Annexin V relocates to the periphery of activated platelets following thrombin activation: an ultrastructural immunohistochemical approach.
Cell Biology International. 1999-09-01; 23(9): 629-635
DOI: 10.1006/cbir.1999.0426
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1. Cell Biol Int. 1999;23(9):629-35.
Annexin V relocates to the periphery of activated platelets following thrombin
activation: an ultrastructural immunohistochemical approach.
Tzima E(1), Poujol C, Nurden P, Nurden AT, Orchard MA, Walker JH.
Author information:
(1)School of Biochemistry and Molecular Biology, University of Leeds, UK.
We have previously shown biochemically that the physiological agonist thrombin
can cause translocation of endogenous annexin V to a fraction containing all
platelet membranes. This paper reports ultrastructural immunohistochemical data
revealing that annexin V molecules localize with plasma membranes of blood
platelets following thrombin activation. When ultrathin sections of resting
platelets were examined by immunogold staining, annexin V was found to be
cytosolic, having a generalized distribution throughout the platelet. After
thrombin activation, annexin V became peripheral in location and plasmalemma
association increased. Morphometric analysis of gold particles shows that annexin
V relocates specifically to the plasma membrane and its underlying cytoskeleton
following treatment with thrombin. In control platelets 6.1% +/- 0.78 of annexin
V is present at the plasma membrane and 15.0% +/- 0.82 in the region
corresponding to the membrane cytoskeleton (10-80 nm); after stimulation with 0.5
unit/ml thrombin for 2 min this increased to 16.7% +/- 0.22 and 40.4% +/- 0.53,
respectively.
DOI: 10.1006/cbir.1999.0426
PMID: 10728574 [Indexed for MEDLINE]