{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-C2-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-C1-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-B1-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-B2-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-A1-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-A2-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-E2-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-B1-02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-B2-02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-C1-02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-C2-02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-A2-02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-D1-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-E1-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-D2-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-A1-02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-C1-03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-C2-03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-D1-03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-D2-02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-D1-02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-A1-03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-B2-03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-B1-03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-E1-02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-A2-03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-E2-02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-E1-03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-D2-03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/21P59-E2-03.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/F.fasta"],"Mztab":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD081616/mzTab.mzTab"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["daniele.capitanio@unimi.it"],"submitter":["Manuela Moriggi"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["spaceflight","structural proteins","protein signaling pathways","proteomics","Skeletal muscle; proteomics; spaceflight; structural proteins; protein signaling pathways","Skeletal muscle"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD081616"],"tissue":["Skeletal Muscle"],"sample_protocol":["Protein Extraction for Label-Free LC–ESI–MS/MS Analysis. Pre- and post-flight muscle biopsies (SOL aliquots) were suspended in HEN buffer (100 mM HEPES pH 7,4, 1 mM EDTA, 0,1 mM Neocuproina) 0.1% SDS, 1% TRITON X-100, 1% phenylmethanesulfonyl fluoride (PMSF) and sonicated on ice until completely dissolved. Lysates were clarified by centrifugation at 12,000x g for 20 min at 4 C. Protein quantitation with a Pierce bicinchoninic acid (BCA) protein assay (Thermo Fisher Scientific, Rodano, Italy) was then performed. Protein extracts were processed following the filter-aided sample preparation (FASP) protocol. Each sample (200 µg) was deposited in a Microcon-30 kDa centrifugal filter unit (Merck Millipore, Burlington, MA, USA) and washed for two times by centrifugation at 14,000x g for 15 min with 200 µL of UA buffer (8 M urea, 0.1 M Tris/HCl, pH 8.5). Samples were carbamydomethylated in 100 µL of 50 mM iodoacetamide in UA buffer for 20 min, then washed for three times in 100 µL UA buffer followed by three washes in 100 µL of 50 mM ammonium bicarbonate in water. Filters were incubated with sequence grade trypsin (Promega, Madison, WI, USA) for 16 h at 37°C using a protein:trypsin ratio of 50:1. After acidification with trifluoracetic acid and desalting on C18 tips (Zip-Tip C18 micro, Merck Millipore, Burlington, MA, USA), peptide samples were vacuum concentrated, reconstituted in HPLC buffer A (0.1% formic acid) and separated on a Dionex UltiMate 3000 HPLC System with an Easy Spray PepMap RSLC C18 column (250 mm, internal diameter of 75 µm) (Thermo Fisher Scientific, Rodano, Italy), adopting a five steps acetonitrile (ACN)/formic acid gradient (5% ACN in 0.1% formic acid for 5 min, 5–35% ACN in 0.1% formic acid for 139 min, 35–60% ACN in 0.1% formic for 40 min, 60–100% ACN for 1 min, 100% ACN for 10 min, at a flow rate of 0.3 µL/min), and electrosprayed into an Orbitrap Fusion Tribrid (Thermo Fisher Scientific, Rodano, Italy) mass spectrometer. The LTQ-Orbitrap was operated in a positive mode in data-dependent acquisition mode to automatically alternate between a full scan (350–2000 m/z) in the Orbitrap (at resolution 60,000, AGC target 1,000,000) and subsequent CID MS/MS in the linear ion trap of the 20 most intense peaks from full scan (normalized collision energy of 35%, 10 ms activation). Isolation window: 3 Da, unassigned charge states: rejected, charge state 1: rejected, charge states 2+, 3+, 4+: not rejected; dynamic exclusion enabled (60 s, exclusion list size: 200)."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Mass spectra were analyzed using MaxQuant software (Max-PlanckInt. Institute of Biochemistry, Munich, Germany, version 1.6.3.3). The maximum allowed mass deviation was set to 6 ppm for monoisotopic precursor ions and 0.5 Da for MS/MS peaks. Enzyme specificity was set to trypsin/P, and a maximum of two missed cleavages was allowed. Carbamidomethylation was set as a fixed modification, while N-terminal acetylation and methionine oxidation were set as variable modifications. Spectra were searched by the Andromeda search engine against the Homo sapiens Uniprot UP000005640 sequence database (78.120 proteins, release 7 March 2021). Protein identification required at least one unique or razor peptide per protein group. Quantification in MaxQuant was performed using the built-in extracted ion chromatogram (XIC)-based label-free quantification (LFQ) algorithm using fast LFQ. The required FDR was set to 1% at the peptide, 1% at the protein, and 1% at the site-modification level, and the minimum required peptide length was set to 7 amino acids. Statistical analyses were performed using the Perseus software (Max Planck Institute of Biochemistry, Munich, Germany, version 1.4.0.6). Statistical analyses were performed using the Perseus software (v.1.4.0.6, Max Planck Institute of Biochemistry, Martinsried, Germany). For each experimental group, proteins identified in at least 80% of samples were considered. For statistical analysis, paired Student’s t-test with a p-value threshold of 0.05 was applied, and results revealed the variation of protein expression between R+0 vs. PRE SDM and R+0 vs. PRE LDM. False positives were excluded utilizing the Benjamini–Hochberg false discovery rate test."],"omics_type":["Proteomics"],"labhead":["Prof. Daniele Capitanio"],"instrument_platform":[""],"labhead_affiliation":["Department of Biomedical Sciences for Health, University of Milan, 20133 Milan, Italy"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)"],"publication":["10.3390/IJMS24044095","36835504 Blottner D, Moriggi M, Trautmann G, Hastermann M, Capitanio D, Torretta E, Block K, Rittweger J, Limper U, Gelfi C, Salanova M. Space Omics and Tissue Response in Astronaut Skeletal Muscle after Short and Long Duration Missions. Int J Mol Sci. 2023 24(4):4095 10.3390/ijms24044095"],"submitter_mail":["manuelamoriggi@yahoo.it"],"submitter_affiliation":["Laboratory of Proteomics and Lipidomics, IRCCS Ospedale Galeazzi-Sant'Ambrogio, Milan, Italy."],"submitter_country":["Italy"],"doi":["10.6019/PXD081616"],"pubmed_abstract":["The molecular mechanisms of skeletal muscle adaptation to spaceflight are as yet not fully investigated and well understood. The MUSCLE BIOPSY study analyzed pre and postflight deep calf muscle biopsies (m. soleus) obtained from five male International Space Station (ISS) astronauts. Moderate rates of myofiber atrophy were found in long-duration mission (LDM) astronauts (~180 days in space) performing routine inflight exercise as countermeasure (CM) compared to a short-duration mission (SDM) astronaut (11 days in space, little or no inflight CM) for reference control. Conventional H&E scout histology showed enlarged intramuscular connective tissue gaps between myofiber groups in LDM post vs. preflight. Immunoexpression signals of extracellular matrix (ECM) molecules, collagen 4 and 6, COL4 and 6, and perlecan were reduced while matrix-metalloproteinase, MMP2, biomarker remained unchanged in LDM post vs. preflight suggesting connective tissue remodeling. Large scale proteomics (space omics) identified two canonical protein pathways associated to muscle weakness (necroptosis, GP6 signaling/COL6) in SDM and four key pathways (Fatty acid β-oxidation, integrin-linked kinase ILK, Rho A GTPase RHO, dilated cardiomyopathy signaling) explicitly in LDM. The levels of structural ECM organization proteins COL6A1/A3, fibrillin 1, FBN1, and lumican, LUM, increased in postflight SDM vs. LDM. Proteins from tricarboxylic acid, TCA cycle, mitochondrial respiratory chain, and lipid metabolism mostly recovered in LDM vs. SDM. High levels of calcium signaling proteins, ryanodine receptor 1, RyR1, calsequestrin 1/2, CASQ1/2, annexin A2, ANXA2, and sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA1) pump, ATP2A, were signatures of SDM, and decreased levels of oxidative stress peroxiredoxin 1, PRDX1, thioredoxin-dependent peroxide reductase, PRDX3, or superoxide dismutase [Mn] 2, SOD2, signatures of LDM postflight. Results help to better understand the spatiotemporal molecular adaptation of skeletal muscle and provide a large scale database of skeletal muscle from human spaceflight for the better design of effective CM protocols in future human deep space exploration."],"pubmed_title":["Space Omics and Tissue Response in Astronaut Skeletal Muscle after Short and Long Duration Missions."],"pubmed_authors":["Blottner Dieter D, Moriggi Manuela M, Trautmann Gabor G, Hastermann Maria M, Capitanio Daniele D, Torretta Enrica E, Block Katharina K, Rittweger Joern J, Limper Ulrich U, Gelfi Cecilia C, Salanova Michele M"],"additional_accession":[]},"is_claimable":false,"name":"Space Omics and Tissue Response in Astronaut Skeletal Muscle after Short and Long Duration Missions","description":"The molecular mechanisms of skeletal muscle adaptation to spaceflight are as yet not fully investigated and well understood. The MUSCLE BIOPSY study analyzed pre and postflight deep calf muscle biopsies (m. soleus) obtained from five male International Space Station (ISS) astronauts. Moderate rates of myofiber atrophy were found in long-duration mission (LDM) astronauts (~180 days in space) performing routine inflight exercise as countermeasure (CM) compared to a short-duration mission (SDM) astronaut (11 days in space, little or no inflight CM) for reference control. Conventional H&E scout histology showed enlarged intramuscular connective tissue gaps between myofiber groups in LDM post vs. preflight. Immunoexpression signals of extracellular matrix (ECM) molecules, collagen 4 and 6, COL4 and 6, and perlecan were reduced while matrix-metalloproteinase, MMP2, biomarker remained unchanged in LDM post vs. preflight suggesting connective tissue remodeling. Large scale proteomics (space omics) identified two canonical protein pathways associated to muscle weakness (necroptosis, GP6 signaling/COL6) in SDM and four key pathways (Fatty acid -oxidation, integrin-linked kinase ILK, Rho A GTPase RHO, dilated cardiomyopathy signaling) explicitly in LDM. The levels of structural ECM organization proteins COL6A1/A3, fibrillin 1, FBN1, and lumican, LUM, increased in postflight SDM vs. LDM. Proteins from tricarboxylic acid, TCA cycle, mitochondrial respiratory chain, and lipid metabolism mostly recovered in LDM vs. SDM. High levels of calcium signaling proteins, ryanodine receptor 1, RyR1, calsequestrin 1/2, CASQ1/2, annexin A2, ANXA2, and sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA1) pump, ATP2A, were signatures of SDM, and decreased levels of oxidative stress peroxiredoxin 1, PRDX1, thioredoxin-dependent peroxide reductase, PRDX3, or superoxide dismutase [Mn] 2, SOD2, signatures of LDM postflight. Results help to better understand the spatiotemporal molecular adaptation of skeletal muscle and provide a large scale database of skeletal muscle from human spaceflight for the better design of effective CM protocols in future human deep space exploration.","dates":{"publication":"2026-07-27","submission":"2026-07-24"},"accession":"PXD081616","cross_references":{"TAXONOMY":["NEWT:68239","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:57577","NEWT:156563","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:93217","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:82569","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:1176302","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:1177","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:143292","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NCBITaxon:5204","NEWT:1916073","NEWT:1303873","NEWT:1310161","NEWT:1230383","NEWT:77133","NCBITaxon:5207","NEWT:160620","NCBITaxon:77643","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:37919","NEWT:1072569","NEWT:1072568","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1336794","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3710","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:284811","NEWT:2902907","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:10882","NEWT:1431297","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3707","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:319224","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:223074","NEWT:2709072","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:28196","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:387344","NEWT:657318","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:422203","NEWT:460523","NEWT:2422","NEWT:2423","NEWT:3755","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:123606","NEWT:1195466","NEWT:85698","NEWT:291146","NEWT:29466","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:34839","NEWT:476","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NEWT:106299","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:64697","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:1120755","NEWT:1862567","NEWT:591090","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:546","NEWT:1431340","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:52694","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:366497","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:771875","NEWT:377142","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:51315","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055","NEWT:13037","NEWT:518","NEWT:519","NEWT:941638","NEWT:511","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:529120","NEWT:7375","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NE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