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Title: Soluble amyloid-β precursor protein binds its cell surface receptor in a cooperative fashion with glypican and syndecan proteoglycans
Authors: Reinhard, Constanze
Borgers, Marianne
David, Guido
De Strooper, Bart # ×
Issue Date: Nov-2013
Publisher: Co. of Biologists
Series Title: Journal of Cell Science vol:126 issue:Pt 21 pages:4856-61
Article number: 10.1242/jcs.137919
Abstract: Proteolytic processing of amyloid-β precursor protein (APP) generates the amyloid-β peptide, which plays a central role in Alzheimer disease. The physiological function of APP and its proteolytic fragments, however, remains barely understood. Here we show that, on the basis of its binding characteristics, the secreted ectodomain of APP (sAPP) is a new member of the heparin-binding growth factor superfamily. Like other of its members, sAPP binds in a bivalent manner to the plasma membrane with two different subdomains. The N-terminal growth-factor-like domain (GFLD) is necessary and sufficient for protein-receptor binding, whereas the E2-domain mediates interaction with membrane-anchored heparan sulfate proteoglycans (HSPGs). The membrane-anchored HSPGs function as low-affinity co-receptors for sAPP and enhance the affinity to the sAPP receptor. Our findings provide a solid basis for the further identification of this receptor.
URI: 
ISSN: 0021-9533
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Department of Human Genetics - miscellaneous
Molecular Genetics Section (-)
× corresponding author
# (joint) last author

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