In:
American Journal of Alzheimer's Disease, SAGE Publications, Vol. 13, No. 5 ( 1998-09), p. 236-244
Abstract:
Proteolytic processing of Alzheimer's disease amyloid precursor protein (APP) by /3-secretase generates the Nterminus ofA/3 (which deposits in the brain) and releases a secreted ectodomain of APP (sAPP/3). We identified in human platelets a band at 125 kDa corresponding to APP ectodomain ending with C-terminal methionine residue (APP 671 ) as characterized by an antibody specificfor the C-terminal methionine residue of sAPP/3. The same antibody also detected bands at -105 and U125 kDa in human brain homogenates. Platelet sAPP/3 is an isoform containing the Kunitzprotease inhibitor domain (sAPP/3-KPI+) and is released into the medium when platelets are induced to aggregate using agonists such as thrombin, collagen, phorbol 12-myristate 13-acetate, or calcium ionophore A2318 7. The release of sAPPB /from aggregatedplatelets is consistent with a role in regulation of the coagulation cascade and/or in platelet aggregation. These data together with previous reports suggest that human platelets contain the a-, /3-and y-secretase activities, and are a suitable system to study APP processing and Ap production, a pathway which is considered to be a prime targetfor therapeutic intervention in AD.
Type of Medium:
Online Resource
ISSN:
1082-5207
DOI:
10.1177/153331759801300504
Language:
English
Publisher:
SAGE Publications
Publication Date:
1998
detail.hit.zdb_id:
2235173-5
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