{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074993/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074993/XA06388DA_cko_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074993/XA06388DA_cko_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074993/XA06388DA_Flox_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074993/XA06388DA_Flox_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074993/XA06388DA_Flox_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074993/XA06388DA_cko_3.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD074993/search.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["altas_zhang@163.com"],"submitter":["yonghui chen"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":["Not available"],"submitter_keywords":["phagocytosis","tfe3","htr2b","Ischemic stroke; monocyte-derived macrophages; htr2b; tfe3; phagocytosis","Ischemic stroke","monocyte-derived macrophages"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074993"],"tissue":["Brain"],"sample_protocol":["At 3 days after transient middle cerebral artery occlusion (tMCAO), mice were deeply anesthetized and perfused with cold phosphate-buffered saline (PBS) to remove circulating blood cells. The ipsilateral brain hemispheres were rapidly dissected and mechanically dissociated into small pieces, followed by enzymatic digestion using a neural tissue dissociation kit according to the manufacturer’s instructions. Single-cell suspensions were filtered through a 70-μm cell strainer to remove debris and centrifuged to obtain cell pellets. To enrich brain myeloid cells, CD11b⁺ cells were isolated using magnetic-activated cell sorting (MACS). Briefly, cell suspensions were incubated with anti-CD11b microbeads, washed, and passed through magnetic columns. The purity of isolated CD11b⁺ cells was assessed by flow cytometry and consistently exceeded 90%. Isolated cells from Htr2bΔLyz2 mice and Htr2b^fl/fl littermate controls were processed in parallel to minimize batch effects. The resulting peptides were desalted using C18 solid-phase extraction columns, vacuum-dried, and reconstituted in loading buffer for liquid chromatography–tandem mass spectrometry (LC-MS/MS) analysis. Peptide separation was performed using a high-performance nano-LC system coupled online to a high-resolution mass spectrometer operating in data-dependent acquisition (DDA) mode. MS1 scans were acquired at high resolution, followed by MS/MS fragmentation of the most intense precursor ions. All samples were randomized prior to LC-MS/MS acquisition, and technical replicates were included to assess analytical reproducibility. This workflow ensured robust, unbiased proteomic profiling of brain myeloid cells following ischemic stroke."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw mass spectrometry data files generated from LC-MS/MS acquisition were processed using standard proteomics data analysis pipelines. Spectra were searched against the Mus musculus reference protein database using a database search engine with trypsin specified as the proteolytic enzyme and up to two missed cleavages allowed. Carbamidomethylation of cysteine was set as a fixed modification, while oxidation of methionine was included as a variable modification. Mass tolerance parameters for precursor and fragment ions were set according to instrument specifications. Peptide-spectrum matches (PSMs) and protein identifications were filtered using a false discovery rate (FDR) threshold of 1% at both peptide and protein levels to ensure high-confidence identifications. Following database searching, a series of quality control (QC) assessments were performed to evaluate data reliability and consistency. These included analysis of peptide length distribution, peptide number distribution per protein, protein sequence coverage, and molecular weight distribution of identified proteins. The majority of identified peptides ranged from 7 to 20 amino acids, consistent with typical tryptic digestion efficiency and fragmentation behavior in LC-MS/MS-based proteomics. The observed peptide length distribution met standard quality control criteria, indicating high digestion efficiency and reliable spectral matching. For quantitative analysis, protein abundance was calculated based on the summed intensities of corresponding peptides. The search results provided Normalized intensity values for each protein across all samples, representing intensity values corrected for inter-sample variation. To enable relative quantification, protein intensities were further normalized by mean-centering across samples. To assess reproducibility and consistency between biological or technical replicates, multiple statistical analyses were applied. Pearson’s correlation coefficient (PCC) was calculated to evaluate linear correlations between samples. Principal component analysis (PCA) was performed to visualize global variance and sample clustering. Additionally, the relative standard deviation (RSD) was computed for each protein to assess quantitative stability across replicates. Together, these analyses demonstrated high reproducibility and robustness of the proteomic dataset."],"omics_type":["Proteomics"],"labhead":["Yueman zhang"],"instrument_platform":[""],"labhead_affiliation":["Department of Anesthesiology, Renji Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["cyhgordon@163.com"],"submitter_affiliation":["Renji Hospital, Shanghai Jiao Tong University School of Medicine‌"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"Htr2b Enhances the Phagocytosis of Brain Macrophages and Alleviates Brain Injury after Stroke","description":"Brain myeloid cells, including infiltrating monocyte-derived macrophages (MDMs) and resident microglia play critical roles in regulating debris clearance following ischemic brain injury, shaping neuroinflammation evolution and neurological outcome, yet the underlying mechanism remains elusive. In this study, using single-cell RNA sequencing and fate mapping, we identified serotonin receptor Htr2b+ MDMs as a pivotal subgroup involved in resolving neuroinflammation within the ischemic penumbra. In addition, we find significant accumulation of Htr2b+ MDMs with enhanced phagocytosis and inflammation-resolving gene signatures in the peri-infarct region. Mechanistically, Htr2b activation promotes nuclear translocation of Tfe3, a key lysosomal regulator, enhancing lysosomal biogenesis and supporting sustained phagocytic activity. Myeloid-specific Htr2b ablation impairs debris clearance, exacerbates neuroinflammation and ischemic injury, while pharmacological Htr2b agonism or Tfe3 activation restores the lysosomal competence of brain MDMs and improves post-stroke neurological outcome. In conclusion, we demonstrate a novel Htr2b+ MDM subset that integrates serotonin signaling to license their intrinsic phagocytosis function, alleviating ischemic brain 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