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Detection of a Soluble Form of BACE-1 in Human Cerebrospinal Fluid by a Sensitive Activity Assay
Author(s) -
Jan H. Verheijen,
L.G.M. Huisman,
Natascha van Lent,
Ulf Neumann,
Paolo Paganetti,
C. Erik Hack,
Femke H. Bouwman,
J. Lindeman,
Edward Bollen,
Roeland Hanemaaijer
Publication year - 2006
Publication title -
clinical chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.705
H-Index - 218
eISSN - 1530-8561
pISSN - 0009-9147
DOI - 10.1373/clinchem.2006.066720
Subject(s) - chemistry , biochemistry , peptide , proteases , neurodegeneration , protease , cleavage (geology) , amyloid precursor protein , enzyme , cerebrospinal fluid , blot , in vivo , alzheimer's disease , biology , medicine , paleontology , microbiology and biotechnology , disease , pathology , neuroscience , fracture (geology) , gene
Formation of deposits of the insoluble amyloid beta-peptide is believed to be causally related with neurodegeneration in Alzheimer disease (AD). The beta-peptide originates from a larger amyloid precursor protein (APP) by the action of proteolytic enzymes. The first proteolytic event leading to amyloid formation is the cleavage of APP by the membrane-bound aspartyl protease BACE-1, also known as memapsin-2. Inhibition of BACE-1 is thought to be a therapeutic approach to AD. Measuring BACE-1 activity in biological samples would be useful to elucidate the mechanism of AD and for development of AD drugs.

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