Abstract

Human platelets are thought to express approximately 2000-3000 proteins, but post-translational modifications, alternatively spliced variants and a rich diversity of vertebrate domain architectures likely make this a conservative estimate. Even though rapidly advancing proteomic techniques have catalyzed the identification of roughly one third of the platelet proteome, a combination of abundance-based and activity-based proteomics is needed for elucidation of platelet functional characteristics including the definition of a “core proteome” and recognition of diverse enzyme activity profiles associated with various physiological states. In this review, we describe the latest mass spectrometry-based techniques capable of providing some of these physiological details required for more comprehensive evaluation of the human platelet repertoire.

Keywords: ABPP, biomarker, cancer, library, mass spectrometry, platelet, proteome, rat, hemostasis, interaction, interactome, protein, thrombosis, megakaryocyte, low-abundant proteins, cytoskeleton, vasodilator-stimulated, phosphorylations, kinase substrates, Glanzmann thrombasthenia