{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_17.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_19.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_20.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_9.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_18.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_16.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/20240527_PK115_2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069675/SEARCH.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["pavel.kielkowski@cup.lmu.de"],"submitter":["Pavel Kielkowski"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["gut-immune-brain axis","midbrain","t cells","neurodegeneration","Neuroinflammation","Neuroinflammation; neurodegeneration; midbrain; microglia; t cells; neutrophils; gut-immune-brain axis; inflammatory bowel disease","neutrophils","microglia","inflammatory bowel disease"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069675"],"tissue":["Brain","Colon"],"sample_protocol":["Protein extraction and preparation for mass spectrometry Isolated midbrain and striatum tissue from contralateral brain hemispheres were used for proteome and transcriptome analysis. Total protein was isolated from snap frozen tissue by homogenization in 1:6 w/v homogenization buffer (50 mM Tris/HCl, 150 mM NaCl, pH 8.0) supplemented with 1x cOmplete™ EDTA-free Protease Inhibitor Cocktail (Roche) and mechanical dissociation using a Potter S Homogenizer (800 U/min; Sartorius AG). Homogenous samples were centrifuged (10,000 g, 10 min, 4°C) and protein concentration was quantified using the Pierce BCA Protein Assay Kit according to the manufacturers protocol (Thermo Fisher). Colorimetric absorbance was measured at a CLARIOstar PLUS high-performance microplate reader (BMG Labtech). Samples were stored at -80°C until mass spectrometric analysis.  Mass spectrometry-based proteomics   Sample preparation and mass spectrometric measurements. All samples were prepared in 96-well plate format using the optimized SP3 protocol according to Hughes et al. (DOI: 10.1038/s41596-018-0082-x). Specifically, tissue samples were lysed in TBS. Protein concentration in lysates was determined using BCA (Thermo Scientific, #23225). Protein amount was adjusted to 20 μg in a total volume of 40 μL lysis buffer. The protein was loaded onto a mixture of hydrophilic and hydrophobic carboxylate-coated magnetic beads (Cytiva, #45152105050250 and #65152105050250, 10 μL each) prewashed three times with 100 µL of MS-grade H2O (Honeywell, #15665350). The magnetic beads with protein samples were mixed at 850 rpm, 1 min at RT. To initiate the binding, 60 µL of absolute EtOH was added, and the mixture was incubated at RT for 5 min at 850 rpm. Subsequently, the beads were washed three times with 80% (v/v) EtOH, with incubation at RT for 1 min and 850 rpm between each wash. After the last wash, the beads were resuspended in 50 μL of 100 mM ammonium acetate buffer (ABC, Sigma-Aldrich, #09689). The wash steps and ABC buffer addition was performed by a liquid handling robot (Hamilton Microlab Prep). The on-beads digestion was performed with trypsin (Promega, V5113, 1 µg) overnight 37 ˚C and 850 rpm. The resulting peptide mixture was eluted from the magnetic beads into a new 1.5 mL tube. The magnetic beads were washed with 50 and 30 μL of 1% (v/v) formic acid (TCI, # F0654) and incubated at 40 ˚C, 850 rpm for 5 min. The fractions were added to the first elution fraction. 4 µL was used for the injection. MS measurements were performed on an Orbitrap Eclipse Tribrid Mass Spectrometer (Thermo Fisher Scientific) coupled to an UltiMate 3000 Nano-HPLC (Thermo Fisher Scientific) via a nanospray Flex ion source (Thermo Fisher Scientific) equipped with column oven (Sonation) and FAIMS interface (Thermo Fisher Scientific). Peptides were loaded on an Acclaim PepMap 100 μ-precolumn cartridge (5 μm, 100 Å, 300 μm ID x 5 mm, Thermo Fisher Scientific) and separated at 40°C on a PicoTip emitter (noncoated, 15 cm, 75 μm ID, 8 μm tip, New Objective) that was in-house packed with Reprosil-Pur 120 C18-AQ material (1.9 μm, 150 Å, Dr. A. Maisch GmbH). Buffer composition: Buffer A consists of MS-grade H2O supplemented with 0.1% FA; Buffer B consists of acetonitrile supplemented with 0.1% FA. The 60-min LC gradient from 4 to 35.2 % buffer B was used. The flow rate was 0.3 µL/min.   Data independent acquisition. The DIC duty cycle comprised one MS1 scan followed by 30 MS2 scans. The MS2 scans had an isolation window of 4 m/z range, which overlapped with an adjacent window at the 2 m/z range.MS1 scan was conducted with Orbitrap at 60000 resolution power and a scan range of 200 – 1800 m/z with an adjusted RF lens at 30%. MS2 scans were conducted with Orbitrap at 30000 resolution power, RF lens was set to 30%. The precursor mass window was restricted to a 500 – 740 m/z range. HCD fragmentation was enabled as an activation method with a fixed collision energy of 35%. FAIMS was performed with one CV at -45V for both MS1 and MS2 scans during the duty cycle."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Computational evaluation of DIA raw files. Raw files were converted in the first step with “MSConvertGUI” as a part of the “ProteoWizard” software package (http://www.proteowizard.org/download.html) to an output mzML format applying the “peakPicking” filter with “vendor msLevel=1”, and the “Demultiplex” filter with parameters “Overlap Only” and “mass error” set to 10 ppm. Standalone DIA-NN software under version 1.8.1 was used for protein identification and quantification. First, a spectral library was predicted in silico by the software’s deep learning-based spectra, RTs and IMs prediction using Uniprot Mus musculus FASTA (containing canonical and isoforms, decoys, common contaminants, downloaded on 10.01.2023). DIA-NN search settings: FASTA digest for library-free search/library generation option was enabled, together with a match between runs (MBR) option and precursor FDR level set at 1%. Library generation was set to smart profiling, Quantification strategy - Robust LC. The mass accuracy and the scan window were set to 0 to allow the software to identify optimal conditions. The precursor m/z range was changed to 500-740 m/z to fit the measuring parameters.  Proteome analysis. Perseus (2.0.9.0) was used to log2 transform LFQ intensities, replace missing values from normal distribution and construct the volcano plots. (Tyanova, S. et al. The Perseus computational platform for comprehensive analysis of (prote)omics data. Nat. Methods 13, 731–740 (2016))."],"omics_type":["Proteomics"],"labhead":["Pavel Kielkowski"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["LMU Munich, Department of Chemsitry"],"species":["Mus Musculus (mouse)"],"submitter_mail":["pavel.kielkowski@cup.lmu.de"],"publication":["10.1186/S12974-026-03926-9"],"submitter_affiliation":["LMU Munich"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Chronic colitis induces a diverse neuroinflammatory fingerprint and myeloid cell-mediated dopaminergic neuron loss in the midbrain","description":"Chronic gut inflammation is associated with neuroinflammation and brain diseases. Yet, the regional pattern and single-cell resolution of the brain immune response to chronic gut inflammation remains elusive. Combining confocal microscopy and multiomic analyses, we observed that chronic colitis-derived systemic inflammation results in a midbrain-specific inflammatory response characterized by an inflammatory shift of microglial clusters, CD8+ T cell extravasation, and increased numbers of vessel-associated neutrophil granulocytes. Myeloid cell targeting after colitis onset resulted in a 67% reduction of midbrain microglia and prevented dopaminergic neuron loss in the substantia nigra pars compacta. Collectively, we provide the first single-cell resolution of an innate and adaptive immune response to chronic gut inflammation in the midbrain and identified a detrimental role of myeloid cells in midbrain dopaminergic neuron loss. These results substantially advance the understanding of the gut-immune-brain axis that links peripheral inflammation to distinct neuroinflammatory and neurodegenerative processes related to Parkinson’s 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