PortalPublikationenShedding of APP limits its synaptogenic activity and cell ad...

Shedding of APP limits its synaptogenic activity and cell adhesion properties

Standard

Shedding of APP limits its synaptogenic activity and cell adhesion properties. / Stahl, Ronny; Schilling, Sandra; Soba, Peter; Rupp, Carsten; Hartmann, Tobias; Wagner, Katja; Merdes, Gunter; Eggert, Simone; Kins, Stefan.

in: FRONT CELL NEUROSCI, Jahrgang 8, 01.01.2014, S. 410.

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

Harvard

Stahl, R, Schilling, S, Soba, P, Rupp, C, Hartmann, T, Wagner, K, Merdes, G, Eggert, S & Kins, S 2014, 'Shedding of APP limits its synaptogenic activity and cell adhesion properties', FRONT CELL NEUROSCI, Jg. 8, S. 410. https://doi.org/10.3389/fncel.2014.00410

APA

Stahl, R., Schilling, S., Soba, P., Rupp, C., Hartmann, T., Wagner, K., Merdes, G., Eggert, S., & Kins, S. (2014). Shedding of APP limits its synaptogenic activity and cell adhesion properties. FRONT CELL NEUROSCI, 8, 410. https://doi.org/10.3389/fncel.2014.00410

Vancouver

Stahl R, Schilling S, Soba P, Rupp C, Hartmann T, Wagner K et al. Shedding of APP limits its synaptogenic activity and cell adhesion properties. FRONT CELL NEUROSCI. 2014 Jan 1;8:410. https://doi.org/10.3389/fncel.2014.00410

Bibtex

@article{52a5093b225b43d0ab21df57a458201b,
title = "Shedding of APP limits its synaptogenic activity and cell adhesion properties",
abstract = "The amyloid precursor protein (APP) plays a central role in Alzheimer's disease (AD) and has essential synapse promoting functions. Synaptogenic activity as well as cell adhesion properties of APP presumably depend on trans-cellular dimerization via its extracellular domain. Since neuronal APP is extensively processed by secretases, it raises the question if APP shedding affects its cell adhesion and synaptogenic properties. We show that inhibition of APP shedding using cleavage deficient forms of APP or a dominant negative α-secretase strongly enhanced its cell adhesion and synaptogenic activity suggesting that synapse promoting function of APP is tightly regulated by α-secretase mediated processing, similar to other trans-cellular synaptic adhesion molecules.",
author = "Ronny Stahl and Sandra Schilling and Peter Soba and Carsten Rupp and Tobias Hartmann and Katja Wagner and Gunter Merdes and Simone Eggert and Stefan Kins",
year = "2014",
month = jan,
day = "1",
doi = "10.3389/fncel.2014.00410",
language = "English",
volume = "8",
pages = "410",
journal = "FRONT CELL NEUROSCI",
issn = "1662-5102",
publisher = "Frontiers Media",

}

RIS

TY - JOUR

T1 - Shedding of APP limits its synaptogenic activity and cell adhesion properties

AU - Stahl, Ronny

AU - Schilling, Sandra

AU - Soba, Peter

AU - Rupp, Carsten

AU - Hartmann, Tobias

AU - Wagner, Katja

AU - Merdes, Gunter

AU - Eggert, Simone

AU - Kins, Stefan

PY - 2014/1/1

Y1 - 2014/1/1

N2 - The amyloid precursor protein (APP) plays a central role in Alzheimer's disease (AD) and has essential synapse promoting functions. Synaptogenic activity as well as cell adhesion properties of APP presumably depend on trans-cellular dimerization via its extracellular domain. Since neuronal APP is extensively processed by secretases, it raises the question if APP shedding affects its cell adhesion and synaptogenic properties. We show that inhibition of APP shedding using cleavage deficient forms of APP or a dominant negative α-secretase strongly enhanced its cell adhesion and synaptogenic activity suggesting that synapse promoting function of APP is tightly regulated by α-secretase mediated processing, similar to other trans-cellular synaptic adhesion molecules.

AB - The amyloid precursor protein (APP) plays a central role in Alzheimer's disease (AD) and has essential synapse promoting functions. Synaptogenic activity as well as cell adhesion properties of APP presumably depend on trans-cellular dimerization via its extracellular domain. Since neuronal APP is extensively processed by secretases, it raises the question if APP shedding affects its cell adhesion and synaptogenic properties. We show that inhibition of APP shedding using cleavage deficient forms of APP or a dominant negative α-secretase strongly enhanced its cell adhesion and synaptogenic activity suggesting that synapse promoting function of APP is tightly regulated by α-secretase mediated processing, similar to other trans-cellular synaptic adhesion molecules.

U2 - 10.3389/fncel.2014.00410

DO - 10.3389/fncel.2014.00410

M3 - SCORING: Journal article

C2 - 25520622

VL - 8

SP - 410

JO - FRONT CELL NEUROSCI

JF - FRONT CELL NEUROSCI

SN - 1662-5102

ER -