{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/sdrf-rat-secretome.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/checksum.txt"],"Mzxml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_con6_-40.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_con6_-60.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_tol5_-60.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_con1_-40.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_tol3_-60.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_tol5_-40.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_con3_-60.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_con3_-40.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_tol1_-60.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_tol6_-60.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_tol3_-40.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_con1_-60.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_tol1_-40.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_tol4_-40.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_con5_-40.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_tol6_-40.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_con5_-60.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_tol4_-60.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_tol2_-40.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_con4_-60.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_con4_-40.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_tol2_-60.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_con2_-40.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/20240427_RatSec_con2_-60.mzXML"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/2024Apr_Rat.fasta"],"Mztab":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/mzTab.mzTab"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/MaxQuant_1.6.17.0.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD070160/spectra.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["peter.barath@savba.sk"],"submitter":["Maksym Danchenko"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Brain Ischemia"],"software":[""],"submitter_keywords":["Body fluid","Ischemia","Rattus norvegicus","Secretome","Label-free quantification"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070160"],"tissue":["Blood Cell","Blood"],"sample_protocol":["Stimulation of the rat blood cells was performed in vivo by remote ischemic conditioning (RIC), based on three cycles of right hind-limb ischaemia for 5 min, followed by a 5-min period of reperfusion. To collect RIC-primed blood cells intended for secretome production, animals were sacrificed one hour following the RIC procedure (tolerant secretome) by cardiac puncture and processed ex vivo as described below. The animals dedicated to non-tolerant secretome production underwent the same procedure without tourniquet application. Blood cells-derived secretome was prepared. After centrifugation of collected blood samples (4500 g, 15 min, 4 °C), the blood plasma was discarded. To retain the original blood volume, the pellet, which represented a mix of all blood cell types, was washed and resuspended in artificial plasma (hydroxyethyl starch, HES, 130/0.4 in an isotonic electrolyte solution, 6% Volulyte). Subsequently, the samples were incubated in a CO2 incubator (37°C for 150 min) followed by centrifugation (4500 g, 15 min, 4 °C). The supernatant was removed and centrifuged again (15,000 g, 15 min, 4 °C) to remove any remaining cells and cellular debris. The final supernatant, the blood cell–derived secretome with preserved exosomes and microparticles, was used. Digestion and purification of proteins were done using magnetic beads according to single-pot, solid-phase-enhanced sample preparation (SP3). Concentrated 60 μg aliquots of proteins were adjusted to 30 μL with 0.1 M Tris-HCl, pH 7.6. Next, the proteins were reduced by 10 mM dithiothreitol, alkylated with 20 mM iodoacetamide, and quenched with 10 mM dithiothreitol. Consequently, the equimolar mixture of beads was prepared: Sera-Mag Carboxylate-Modified Beads, hydrophilic and hydrophobic solids. Washed beads slurry was added to the protein samples (10:1) and pipette-mixed. For binding, 100% ethanol was added to the suspension up to 50% final concentration. Pelleting was done on the magnetic rack MagneSphere. Bound proteins were washed 5 times with 80% ethanol. For digestion, 1 μg of modified sequencing grade trypsin was added, buffered with 50 mM ammonium bicarbonate. The samples were incubated in the thermoshaker TS-100C for 18 h at 37 °C and 1000 rpm. The supernatant was recovered, followed by a second elution with 50 mM ammonium bicarbonate. The peptide concentration was measured with a microvolume spectrophotometer DS-11 FX+. Chromatographic separation was done on Vanquish Neo at 35 °C and a 250 nL/min flow rate. Peptide aliquots (500 ng) were desalted on PepMap Neo trap C18, 300 μm × 5 mm, 5-μm particle size at 50 μL/min and profiled on EASY-Spray PepMap Neo C18, 75 μm × 500 mm, 2-μm particle size in a 2-step gradient 2–24% in 100 min and 24–40% in 20 min of mobile phase (80% acetonitrile and 0.1% formic acid). High-field asymmetric-waveform ion mobility spectrometry (FAIMS) Pro Duo interface provided alternating compensating voltages –40 and –60 for filtering noise. Mass spectra were collected on Orbitrap Exploris 240 in data-dependent mode with a 2-s cycle at top speed and 2 kV on the capillary with internal mass calibration at run start. Parent scan 350–1,700 m/z was done at 120,000 resolution with a 200% automatic gain control (AGC) target and a 200 ms maximum injection time. The precursor intensity threshold was set to 5 × 104 with 60 s exclusion and 30% high-energy collisional dissociation (HCD) fragmentation. Fragments were acquired at a 30,000 resolution, an AGC target 300%, and a 50 ms maximum injection time."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Data were preprocessed with FAIMS MzXML Generator v1.0. Next, the generated dataset was processed in MaxQuant v1.6.17.0 with Andromeda search engine. Carbamidomethylation C was set as a permanent modification, and oxidation M, protein N-terminal acetylation, and deamidation N/Q were selected as variable modifications. Peptide tolerance in the first search was 10 ppm, and in the main search, after recalibration, was 2 ppm. The fragment tolerance was 10 ppm. Up to 2 enzymatic miscleavages were allowed, and based on the reverse decoy database search, the false discovery rate for peptides and proteins was 1%. Match between the runs and label-free quantification (LFQ) were activated. The search was performed against rat (Rattus norvegicus) proteome (including gene ontologies) downloaded from UniProt in April 2024 (49,582 sequences). Proteomic data were evaluated in Perseus v1.6.15. The output protein Group table from MaxQuant was filtered for the reverse proteins, the contaminants, and the low-confidence proteins. After log2 transformation of the LFQ intensities, only proteins with 4 or more valid values in any experimental group were retained, and missing values were imputed from a lower range of the normal distribution curve. Next, t-test was performed with permutation correction for multiple testing and a Q threshold 0.05. A complementary Volcano plot was created for a graphical evaluation of the dataset. Gene ontology enrichment analysis was performed separately on accumulated/depleted proteins in the tolerant secretome with Fisher exact test P threshold 0.005."],"omics_type":["Proteomics"],"labhead":["Peter Baráth"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Department of Glycobiology, Institute of Chemistry, Slovak Academy of Sciences"],"species":["Rattus Norvegicus (rat)"],"submitter_mail":["maxymdan@gmail.com"],"publication":["Not available"],"submitter_affiliation":["Plant Science and Biodiversity Center SAS"],"submitter_country":["Slovakia"],"doi":["10.6019/PXD070160"],"additional_accession":[]},"is_claimable":false,"name":"Remodeling of Blood Cell Paracrine Profile Reveals GO-Driven Neuroprotective Signatures in an Experimental Model of Stroke—Proteomic Perspective","description":"Blood cells serve as a relevant source of bioactive substances that provide neuroprotection following stroke. Blood cells, as a cell source for secretome production, exhibit the potential to be stimulated by external stimuli, such as remote ischemic conditioning (RIC), resulting in changes to the quantitative and qualitative profile of released proteins, leading to an even higher potential to activate pro-survival mechanisms in ischemia-affected neurons. This reprogramming is characterized by attenuated blood cell hemolysis and enhanced oxidative defense mechanisms in the blood cells. Focusing on the paracrine activity, stimulation of blood cells tends to suppress rather than enhance the synthesis of protein released to the cell surrounding, while only minimal changes in the biomacromolecular composition of the secretome occur. This is reflected within the affected Gene Ontology (GO) terms, by the suppression of protein synthesis involved in immunomodulation, metabolic processes related to the antioxidant glutathione, and the loss of synaptic connections. Conversely, it also includes the downregulation of proteins that negatively regulate the extrinsic apoptotic signaling pathway. RIC-mediated protein synthesis/secretion reprogramming of blood cells mediates meaningful changes in the recipient of the secretome treatment, in enhanced survival of neurons, reduced redox imbalance, and extracellular content of the major neurotransmitter glutamate in the penumbra region and decreases the systemic oxidative stress index. Due to the easy accessibility of blood cell sources for its production, the secretome derived from properly primed cells represents a highly attractive strategy for stroke management—albeit currently limited to the experimental 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