ArticleBlood2014
TAILS N-terminomics of human platelets reveals pervasive metalloproteinase-dependent proteolytic processing in storage.
Article in Blood, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 62 citations in OpenAlex.
- Nascent ADAM17 synthesis potentiates GPIbα cleavage in resting and stimulated stored platelets.Blood vessels, thrombosis & hemostasis · 2026Article
- Using High-Throughput Screening to Identify Crosslinking Peptides That Control Cell-Mediated Matrix Degradation.Advanced healthcare materials · 2025Article
- The Effect of Leukocyte Removal and Matrix Metalloproteinase Inhibition on Platelet Storage Lesions.Cells · 2024Article
- The Perspectives of Platelet Proteomics in Health and Disease.Biomedicines · 2024Review
- Structural analysis of platelet fragments and extracellular vesicles produced by apheresis platelets during storage.Blood advances · 2024Article
- Tissue Inhibitor of Metalloproteases 3 (TIMP-3): In Vivo Analysis Underpins Its Role as a Master Regulator of Ectodomain Shedding.Membranes · 2022Review
- Identification of novel ADAMTS1, ADAMTS4 and ADAMTS5 cleavage sites in versican using a label-free quantitative proteomics approach.Journal of proteomics · 2021Article
- Molecular Proteomics and Signalling of Human Platelets in Health and Disease.International journal of molecular sciences · 2021Review
- Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae.Scientific reports · 2021Article
- Post-translational Modifications of the Protein Termini.Frontiers in cell and developmental biology · 2021Review
- Proteomics identifies a convergent innate response to infective endocarditis and extensive proteolysis in vegetation components.JCI insight · 2020Article
- Moonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage.The Journal of biological chemistry · 2020Article
- Platelet Membrane Receptor Proteolysis: Implications for Platelet Function.Frontiers in cardiovascular medicine · 2020Review
- Simple, scalable, and ultrasensitive tip-based identification of protease substrates.Molecular & cellular proteomics : MCP · 2018Article
- Flow cytometry analysis of platelet populations: usefulness for monitoringthe storage lesion in pooled buffy-coat platelet concentrates.Blood transfusion = Trasfusione del sangue · 2018Article
- Monitoring storage induced changes in the platelet proteome employing label free quantitative mass spectrometry.Scientific reports · 2017Article
- Comprehensive analysis of human protein N-termini enables assessment of various protein forms.Scientific reports · 2017Article
- Sharpening Host Defenses during Infection: Proteases Cut to the Chase.Molecular & cellular proteomics : MCP · 2017Review
- Systems biology-opportunities and challenges: the application of proteomics to study the cardiovascular extracellular matrix.Cardiovascular research · 2016Review
- Quantitative proteomics and terminomics to elucidate the role of ubiquitination and proteolysis in adaptive immunity.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Proteases, and specifically metalloproteinases, have been linked to the loss of platelet function during storage before transfusion, but the underlying mechanisms remain unknown. We used a dedicated N-terminomics technique, iTRAQ terminal amine isotopic labeling of substrates (TAILS), to characterize the human platelet N-terminome, proteome, and posttranslational modifications throughout platelet storage over 9 days under blood-banking conditions. From the identified 2938 proteins and 7503 unique peptides, we characterized N-terminal methionine excision, co- and posttranslational Nα acetylation, protein maturation, and proteolytic processing of proteins in human platelets. We also identified for the first time 10 proteins previously classified by the Human Proteome Organization as "missing" in the human proteome. Most N termini (77%) were internal neo-N termini (105 were novel potential alternative translation start sites, and 2180 represented stable proteolytic products), thus highlighting a prominent yet previously uncharacterized role of proteolytic processing during platelet storage. Protease inhibitor studies revealed metalloproteinases as being primarily responsible for proteolytic processing (as opposed to degradation) during storage. System-wide identification of metalloproteinase and other proteinase substrates and their respective cleavage sites suggests novel mechanisms of the effect of proteases on protein activity and platelet function during storage. All data sets and metadata are available through ProteomeXchange with the data set identifier PXD000906.
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Registered trials
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