{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD064579/Peptides_C3_E.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD064579/Peptides_C2_E.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD064579/Peptides_K2_E.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD064579/Peptides_C1_E.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD064579/Peptides_K3_E.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD064579/Peptides_K1_E.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD064579/240517_OE_KC_PLT008_C1_E_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD064579/240517_OE_KC_PLT008_C3_E.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD064579/240517_OE_KC_PLT008_K3_E.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD064579/240517_OE_KC_PLT008_K1_E.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD064579/240517_OE_KC_PLT008_C2_E_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD064579/240517_OE_KC_PLT008_K2_E.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["morten.andersen@mq.edu.au"],"submitter":["The Huong Chau"],"technology_type":["Glycoproteomics","Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Platelet","Glycoproteomics","Fut8","Lysate","Glycopeptide","Core fucosylation","Blood"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD064579"],"tissue":["Blood Platelet","Platelet"],"sample_protocol":["N-glycoproteomics profiling of platelet lysates of healthy (n = 3) and Fut8-KO (n = 3) mice was performed using a well-established method. In brief, 200 µg protein extract of each biological replicate was firstly reduced using 10 mM DTT (final concentration) for 45 min at 56°C, alkylated using 40 mM IAA (final concentration) for 30 min in the dark at room temperature and the reaction quenched using surplus DTT. The protein samples were then exhaustively digested using sequencing-grade modified porcine trypsin (Promega) at a 1:50 ratio (enzyme:substrate, w/w) at 37°C for 17 h. The digestion reaction was stopped by acidification with 1% (v/v) TFA (final concentration). Digested peptides were desalted using Oligo R3-C18-SPE micro-columns. In preparation of this, 1 mm Empore discs (Octyl C18 47 mm Extraction DISK 66883-U, Thermo Fisher Scientific) were inserted into P10 pipette tips (Eppendorf) onto which micro-columns of R3 resin (Thermo Fisher Scientific) were packed. After conditioning, the peptide samples were then loaded on to the Oligo R3-C18-SPE micro-columns, washed, and eluted firstly with 50 µL 0.1% (v/v) TFA in 50% (v/v) ACN followed by 50 µL 0.1% (v/v) TFA in 70% (v/v) ACN. Glycopeptides were enriched from the desalted peptides utilising an established hydrophilic interaction liquid chromatography (HILIC)-SPE based enrichment method. Custom-made HILIC-C8-SPE micro-columns were prepared by inserting 1 mm Empore discs (Octyl C8 47 mm Extraction DISK 66882-U, Thermo Fisher Scientific) into P10 pipette tips (Eppendorf) onto which micro-columns of zwitterionic HILIC resin (ZIC-HILIC, 10 μm particle size, 200 Å pore size, kindly donated by Merck KGaA, Darmstadt, Germany) were packed. The HILIC-C8-SPE micro-columns were conditioned before peptides were gently loaded and reloaded onto the HILIC-C8-SPE micro-columns. Following thorough washing, glycopeptides were eluted sequentially using 50 µL 0.1% (v/v) TFA, 50 µL 25 mM aqueous NH4HCO3 and finally 50 µL 50% (v/v) ACN. The eluted glycopeptide fractions were combined, dried and resuspended in 20 µL 0.1% (v/v) formic acid for LC-MS/MS analysis. The enriched glycopeptide fractions were analysed in a single batch on an Orbitrap Exploris 480 mass spectrometer (Thermo Fisher Scientific) operated in positive ion polarity mode. Peptides (900 ng/sample) were loaded on to an Acclaim™ PepMap™ C18 reversed phase HPLC column (5 mm × 300 μm inner diameter, Thermo) and were separated on a nanoLC column (75 μm inner diameter x 30 cm length) packed in-house with Solidcore Halo® 2.7 μm 150 Å ES-C18 resin (Advanced Material Technology) operated at 45°C by an UltiMate™ NCS-3500RS HPLC system (Thermo Fisher Scientific). The HPLC produced a constant flow rate of 300 nL/min using a binary mobile phase system comprising 0.1% (v/v) formic acid (solvent A) and 0.1% (v/v) formic acid in 99% (v/v) ACN (solvent B). Following an initial equilibration for 5 min using solvent A, peptides were separated over a linear gradient ramping from 3.2-36% solvent B over 56 min followed by 36-95% solvent B over 2 min and an 8 min wash at 95% solvent B for a total run time of 75 min per sample. MS1 full scans (m/z 350-1,450) were acquired with a resolution of 60,000 and a normalised AGC target of 3 x 10E6, a maximum injection time of 50 ms and a 1 s cycle time. Data-dependent acquisition was used to select the ten most abundant precursors in each MS1 scan for MS/MS, which were performed using higher-energy collisional dissociation (HCD) at 27.5% NCE. The precursor isolation window was m/z 1.4 and the MS/MS AGC target was 1 x 10E5 with a resolution of 15,000. Selected precursors were dynamically excluded for 15 s. Unassigned, singly charged precursors and highly charged precursors (z > 7) were excluded for MS/MS."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The generated and downloaded LC-MS/MS raw data files were browsed and interrogated using Xcalibur v2.2 (Thermo Fisher Scientific) and Byonic v2.6.46 (Protein Metrics Inc, CA, USA) as previously described. In short, the MS/MS spectra were searched against a protein search space composed of all reviewed UniProtKB Mus musculus proteins with a predefined glycan search space of 310 mammalian N-glycans without sodium adducts. The output from the glycopeptide searches was filtered to < 1% false discovery rate at the protein level and 0% at the peptide level using a decoy database and only confidently identified glycopeptides (PEP 2D < 0.001) were considered. The relative abundances of the identified N-glycopeptides were determined using a spectral counting approach employing the glycopeptide-to-spectrum matches (glycoPSMs). Unpaired one-tailed Student’s t-tests were used to compare the relative core fucosylation levels both within the global glycoproteome and for each identified glycoprotein. p < 0.05 was chosen as the confidence threshold. A one-tailed analysis could be justified based on the expectation that Fut8 disruption would lower core fucosylation levels. Statistical confidence has been indicated by * (p < 0.05), ** (p < 0.01), *** (p < 0.001), and **** (p < 0.0001), while ns was used to indicate that no significance was found (p ≥ 0.05)."],"omics_type":["Proteomics"],"labhead":["Morten Thaysen-Andersen"],"instrument_platform":[""],"labhead_affiliation":["School of Natural Sciences, Macquarie University, Sydney, Australia"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["42237907 Yang RB,Tu CF,Chen YT,Chau TH,Lin SW,Tsai CD,Li FA,Thaysen-Andersen M,Lin YC FUT8-Dependent Core Fucosylation: Essential for Platelet Function and a Target in Thrombosis. Arterioscler Thromb Vasc Biol. 2026 Jun 4 10.1161/ATVBAHA.126.324757"],"submitter_mail":["the-huong.chau@hdr.mq.edu.au"],"submitter_affiliation":["Macquarie University"],"submitter_country":["Australia"],"pubmed_abstract":["<h4>Background</h4>FUT8 (fucosyltransferase 8) adds core fucose to the innermost <i>N</i>-acetylglucosamine of <i>N</i>-glycans on surface receptors, affecting ligand binding and downstream signaling in various cellular contexts. Here, we examine the role of FUT8-catalyzed core fucosylation in platelet activity in vivo, and we evaluate the potential antithrombotic strategy of FUT8 inhibition.<h4>Methods</h4>To investigate whether the extracellular domains of platelet adhesion receptors are core fucosylated, we used genetic, biochemical, glycomics, and glycoproteomics approaches. To investigate the impact of core fucosylation on platelet receptors for their ligand affinity, platelet activation, and downstream signaling, we used binding assays, platelet aggregometry, and phospho-specific effector antibodies. To investigate the biological effect of genetic and pharmacological inhibition of FUT8, we used murine thrombosis models.<h4>Results</h4>We identified core fucosylated <i>N</i>-glycans in the extracellular domains of platelet adhesion receptors, such as GPVI (glycoprotein VI) and integrin αIIbβ3. Core fucosylation at platelet GPVI or αIIbβ3 N-glycans enhanced affinity and binding to type I collagen or fibrinogen, leading to greater platelet activation and downstream signaling. In 2 murine thrombosis models, platelet-specific <i>Fut8</i> deletion inhibited platelet activation and thrombus formation. Furthermore, FUT8 inhibition with FDW028 led to reduced platelet aggregation and activation, protecting mice from lethal thrombosis.<h4>Conclusions</h4>This study provides genetic and pharmacological evidence that FUT8-mediated core fucosylation of platelet receptors promotes platelet activation and thrombus formation. Our results suggest that FUT8 in platelets may be a therapeutic target for thrombosis-related cardiovascular diseases."],"pubmed_title":["FUT8-Dependent Core Fucosylation: Essential for Platelet Function and a Target in Thrombosis."],"pubmed_authors":["Yang Ruey-Bing RB, Tu Cheng-Fen CF, Chen Yan-Ting YT, Chau The Huong TH, Lin Shu-Wha SW, Tsai Cheng-Da CD, Li Fu-An FA, Thaysen-Andersen Morten M, Lin Yuh-Charn YC"],"additional_accession":[]},"is_claimable":false,"name":"Glycoproteomics of healthy and Fut8-KO mice platelet lysates","description":"To validate the knockout of FUT8, the core fucosylation enzyme on mice 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