{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057655/checksum.txt"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057655/251.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057655/392.mzML"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057655/251.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057655/392.raw"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057655/251.mzid.gz","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057655/392.mzid.gz"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["fushimi.k.2b47@m.titech.ac.jp"],"submitter":["Kai Fushimi"],"technology_type":["Mass Spectrometry","Top-down proteomics"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD057655"],"tissue":["Blood Serum"],"sample_protocol":["Sample preparation for two-dimensional gel electrophoresis(2-DE) In order to remove high abundant protein, Aurum serum protein mini kit (Bio-Rad) and Multiple Affinity Removal Spin Cartridge Human 14 (Agilent) were used. Firstly, albumin and IgG were removed by Aurum serum protein mini kit. After that, 14 highly abundant proteins were selectively removed by Multiple Affinity Removal Spin Cartridge Human 14. The experiments were conducted according to the manufacture’s protocols. After depletion of high abundant proteins, the samples were then concentrated using a Vivaspin 2 MWCO 3000 (Cytiva) to a final volume of 100 μL. For protein purification, a 2D clean up kit (Cytiva) was used to remove potential impurities in the sample and a 2D Quant kit (Cytiva) was used for protein quantification. Two-dimensional gel electrophoresis(2-DE) Protein samples were dissolved in Destreak Rehydration Solution (Cytiva) and 15μg protein was loaded to a Immobiline Drystrip (7 cm, pH 3-10, Cytiva). Proteins were first separated by isoelectric focusing (IEF) using an Ettan IPGphor3 (Cytiva) under these conditions: (i) 0-300 V, 30 min (ii) 300-1000 V, 60 min (iii) 1000-5000V, 90 min (iiii) 5000V, 36 min. After IEF separation, gel strips 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)] in 1% w/v dithiothreitol (DTT) for reduction followed by iodoacetamide (IAA) for alkylation. For second dimension separation, NuPAGE 4-12% Bis-Tris ZOOM GEL（Thermo Fisher Scientific）was used. The electrophoresis was run using XCell-SureLock（Thermo Fisher Scientific）at 200 V, 2 mA for 40 min. The gels were stained with SYPRO RUBY stain (Invitrogen) and scanned using Typhoon FLA 9500 (Cytiva). 2-DE images were analyzed using a gel analysis software, Melanie (Cytiva), and spots on all 2-DE images were detected. Both non-normalized volume (Vol) and percentage of volume contribution (%vol) of all spots were acquired. %vol is the relative volume of a spot determined by normalizing the spot’s volume to the total volume of all spots in an image. In-gel digestion Spots determined to be significantly changed in the statistical analysis were subjected to mass spectrometry analysis. These spots were first excised by an automated spot picker, the Ettan Spot Picker (Cytiva), before they were in-gel digested with trypsin. 2-DE images from Fig 1 were used for this experiment. Excised gel plugs were then incubated in 50% 400 mM ammonium bicarbonate [pH 8.1], 50% acetonitrile (ACN), for 20 min at room temperature (R.T.). Next, the gel plugs were reduced with 100 mM DTT for 30 min at 60℃, and then alkylated with 50 mM IAA for 30 min at room temperature in the dark. After 5 min incubation in ACN at R.T, trypsin (+) solution[20 ng/µL trypsin (Trypsin Gold, Mass Spectrometry Grade, Promega), 40 mM ammonium bicarbonate, 0.2 mM HCl, 5 mM calcium chloride (CaCl2) and 10% acetonitrile (ACN)] were added and incubated for 5 min at R.T. Finally, the gel plugs were incubated in trypsin (-) solution containing same components as trypsin(+) but without trypsin at 37℃ for overnight. The next day, the supernatant was collected. The gel plugs were incubated in ultra-pure water for 10 min, and the supernatant was pooled into the same tube from the previous step. Following that, 60% ACN was added and incubated for 20 minutes, and the supernatant was collected in the same tube again. This step was repeated with 80% ACN and 100% ACN. Collected supernatants were concentrated by Smart Evaporator C10 (BioChromato, Japan) to approximately 2 μl. Peptide desalting before mass spectrometry was performed using C18 column (Nikkyo Technos, Co., Ltd.). The procedure was carried out according to the manufacturer’s guideline."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Protein identification was performed by a liquid chromatography–tandem mass spectrometry (LC-MS/MS). The samples after desalination were concentrated again and replace with TFA-A(0.1 trifluoroacetic acid(TFA), 2%ACN in ultra-pure water). These samples were injected into LC(Thermo Fisher Scientific, MA, US) equipped with a C18 column(300 µm diameter × 5 mm length, packed with 5 µm particles). As mobile phase, H2O including 0.1% formic acid(A) and 80% acetonitrile including 0.1% formic acid were prepared. The peptides separation and elution were conducted under the condition of 0.3μl/min flow rate with a gradient 5%-57% in B buffer for 20 min. Eluted peptides were ionized by electrospray ionization and the generated ions were sent to analyzed quadrupole orbital trap mass spectrometer (Orbitrap Exploris 480, Thermo Fisher Scientific) and analyzed with NIMS Proteome Discoverer 2.0 software (Thermo Fisher Scientific). In order to identify protein candidates from MS/MS spectra, MASCOT(Version 2.5.1, Matrix Science, United Kingdom) and Swiss-Prot database (SwissProt 2019_11, 561,568 sequences; 201,997,950 residues) using the digestion enzyme trypsin were used. The parameters are shown follows: mass range of the precursor ion was 375–1500 m/z; mass tolerance was set to 10.0 PPM; Carbamidomethylation of Cys residues as static modification and Met oxidation as dynamic modification were allowed. Identified proteins which match following conditions were excluded from protein candidates: did not achieve a false discovery rate(FDR) of 0.01; protein candidates identified as Keratin due to possibility of contamination during experiment."],"omics_type":["Proteomics"],"labhead":["Kai Fushimi"],"instrument_platform":[""],"labhead_affiliation":["School of Life Science and Technology, Institute of Science Tokyo"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)"],"publication":["41986428 Fushimi K, Kondo T, Ikegami N, Yamada M, Wong SY, Sakamaki-Sunaga M, Hayashi N. Proteomics to reveal relationship between menstrual cycle and subjective conditions. Sci Rep. 2026 16(1):17482 10.1038/s41598-026-47566-8"],"submitter_mail":["fushimi.k.2b47@m.isct.ac.jp"],"submitter_affiliation":["Tokyo Institute of Technology, Grd of Life science and technology"],"submitter_country":["Japan"],"doi":["10.6019/PXD057655"],"pubmed_title":["Proteomics to reveal relationship between menstrual cycle and subjective conditions."],"pubmed_authors":["Fushimi Kai K, Kondo Tasuku T, Ikegami Nodoka N, Yamada Mizuki M, Wong Sing Ying SY, Sakamaki-Sunaga Mikako M, Hayashi Nobuhiro N"],"additional_accession":[]},"is_claimable":false,"name":"Proteomics to reveal relationship between menstrual cycle and subjective conditions: a pilot study","description":"The menstrual cycle is a vital aspect of women’s health, influencing both physical and mental well-being. Many women experience premenstrual symptom (PMS), such as stomachache and irritability, which can impact daily life. However, the underlying biological mechanisms remain poorly understood, indicating a need for further research. This study aimed to explore the relationship between proteins and subjective condition related to menstrual cycle using two-dimensional gel electrophoresis (2-DE) technique. Serum samples were collected weekly from 42 female students over a period of 5 weeks, resulting in a total of 210 2-DE images. At the same time, two female hormones -- estradiol and progesterone -- were measured. On the morning of every blood collection day, participants rated their subjective condition (SC) score on a scale of 1-5, with scores closer to 5 indicating better condition. These data were categorized into three groups: scores of 1-2 as SC Low, a score of 3 as SC Mid, and scores of 4-5 as SC High. The Steel-Dwass test comparing these groups revealed that two proteins related to oxidative stress, kallistatin and transferrin, are significantly higher in the SC high group compared to both the SC Low and SC Mid groups. Although the specific symptoms that primarily affect SC are not known, oxidative stress is believed to be associated with fatigue and migraine. This study demonstrates that proteins linked to oxidative stress reflect women’s subjective condition during the menstrual cycle. Notably, the evaluation of discernment ability using receiver operating characteristic curve (ROC) shows kallistatin and transferrin exhibit greater discernment than conventional hormonal markers for identifying negative or positive conditions. Investigating well-being related to the menstrual cycle through the lens of proteomics proves to be valuable approach, and targeting these proteins may lead to effective health management strategies for 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