{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066510/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066510/S3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066510/S1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066510/M1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066510/C3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066510/S2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066510/C1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066510/C4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066510/M2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066510/M3.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066510/search.rar"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["shlhmu2018@163.com"],"submitter":["Hongli Sun"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":[""],"submitter_keywords":["neutrophil extracellular traps","Myocardial ischemia-reperfusion injury; sleep fragmentation; neutrophil extracellular traps; cardiac microvascular endothelial cells; cuproptosis","sleep fragmentation","Myocardial ischemia-reperfusion injury","cardiac microvascular endothelial cells","cuproptosis"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD066510"],"tissue":["Heart"],"sample_protocol":["1.Protein extraction 300 μL of 8M urea was added to the sample and the protease inhibitor was added at 10% of the lysate.After centrifuging at 14,100×g for 20 min, thesupernatant was collected.The protein concentration was determined using Bradford method，rest was frozen to -80℃. 2.Protein digestion and desalination A 100 µg aliquot of extracted proteins from each sample was then subjected to reduction. Adding 200 mM dithiothreitol (DTT) solution and incubating at 37 °C for 1 h. The sample was diluted 4 times by adding 25 mM ammonium bicarbonate (ABC) buffer.Then adding trypsin (trypsin: protein =1:50) and incubating at 37℃ overnight. The next day, adding 50μL 0.1% FA to terminate the digestion.Take 100μl 100% ACN to wash the C18 column, and centrifuge at 1200rpm for 3min. Wash the column once with 100 μl of 0.1% FA and centrifuge at 1200 rpm for 3 min. Replace the EP tube, add the sample, and centrifuge at 1200rpm for 3min. Wash the column twice with 100 μl of 0.1% FA and centrifuge at 1200 rpm for 3 min. Wash once with 100 μl of pH 10 water. Replace the EP tube and elute with 70% ACN. The eluents of each sample were combined and lyophilized. Store at -80°C until loading. 3.LC-MS/MS Analysis  Nanoflow LC-MS/MS analysis of tryptic peptides was conducted on a quadrupole Orbitrap mass spectrometer (Orbitrap Exploris™ 480, Thermo Fisher Scientific, Bremen, Germany) coupled to an EASY nLC 1200 ultra-high pressure system (Thermo Fisher Scientific) via a nano-electrospray ion source. 500 ng of peptides were loaded on a 25 cm column (150 μm inner diameter, packed using ReproSil-Pur C18-AQ 1.9- µm silica beads; Promegene Biotech Co.,Ltd, Guangzhou, China). Peptides were separated using a gradient from 8 to 12% B in 7 min ,then12% to 30 % B in 48 min and stepped up to 40% in 10 min followed by a 15 min wash at 95% B at 600 nl per minute where solvent A was 0.1% formic acid in water and solvent B was 80% ACN and 0.1% formic acid in water. The total duration of the run was 60 min. Column temperature was kept at 60 °C using an in-house-developed oven. Briefly, the mass spectrometer was operated in “top-40” data-dependent mode, collecting MS spectra in the Orbitrap mass analyzer (60,000 resolution, 350–1200 m/z range) with an automatic gain control (AGC) target of 3E6 and a maximum ion injection time of 50 ms. The most intense ions from the full scan were isolated with an isolation width of 1.6 m/z. Following higher-energy collisional dissociation (HCD) with a normalized collision energy (NCE) of 27, MS/MS spectra were collected in the Orbitrap (15,000 resolution) with an AGC target of 5E4 and a maximum ion injection time of 22 ms. Precursor dynamic exclusion was enabled with a duration of 16 s."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Sequence Database Searching  All RAW files were analyzed using the Proteome Discoverer suite (version 2.4, Thermo Fisher Scientific). MS2 spectra were searched against the UniProtKB Mus musculus (Mouse) [10090]-87492-20250414. The Sequest HT search engine was used, and parameters were specified as follows: fully tryptic specificity, maximum of two missed cleavages, minimum peptide length of 6, fixed carbamidomethylation of cysteine residues (+57.02146Da), variable modifications for oxidation of methionine residues (+15.99492Da), precursor mass tolerance of 15 ppm and a fragment mass tolerance of 0.02Da for MS2 spectra collected in the Orbitrap. Percolator was used to filter peptide spectral matches and peptides to a false discovery rate (FDR) of less than 1%. After spectral assignment, peptides were assembled into proteins and were further filtered based on the combined probabilities of their constituent peptides to a final FDR of 1%. As default, the top matching protein or ‘master protein’ is the protein with the largest number of unique peptides and with the smallest value in the percent peptide coverage (that is, the longest protein). Only unique and razor (that is, parsimonious) peptides were considered for quantification.  Bioinformatics analysis Bioinformatic analysis were carried out with Microsoft Excel and R statistical computing software. Hierarchical clustering analysis and volcano figure were executed with statistical language R. To annotate the sequences, information was extracted from UniProtKB, Kyoto Encyclopedia of Genes and Genomes (KEGG) , and Gene Ontology (GO) . GO and KEGG enrichment analyses were carried out with the Fisher’s exact test, and FDR correction for multiple testing was also performed. GO terms were grouped into three categories: biological process (BP), molecular function (MF), and cellular component (CC) . Enriched GO and Kegg pathways were nominally statistically significant at the Fisher exact test p<0.01. Construction of protein–protein interaction (PPI) networks were also conducted by using the STRING database with the Cytoscape software ."],"omics_type":["Proteomics"],"labhead":["Hongli Sun"],"instrument_platform":[""],"labhead_affiliation":["Department of Pharmacology, Harbin Medical University, Heilongjiang 163319, China"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["shlhmu2018@163.com"],"publication":["42109881 Shi P, Sha Y, Guan X, Wu J, Yang J, Min D, Wang C, Cao Y, Wang X, Qiao Y, Sun H. Neuromodulation and Copper Chelation Reverse Sleep Fragmentation-Aggravated Myocardial Ischemia-Reperfusion Injury by Targeting NET-Induced Endothelial Cuproptosis. Research (Wash D C). 2026 9:1266 10.34133/research.1266"],"submitter_affiliation":["Harbin Medical Universiy"],"submitter_country":["China"],"pubmed_abstract":["This study sought to investigate the link between sleep disorders and cardiac microvascular injury in myocardial ischemia-reperfusion injury (MI/RI) mice. Mice were subjected to a sleep deprivation protocol within a designated chamber. During the light phase (ZT0 to ZT12), a sweep bar moved across the cage floor at 2-min intervals, whereas it remained static throughout the dark phase (ZT12 to ZT24), with this routine maintained for 16 weeks. Subsequently, an MI/RI model was established to assess the extent of cardiac microvascular injury, and the underlying mechanisms were explored via proteomic analyses. It was demonstrated that 16 weeks of sleep fragmentation (SF) intensified cardiac microvascular damage in MI/RI mice. From a mechanistic perspective, SF was found to induce sympathetic hyperactivity, elevate plasma epinephrine levels, and consequently facilitate neutrophil chemotaxis and the generation of neutrophil extracellular traps (NETs). Moreover, the findings revealed that NETs suppressed Atox1 expression, impaired ATP7A-mediated copper transport, and contributed to copper accumulation within cardiac microvascular endothelial cells (CMECs) and oxidative stress. This copper overload further augmented cuproptosis, while these pathological alterations were shown to be reversible through sympathetic denervation, vagal electrical stimulation (ES), targeted delivery of copper chelators, or the inhibition of NETs. Overall, our data established that SF exacerbated MI/RI by promoting copper overload in CMECs. This study elucidated a molecular pathway through which sleep disturbances aggravated cardiac microvascular damage and suggested prospective targets for treatment strategies."],"pubmed_title":["Neuromodulation and Copper Chelation Reverse Sleep Fragmentation-Aggravated Myocardial Ischemia-Reperfusion Injury by Targeting NET-Induced Endothelial Cuproptosis."],"pubmed_authors":["Shi Pilong P, Sha Yuetong Y, Guan Xue X, Wu Jiawei J, Yang Jing J, Min Dongyu D, Wang Cong C, Cao Yonggang Y, Wang Xinran X, Qiao Yuandong Y, Sun Hongli H"],"additional_accession":[]},"is_claimable":false,"name":"Sleep fragmentation exacerbates cardiac microvascular endothelial cell cuproptosis via promoting neutrophil extracellular trap formation in myocardial ischemia-reperfusion injury","description":"Objective: This study aimed to investigate the relationship between sleep disorders and cardiac microvascular injury in myocardial ischemia-reperfusion injury (MI/RI) mice. Design: Mice were placed in a sleep deprivation chamber. The sweep bar moved along the bottom of the cage every 2 min during the light cycle (ZT0-12) and was stationary during the dark cycle (ZT12-24) for 16 weeks. Then, a MI/RI model was prepared to evaluate cardiac microvascular injury and investigate its specific mechanism via proteomics analysis. Results: Here, we showed that 16 weeks of sleep fragmentation (SF) exacerbated cardiac microvascular injury in MI/RI mice. Mechanistically, we found that SF promotes sympathetic overactivity, increases the level of norepinephrine (EPI) in plasma, thereby promotes the chemotaxis of neutrophils (NEs) and formation of Neutrophil extracellular traps (NETs). Furthermore, our data indicated that NETs inhibit Atox1 expression and leads to impaired ATP7A related copper transport and copper overload in cardiac microvascular endothelial cells (CMECs). Copper overload further leads to exacerbated cuproptosis, and these effects can be rescued by excision of the sympathetic nerve, targeted administration of copper chelating agent or NETs inhibitor. Conclusions: This study demonstrated that SF exacerbated MI/RI by promoting copper overload in CMECs. Our study elucidated one of the molecular mechanisms by which sleep disorders aggravate cardiac microvascular injury and suggested possible tar gets for 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