
The beta-amyloid protein precursor of Alzheimer disease has soluble derivatives found in human brain and cerebrospinal fluid.
Author(s) -
Mark R. Palmert,
Marcia B. Podlisny,
Dennis S. Witker,
Tilman Oltersdorf,
Linda H. Younkin,
Dennis J. Selkoe,
Steven G. Younkin
Publication year - 1989
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.86.16.6338
Subject(s) - amyloid precursor protein , cerebrospinal fluid , beta (programming language) , biochemistry , chemistry , peptide , amyloid beta , amyloid precursor protein secretase , amyloid (mycology) , p3 peptide , protein precursor , alzheimer's disease , microbiology and biotechnology , biology , medicine , enzyme , pathology , disease , neuroscience , inorganic chemistry , computer science , programming language
In this study, we use antisera to synthetic beta-amyloid protein precursor (beta APP) peptides to identify, in human brain and cerebrospinal fluid (CSF), soluble approximately 125- and approximately 105-kDa derivatives of the beta APP that lack the carboxyl terminus of the full-length, membrane-associated forms. We show that the soluble approximately 125-kDa beta APP derivative contains the Kunitz protease inhibitor domain, whereas the approximately 105-kDa form does not, and we confirm that these two proteins are soluble beta APP derivatives by purifying each from human CSF and directly sequencing its amino terminus.