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Procoagulant Platelet Characterization by Measuring Phosphatidylserine Exposure and Microvesicle Release from Human Purified Platelets
Published on: November 29, 2024
Proteome analysis of signaling cascades in human platelets
1Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. angel.garcia@bioch.ox.ac.uk
Abstract:
During the last 15 years, advances in mass spectrometry (MS) instrumentation and techniques have revolutionized the emerging field of proteomics. Proteomics technology allows a comprehensive and efficient analysis of the protein content (i.e., the proteome) of any cell, tissue or biological fluid and has become an indispensable tool in biomedical research, complementing the powerful field of genomics. Proteomics is based on the huge analytical power offered by mass spectrometry in combination with several separation techniques, such as two-dimensional gel electrophoresis (2-DE) or multidimensional liquid chromatography. The technology is particularly suitable for platelets because of the absence of a nucleus. In the recent years, there has been success in mapping the proteome of the platelet in a basal state. Furthermore, a handful of research groups have also applied this technology to the study of signaling cascades in human platelets, allowing the identification of novel platelet signaling proteins and phosphorylation events. Those studies provide new insights into the mechanisms of platelet activation and build the basis for the development of therapeutic agents for thrombotic disease. This article focus on the application of 2-DE-based proteomics to the study of signaling cascades in human platelets.
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