Shedding of APP limits its synaptogenic activity and cell adhesion properties
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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, Vol. 8, 01.01.2014, p. 410.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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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 -