Abstract
Intact annexin V but not its fragments bound specifically to platelets in the presence of calcium. Maximal binding observed was 0.87 pmole annexin V per 108 platelets with an apparent dissociation constant of 2.13 × 1011 M. This represents approximately 5000 binding sites per platelet. Platelet stimulation by thrombin increased the binding of annexin V by 40-fold. Addition of phospholipid vesicles or treatment with phospholipase C inhibited annexin V binding to platelets, suggesting that phospholipid is the binding site for annexin V and that phosphatidylcholine forms at least part of this site. Binding of annexin V did not cause platelet aggregation and did not affect thrombin or collagen induced aggregation. However annexin V significantly inhibited the binding of protein S to the platelet surface.
| Original language | English |
|---|---|
| Pages (from-to) | 289-296 |
| Number of pages | 8 |
| Journal | Thrombosis Research |
| Volume | 69 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 1 Feb 1993 |
| Externally published | Yes |
Keywords
- annexin V
- phosphatidylcholine
- phospholipid
- Platelets
- protein S
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