion disease

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The sheddase ADAM10 is a potent modulator of prion disease. / Altmeppen, Hermann C; Prox, Johannes; Krasemann, Susanne; Puig Martorell, Berta; Kruszewski, Katharina; Dohler, Frank; Bernreuther, Christian; Hoxha, Ana; Linsenmeier, Luise; Sikorska, Beata; Liberski, Pawel P; Bartsch, Udo; Saftig, Paul; Glatzel, Markus.

in: ELIFE, Jahrgang 4, 01.01.2015.

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

Harvard

Altmeppen, HC, Prox, J, Krasemann, S, Puig Martorell, B, Kruszewski, K, Dohler, F, Bernreuther, C, Hoxha, A, Linsenmeier, L, Sikorska, B, Liberski, PP, Bartsch, U, Saftig, P & Glatzel, M 2015, 'The sheddase ADAM10 is a potent modulator of prion disease', ELIFE, Jg. 4. https://doi.org/10.7554/eLife.04260

APA

Altmeppen, H. C., Prox, J., Krasemann, S., Puig Martorell, B., Kruszewski, K., Dohler, F., Bernreuther, C., Hoxha, A., Linsenmeier, L., Sikorska, B., Liberski, P. P., Bartsch, U., Saftig, P., & Glatzel, M. (2015). The sheddase ADAM10 is a potent modulator of prion disease. ELIFE, 4. https://doi.org/10.7554/eLife.04260

Vancouver

Altmeppen HC, Prox J, Krasemann S, Puig Martorell B, Kruszewski K, Dohler F et al. The sheddase ADAM10 is a potent modulator of prion disease. ELIFE. 2015 Jan 1;4. https://doi.org/10.7554/eLife.04260

Bibtex

@article{e53e59d1099f4b768b91c3f80dca6a09,
title = "The sheddase ADAM10 is a potent modulator of prion disease",
abstract = "The prion protein (PrP(C)) is highly expressed in the nervous system and critically involved in prion diseases where it misfolds into pathogenic PrP(Sc). Moreover, it has been suggested as a receptor mediating neurotoxicity in common neurodegenerative proteinopathies such as Alzheimer's disease. PrP(C) is shed at the plasma membrane by the metalloprotease ADAM10, yet the impact of this on prion disease remains enigmatic. Employing conditional knockout mice, we show that depletion of ADAM10 in forebrain neurons leads to posttranslational increase of PrP(C) levels. Upon prion infection of these mice, clinical, biochemical, and morphological data reveal that lack of ADAM10 significantly reduces incubation times and increases PrP(Sc) formation. In contrast, spatiotemporal analysis indicates that absence of shedding impairs spread of prion pathology. Our data support a dual role for ADAM10-mediated shedding and highlight the role of proteolytic processing in prion disease.",
author = "Altmeppen, {Hermann C} and Johannes Prox and Susanne Krasemann and {Puig Martorell}, Berta and Katharina Kruszewski and Frank Dohler and Christian Bernreuther and Ana Hoxha and Luise Linsenmeier and Beata Sikorska and Liberski, {Pawel P} and Udo Bartsch and Paul Saftig and Markus Glatzel",
year = "2015",
month = jan,
day = "1",
doi = "10.7554/eLife.04260",
language = "English",
volume = "4",
journal = "ELIFE",
issn = "2050-084X",
publisher = "eLife Sciences Publications",

}

RIS

TY - JOUR

T1 - The sheddase ADAM10 is a potent modulator of prion disease

AU - Altmeppen, Hermann C

AU - Prox, Johannes

AU - Krasemann, Susanne

AU - Puig Martorell, Berta

AU - Kruszewski, Katharina

AU - Dohler, Frank

AU - Bernreuther, Christian

AU - Hoxha, Ana

AU - Linsenmeier, Luise

AU - Sikorska, Beata

AU - Liberski, Pawel P

AU - Bartsch, Udo

AU - Saftig, Paul

AU - Glatzel, Markus

PY - 2015/1/1

Y1 - 2015/1/1

N2 - The prion protein (PrP(C)) is highly expressed in the nervous system and critically involved in prion diseases where it misfolds into pathogenic PrP(Sc). Moreover, it has been suggested as a receptor mediating neurotoxicity in common neurodegenerative proteinopathies such as Alzheimer's disease. PrP(C) is shed at the plasma membrane by the metalloprotease ADAM10, yet the impact of this on prion disease remains enigmatic. Employing conditional knockout mice, we show that depletion of ADAM10 in forebrain neurons leads to posttranslational increase of PrP(C) levels. Upon prion infection of these mice, clinical, biochemical, and morphological data reveal that lack of ADAM10 significantly reduces incubation times and increases PrP(Sc) formation. In contrast, spatiotemporal analysis indicates that absence of shedding impairs spread of prion pathology. Our data support a dual role for ADAM10-mediated shedding and highlight the role of proteolytic processing in prion disease.

AB - The prion protein (PrP(C)) is highly expressed in the nervous system and critically involved in prion diseases where it misfolds into pathogenic PrP(Sc). Moreover, it has been suggested as a receptor mediating neurotoxicity in common neurodegenerative proteinopathies such as Alzheimer's disease. PrP(C) is shed at the plasma membrane by the metalloprotease ADAM10, yet the impact of this on prion disease remains enigmatic. Employing conditional knockout mice, we show that depletion of ADAM10 in forebrain neurons leads to posttranslational increase of PrP(C) levels. Upon prion infection of these mice, clinical, biochemical, and morphological data reveal that lack of ADAM10 significantly reduces incubation times and increases PrP(Sc) formation. In contrast, spatiotemporal analysis indicates that absence of shedding impairs spread of prion pathology. Our data support a dual role for ADAM10-mediated shedding and highlight the role of proteolytic processing in prion disease.

U2 - 10.7554/eLife.04260

DO - 10.7554/eLife.04260

M3 - SCORING: Journal article

C2 - 25654651

VL - 4

JO - ELIFE

JF - ELIFE

SN - 2050-084X

ER -