Abstract
Platelets are small anucleate blood cells that play vital roles in haemostasis and thrombosis, besides other physiological and pathophysiological processes. These roles are tightly regulated by a complex network of signalling pathways. Mass spectrometry-based proteomic techniques are contributing not only to the identification and quantification of new platelet proteins, but also reveal post-translational modifications of these molecules, such as acetylation, glycosylation and phosphorylation. Moreover, target proteomic analysis of platelets can provide molecular biomarkers for genetic aberrations with established or non-established links to platelet dysfunctions. In this report, we review 67 reports regarding platelet proteomic analysis and signalling on a molecular base. Collectively, these provide detailed insight into the: (i) technical developments and limitations of the assessment of platelet (sub)proteomes; (ii) molecular protein changes upon ageing of platelets; (iii) complexity of platelet signalling pathways and functions in response to collagen, rhodocytin, thrombin, thromboxane A2 and ADP; (iv) proteomic effects of endothelial-derived mediators such as prostacyclin and the anti-platelet drug aspirin; and (v) molecular protein changes in platelets from patients with congenital disorders or cardiovascular disease. However, sample sizes are still low and the roles of differentially expressed proteins are often unknown. Based on the practical and technical possibilities and limitations, we provide a perspective for further improvements of the platelet proteomic field.
Highlights
We provide a topical overview of how technical developments in the mass-spectrometric technologies are contributing to our knowledge of the basic proteome of freshly isolated and stored platelets, as well as of platelets stimulated via key receptor-dependent signalling mechanisms
Most papers used healthy donor platelets without agonist (33%), patient platelets (PAT, 20%) or platelets stimulated via Glycoprotein VI (GPVI) (15%) or proteinase-activated receptor (PAR) (17%)
Using a label-free proteomic approach, platelets obtained from cord blood, which relatively poorly respond to thromboxane stimulation, express normal receptor levels, but are enriched in mitochondrial energy and metabolism proteins, including NDUFS1, NDUFA10, NDUFAS
Summary
An extensive network of molecular signal transduction processes in platelets allows their fast adhesion and secretion upon injury of the vessel wall or damage of an atherosclerotic plaque, and allows the formation of a rapidly growing thrombus [4,5]. Because of their anucleate structure, gene transcription and ribosomal translation activities are restricted in platelets [6,7], resulting in a relatively stable proteome [8]. Mass-spectrometry-based proteomic analyses can be a valuable tool to assess the molecular build-up especially of these out-differentiated cells
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