| Literature DB >> 23713824 |
Ana Lopez-Alonso1, Bincy Jose, Martin Somers, Karl Egan, David P Foley, Antonio J Ricco, Sofia Ramström, Lourdes Basabe-Desmonts, Dermot Kenny.
Abstract
Widespread monitoring of platelet function and the effect of antiplatelet drugs will improve outcomes in cardiovascular patients, but platelet function testing is not routine in clinical practice. We report a rapid, accurate methodology to quantify platelet-protein interactions: a microarray of contact-printed 6-μm fibrinogen dots on a transparent substrate binds platelets from whole blood, one platelet per dot. The fractional occupancy of an array of fibrinogen dots after a predefined incubation time quantitatively assays platelet adhesion to the protein matrix. We demonstrate this technique by measurement of platelet adhesion to fibrinogen as a means to quantify the effect of the P2Y12 and αIIbβ3 receptor inhibitors cangrelor and abciximab, respectively, both in vitro--by incubating the drug with a freshly drawn blood sample--and in blood from patients treated with antiplatelet agents. The effects of single- and dual-antiplatelet therapy are also assessed. Results from this platelet-binding assay are well correlated with standard techniques including flow cytometry and light transmission aggregometry. This assay technology, readily integrated with microfluidic platforms, is generally applicable to the assay of cell-protein interactions and promises more effective, rapid assay of drug effects in cardiovascular disease patients.Entities:
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Year: 2013 PMID: 23713824 DOI: 10.1021/ac401076s
Source DB: PubMed Journal: Anal Chem ISSN: 0003-2700 Impact factor: 6.986