Eriksson AC, Whiss PA
Characterization of static adhesion of human platelets in plasma to protein surfaces in microplates. [Journal Article]
Blood Coagul Fibrinolysis 2009 Apr; 20(3):197-206.
Platelet adhesion is a complex and important event for prevention of blood loss after vessel injury. This study investigated fundamental adhesive mechanisms occurring in an in-vitro assay developed for the measurement of static adhesion of human platelets in plasma. The aim was to gain methodological knowledge that could be used for interpretations of results from other studies using this specific assay. Involvement of adhesive receptors was investigated by the use of various antibodies as well as therapeutic drugs (abciximab, eptifibatide and tirofiban). Inhibitors of adenosine 5'-diphosphate receptors (cangrelor, MRS2179) and of thromboxane A2 signalling (BM-531) were used to estimate the role of autocrine activation. Adhesion to collagen was found to be mainly mediated by alpha2beta1 and to some extent by alphaIIbbeta3. Adhesion to fibrinogen was mediated by alphaIIbbeta3. In addition, adenosine 5'-diphosphate-induced adhesion to albumin was dependent on alphaIIbbeta3. Furthermore, experiments with cangrelor and BM-531 showed that the majority of the adhesive interactions tested were dependent on adenosine 5'-diphosphate or thromboxane A2. We conclude that the mechanisms of adhesion measured by the static platelet adhesion assay are in accordance with the current knowledge regarding platelet activation and adhesion. Despite its simplicity, we suggest that this adhesion assay could be used as a screening device for the study of the influence of various surfaces and soluble substances on platelet adhesion.
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