Abstract
The β-amyloid (Aβ) peptide is present both in serum and in platelets, however it is unclear whether Aβ plays a role in platelet function. We have now investigated the effects of soluble Aβ on platelet function and have found that low levels (0.1–1 nM) of soluble Aβ augment ADP-dependent platelet aggregation and translocation of focal adhesion kinase to the platelet cytoskeleton. Addition of Aβ to gel-filtered platelets along with concentrations of adenosine diphosphate (ADP) producing submaximal aggregation responses increased the aggregation response by over 2-fold depending on the ADP:Aβ ratios. The structure activity requirements for Aβ activity showed intriguing constraints. Only full length Aβ has significant activity. Truncated Aβ peptides, such as Aβ1–16 or Aβ25–35, or reverse Aβ40–1 all show little or no activity. We also examined the activity of mutant Aβ peptides, corresponding with the APP692A→G and APP693E→Q (at Aβ21 and Aβ22, respectively) which are found in familial Alzheimer's disease and hereditary cerebral hemorrhagic amyloidosis, Dutch type (HCHWA-D), and found that these peptides showed little or no activity. These results suggest that Aβ interacts with platelets in a highly specific manner and may play a role in regulating platelet function.
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Wolozin, B., Maheshwari, S., Jones, C. et al. β-Amyloid augments platelet aggregation: reduced activity of familial angiopathy-associated mutants. Mol Psychiatry 3, 500–507 (1998). https://doi.org/10.1038/sj.mp.4000451
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DOI: https://doi.org/10.1038/sj.mp.4000451