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Platelet releasate proteome profiling reveals a core set of proteins with low variance between healthy adults

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dc.contributor.authorGuerrero López, José Antonio
dc.contributor.authorParsons, Martin E. M.
dc.contributor.authorSzklanna, Paulina B.
dc.contributor.authorWynne, Kieran
dc.contributor.authorDervin, Feidhlim
dc.contributor.authorO'Connell, Karen
dc.contributor.authorAllen, Seamus
dc.contributor.authorEgan, Karl
dc.contributor.authorBennett, Cavan
dc.contributor.authorMcGuigan, Christopher
dc.contributor.authorGheveart, Cedric
dc.contributor.authorÁinle, Fionnuala Ní
dc.contributor.authorMaguire, Patricia B.
dc.contributor.departmentMedicina
dc.date.accessioned2026-02-24T09:29:32Z
dc.date.available2026-02-24T09:29:32Z
dc.date.copyright© 2018 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
dc.date.issued2018-06-22
dc.description.abstractUpon activation, platelets release a powerful cocktail of soluble and vesicular signals, collectively termed the "platelet releasate" (PR). Although several studies have used qualitative/quantitative proteomic approaches to characterize PR; with debated content and significant inter-individual variability reported, confident, and reliable insights have been hindered. Using label-free quantitative (LFQ)-proteomics analysis, a reproducible, quantifiable investigation of the 1U mL−1 thrombin-induced PR from 32 healthy adults was conducted. MS proteomics data are available via ProteomeXchange, identifier PXD009310. Of the 894 proteins identified, 277 proteins were quantified across all donors and form a "core" PR. Bioinformatics and further LFQ-proteomic analysis revealed that the majority (84%) of "core" PR proteins overlapped with the protein composition of human platelet-derived exosomes. Vesicles in the exosomal-size range were confirmed in healthy-human PR and reduced numbers of similar-sized vesicles were observed in the PR of a mouse model of gray platelet syndrome, known to be deficient in platelet alpha-granules. Lastly, the variability of proteins in the PR was assessed, and reproducible secretion levels were found across all 32 healthy donors. Taken together, the PR contains valuable soluble and vesicular cargo and has low-population variance among healthy adults, rendering it a potentially useful platform for diagnostic fingerprinting of platelet-related disease.
dc.formatapplication/pdf
dc.format.extent9
dc.identifier.citationProteomics, 2018, Vol. 18, Issue 15, 1800219
dc.identifier.doihttps://doi.org/10.1002/pmic.201800219
dc.identifier.eissn1615-9861
dc.identifier.issn1615-9853
dc.identifier.urihttp://hdl.handle.net/10201/211701
dc.languageeng
dc.publisherWiley
dc.relationScience Foundation Ireland Irish Research Council. Grant Number: GOIPG/2014/575
dc.relation.publisherversionhttps://analyticalsciencejournals.onlinelibrary.wiley.com/doi/10.1002/pmic.201800219
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectRacellular vesicles
dc.subjectLabel free quantification
dc.subjectPlatelet releasate
dc.subjectPlatelets
dc.subjectTandem MS
dc.subject.odsObjetivo 3: Salud
dc.titlePlatelet releasate proteome profiling reveals a core set of proteins with low variance between healthy adults
dc.typeinfo:eu-repo/semantics/article
dc.type.versioninfo:eu-repo/semantics/publishedVersion
dspace.entity.typePublicationes
relation.isAuthorOfPublication099fb9a8-9bae-43fb-be04-b8ea37502882
relation.isAuthorOfPublication.latestForDiscovery099fb9a8-9bae-43fb-be04-b8ea37502882
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