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Evidence that glypican is a receptor mediating β‐amyloid neurotoxicity in PC12 cells
Author(s) -
Schulz Joachim G.,
Megow Dirk,
Reszka Regina,
Villringer Arno,
Einhäupl Karl M.,
Dirnagl Ulrich
Publication year - 1998
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1046/j.1460-9568.1998.00220.x
Subject(s) - neurotoxicity , chemistry , microbiology and biotechnology , amyloid beta , receptor , amyloid (mycology) , cell , biochemistry , biology , toxicity , peptide , inorganic chemistry , organic chemistry
Docking of β‐amyloid fibrils to neuronal or glial cell membranes may be an early, necessary and intervenable step during the progression of Alzheimer's disease. Formation of neurofibrillary tangles and amyloid plaques as well as neurotoxicity and inflammation may be direct or indirect consequences. In an attempt to find a receptor that mediates those effects, we assessed rat pheochromocytoma PC12 cell 3‐[4,5‐dimethylthiazol‐2‐yl]‐2,5‐diphenyl tetrazolium bromide (MTT) reduction after addition of β‐amyloid to the culture medium. Presence of competitive substances in the medium, cell‐surface treatment and specific block of cellular synthesis pathways helped to identify the heparan sulphate moiety of a glycosylphosphatidylinositol‐anchored protein likely to represent glypican as a possible receptor mediating β‐amyloid neurotoxicity.