{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/29_O_V_27.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/27_O_V_25.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/5_T_G_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/31_O_V_28.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/11_T_V_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/6_T_G_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/15_T_V_15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/13_T_V_13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/17_T_V_17.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/33_O_V_30.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/24_O_G_23.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/22_O_G_21.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/2_T_G_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/28_O_V_26.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/1_T_G_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/7_T_G_7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/10_T_G_10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/32_O_V_29.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/20_O_G_19.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/3_T_G_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/9_T_G_9.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/12_T_V_12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/16_T_V_16.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/14_T_V_14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/18_T_V_18.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/4_T_G_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/23_O_G_22.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/25_O_G_24.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/21_O_G_20.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/8_T_G_8.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/20240626_104054_Arterie.sne","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD053441/Arteries.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["a.petretto@gmail.com"],"submitter":["Martina Bartolucci"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Migraine surgery","Migraine","Vascular anomaly","Proteomics"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD053441"],"tissue":["Artery"],"sample_protocol":["The samples were washed in PBS and then dissociated in 500 μL RPMI with 0.25 mg/mL Liberase TL enzyme (Roche) for 2 hours at 37°C and 300 rpm shaking. After dissociation, the samples were centrifuged at 1000 g for 10 minutes, and the pellet was washed with PBS before being resuspended in 100 μL guanidine lysis buffer (6M GdmCl, 10mM TCEP, 40mM CAA, 100mM Tris pH 8). The resuspended pellets were homogenized using a TissueLyser II (QIAGEN) with two cycles of four minutes each. Subsequently, they were lysed at 95°C for 10 minutes at 1000 rpm and sonicated with an Ultrasonic Processor UP200St (Hielscher) for three cycles of 30 seconds each. After centrifugation at 10,000 g for 10 minutes, the supernatants were retained for analysis. Protein digestion was performed using the PAC method automated on a KingFisher™ Apex robot (Thermo Fisher Scientific) in a 96-well format, as described in (https://doi.org/10.1074/mcp.TIR119.001906) with minor modifications.The digested peptides were analyzed on the Evosep One system using an EASY spray column (150 μm x 15 cm, Thermo Scientific) and the pre-programmed gradient of 30 samples per day, with a flow rate of 220 nl/min. The column temperature was maintained at 40°C and interfaced online with the Orbitrap Exploris 480 MS (Thermo Scientific) with FAIMS Pro Duo Interface (Thermo Scientific). MS analysis was performed in DIA mode. FAIMS CV was set to -45 at standard resolution. Full MS resolution was set to 120,000 in a range between 375 and 1500 m/z with an AGC target of 300% and a maximum IT set to Auto. AGC target value for fragment spectra was set at 1000%. Forty windows of 15 Da were used with an overlap of 1 Da. Resolution was set to 30,000 and IT to Auto. Normalized collision energy was set at 30%. All data were acquired in profile mode using positive polarity."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["All DIA raw files were processed with Spectronaut version 17 (DOI: 10.1074/mcp.M114.044305) using a library-free approach (directDIA). Enzymes/Cleavage Rules were set to Trypsin/P, LysC. The library was generated against the Uniprot Human database (release UP000005640_9606 November 2022). Carbamidomethylation was selected as a fixed modification, and methionine oxidation and N-terminal acetylation were selected as variable modifications. The false discovery rates (FDRs) of peptide-spectrum matches (PSMs) and peptide/protein groups were set to 0.01. For quantification, Precursor Filtering was set to Identified (Q-value), Imputation Strategy was set to Run Wise Imputing, and MS2 was chosen as the quantity MS-level."],"omics_type":["Proteomics"],"labhead":["Andrea Petretto"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["IRCCS Istituto G Gaslini"],"species":["Homo Sapiens (human)"],"publication":["10.1007/S00238-024-02256-4"],"submitter_mail":["smartibartolucci@gmail.com"],"submitter_affiliation":["IRCCS Gaslini"],"submitter_country":["Italy"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic Vascular Anomalies detected during Migraine Surgery","description":"BACKGROUND: Many patients with temporal or occipital migraines experience localized and throbbing pain, suggesting potential involvement of extracranial vessels. This study aimed to assess the presence or absence of vascular anomalies through proteomic analysis of biopsies. METHODS: Intraoperatively, thirty-three biopsies were collected, including 19 from the superficial temporal artery and 14 from the occipital artery, and immediately processed for proteomic analysis. RESULTS: A total of 5339 proteins were identified. Comparison of temporal arteries between younger and older patients revealed 394 significantly dysregulated proteins, with 204 upregulated in younger patients and 190 upregulated in older patients. Similarly, comparison of occipital arteries between younger and older patients revealed 325 significantly dysregulated proteins, with 91 upregulated in younger patients and 234 upregulated in older patients. CONCLUSIONS: The data collected, indicative of organic lesions, support the rationale for surgical therapy. Our results suggest differences between younger patients (showing an antiinflammatory substrate) and older patients (displaying a pro-inflammatory substrate). These findings imply that in younger patients, the local tissue response tends to counteract the inflammatory state, while in older patients, the local inflammatory state becomes chronic and 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