Prideapplication/xmlftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/checksum.txtftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/636.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/281.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/599.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/285.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/607.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/580.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/288.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/592.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/580.mgfftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/592.mgfftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/288.mgfftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/281.mgfftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/599.mgfftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/285.mgfftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/636.mgfftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/607.mgfftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/599.mzTabftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/288.mzTabftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/636.mzTabftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/592.mzTabftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/281.mzTabftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/580.mzTabftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/285.mzTabftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065313/607.mzTabprimaryOK200fushimi.k.2b47@m.isct.ac.jpKai FushimiMass SpectrometryTop-down proteomicsHumanLc-msSerumTwo-dimentional gel electrophoresishttps://www.ebi.ac.uk/pride/archive/projects/PXD065313Blood SerumPretreatment of serum sample before proteomic analysis Highly abundant proteins in serum were removed using affinity columns since they can interfere with the analysis by masking low-abondance protein in serum. Albumin and IgG were selectively depleted from the serum using the Aurum serum protein mini kit (Bio-Rad) removed. Furthermore, 14 highly abundant proteins remaining in the sample were removed with Multiple Affinity Removal Spin Cartridge Human 14 (Agilent). The depleted fraction was then concentrated to a final volume of 100 μL using a Vivaspin 2 MWCO 3000 (Cytiva). Concentrated samples were further purified to remove contaminants using a 2D clean up kit (Cytiva) and protein concentration was quantified with the 2D quant kit (Cytiva). All procedure were performed according to the manufactures’ protocols. Two-dimensional gel electrophoresis(2DE) 2-DE experiments were conducted according to the method described in a previous study[31]. For 2-DE, 15 μg of protein sample dissolved in Destreak Rehydration Solution (Cytiva) was used. The proteins sample was loaded onto an Immobiline Drystrip(7cm, pH 3-10, Cytiva) at room temperature. Isoelectric focusing was performed under the following conditions: (i) 0-300 V for 30min; (ii) 300-1000 V for 60 min; (iii) 1000-5000V for 90 min; (iiii) 5000V for 36 min. The gel strips containing proteins separated by isoelectric points were equilibrated in equilibration buffer [6 M urea; 1.5 M Tris-Hydrochloric Acid (Tris- HCl), pH 8.8; 30% v/v glycerol; 2% sodium dodecyl sulfate(SDS)]. For the first 15 min, the strips were reduced in equilibration buffer containing 1 % (w/v) dithiothreitol (DTT). For the next 15 min, they were alkylated in equilibration buffer containing 4.5% iodoacetamide (IAA). The secondary-dimension electrophoresis was carried out using NuPAGE 4-12% Bis-Tris ZOOM GEL (Thermo Fisher Scientific). Gels were set in XCell-SureLock (Thermo Fisher Scientific) and run at 200 V, 2mA for 40 min. SYPRO RUBY stain (Invitrogen) was used for staining, and the stained gels were scanned using Typhoon FLA 9500 (Cytiva). The resulting 2-DE images were analyzed using a gel analysis software, Melanie (Cytiva) and spot detection was performed on all gel images. The %vol, representing the percentage contribution of each protein spot to total protein volume, was obtained and used for subsequent statistical analysis.PrideNot availableIn gel tryptic digestion Significant spots identified in the statistical analysis were automatically excised from the gels by the Ettan Spot Picker (Cytiva) for subsequent protein identification by mass spectrometry. The excised gel plugs were reduced and alkylated with 100mM DTT and 50mM IAA, respectively. Protein-containing gel plugs were incubated with trypsin (+) solution [20ug/µL trypsin (Trypsin Gold, Mass Spectrometry Grade, Promega), 40 mM ammonium bicarbonate, 0.2mM HCl, 5mM calcium chloride(CaCl2) and 10% acetonitrile (ACN)] for 5 min at room temperature, and then incubated at 37℃ for overnight with trypsin (-) solution, which is consisted of same components as the trypsin (+) solution except for the absence of trypsin. For peptide extraction, supernatants were collected after incubating the digested gels with the following solvents, in order, for 10 min at room temperature: ultra-pure water, 60% ACN, 80%ACN, 100%ACN. The collected peptide solutions were concentrated to approximately 2μL using a Smart Evaporator C10 (BioChromato, Japan). Prior to mass spectrometry, peptide solution was desalted using C-tip (AMR) according to the manufacturer’s protocol. Protein identification by LC-MS/MS Protein contained in significant protein spots were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS). Desalted peptide samples were dissolved in TFA-A (0.1 trifluoroacetic acid (TFA), 2% ACN in ultra-pure water). The peptide solution was injected into LC (Vanquish Neo,Thermo Fisher Scientific) equipped with an AURORA Elite column (75 μm × 15 mm, packed with 1.7 μm particles). Peptides were separated and eluted using two mobile phases: solvent A (ultrapure water including 1 % formic acid) and solvent B (80% acetonitrile including 1 % formic acid). The gradient condition was set to change from 5% to 57% B buffer over 20 min with 0.3μL flow rate. Peptide were ionized using the electrospray ionization (ESI) technique and analyzed by a mass spectrometer (Orbitrap Exploris 480, Thermo Fisher Scientific). Data were analyzed using NIMS Proteome Discoverer 3.1 software (Thermo Fisher Scinetific). Protein identification was performed using MASCOT (Version 2024_3, Matrix Science, United Kingdom) and the Swiss-Prot database. The following parameters were applied for the mass spectrometry analysis: (1) precursor ion mass range: 350- 5000 Da, (2) mass tolerance:10.0 PPM, (3) Fixed modification: (4) carbamidomethylation of Cys residues, (4) variable modification: (5) oxidation of Met residues. Proteins were filtered using the following exclusion criteria: (1) FDR > 0.01, (2) common contaminants, such as keratin, potentially introduced during sample preparation.ProteomicsKai FushimiCOMPLETEDepartment of Life Science and Technology, Graduate School of Life Science and Technology Institute of Science TokyoHomo Sapiens (human)42022054 Fushimi K, Kondo T, Ikegami N, Yamada M, Wong SY, Sakamaki-Sunaga M, Hayashi N. Serum Proteomics of Multiple Menstrual Symptoms in Female Athletes: A Pilot Study. FASEB Bioadv. 2026 8:e70109 10.1096/fba.2026-00002fushimi.k.2b47@m.isct.ac.jpTokyo Institute of Technology, Grd of Life science and technologyJapan10.6019/PXD065313Menstrual symptoms, including primary dysmenorrhea and premenstrual syndrome, are significant problems affecting women's health condition. However, their biological functions are still unclear. The objective of this study was to elucidate proteins related to menstrual symptoms with high-performance two-dimensional gel electrophoresis (2DE). Serum samples were collected once a week over 5 weeks. At the same time, 46 types of menstrual symptoms were evaluated using a menstrual distress questionnaire (MDQ) on a scale of 0-4 (0: not at all, closer to 4: very strongly). 2DE images were obtained from the serum of participants with continuous menstrual phases, including the luteal, menstrual, and follicular phases. Multiple regression analysis was conducted to identify proteins that change in response to the interaction between menstrual phase and menstrual symptoms. As a result, six symptoms were associated with specific proteins (muscle stiffness with serine protease-1; general aches and pains with junction plakoglobin; tension with transferrin, ceruloplasmin, and desmoglein; depression with kininogen-1; distractibility with dermcidin; take naps; stay in bed with transferrin and hemopexin). These results indicate that various menstrual symptoms may have different underlying mechanisms. Further research into these proteins may lead to novel understanding of menstrual symptoms and support more effective health management for women.Serum Proteomics of Multiple Menstrual Symptoms in Female Athletes: A Pilot Study.Fushimi Kai K, Kondo Tasuku T, Ikegami Nodoka N, Yamada Mizuki M, Wong Sing Ying SY, Sakamaki-Sunaga Mikako M, Hayashi Nobuhiro NfalseSerum proteomics of multiple menstrual symptoms in female athleteMenstrual symptoms, including primary dysmenorrhea and premenstrual syndrome, are significant problems affecting women’s health condition. However, their biological functions are still unclear. The objective of this study was to elucidate proteins related to menstrual symptoms with high-performance two-dimensional gel electrophoresis (2DE). Serum samples were collected once a week over five weeks. At the same time, 46 types of menstrual symptoms were evaluated using a menstrual distress questionnaire (MDQ) on a scale of 0-4 (0:no symptom, closer to 4:severe). 2DE images were obtained from the serum of participants with continuous menstrual phases, including the luteal, menstrual and follicular phases. Multiple regression analysis was conducted to identify proteins that change in response to the interaction between menstrual phase and menstrual symptoms. As a result, six symptoms were associated with specific proteins (muscle stiffness with serin protease-1; general aches and pains with junction plakoglobulin; tension with transferrin, ceruloplasmin and desmoglein; depression with kininogen-1; distractible with dermcidin; tendency to take a nap or stay in bed with transferrin and hemopexin). These results indicate that various menstrual symptoms may have different underlying mechanisms. Further research into these proteins may lead to novel understanding of menstrual symptoms and support more effective health management for 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