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Hansen"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Wounds And Injuries"],"software":[""],"submitter_keywords":["Muscle injury","Duchenne muscular dystrophy","Dysferlin","Limb girdle muscular dystrophy","Extracellular matrix","Annexin","Macrophage"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077779"],"tissue":["Quadriceps"],"sample_protocol":["Sample preparation for proteomic analysis. Skeletal muscle samples were processed as previously described (McCabe et al., 2023; McCabe et al., 2021). Tissues were snap-frozen in liquid nitrogen, lyophilized overnight using a FreeZone 4.5 L benchtop freeze dryer (Labconco #7750020), and milled to a fine powder prior to extraction.  All following extraction buffers were applied at 200 μL/mg of the starting tissue dry weight. Five milligrams of lyophilized material from each sample was homogenized in decellularization buffer (50mM Tris-HCl (pH 7.4), .25% CHAPS, 25mM EDTA, 3M NaCl) at power 8 for 3 min (Bullet Blender, Model BBX24, Next Advance, Inc.) before being mixing by vortex for 20 min at 4°C (power 7).  Homogenate was centrifuged at 18,000 x g (4°C) for 15 min and the supernatant was collected.  Decellularization was repeated for a total of 3 washes, homogenizing and vortexing samples before each collection, and all washes were pooled to generate the cellular fraction.  The remaining pellets were homogenized in 6 M guanidine hydrochloride (Gnd-HCl), 100 mM ammonium bicarbonate (ABC) at power 8 for 1 min and vortexed (power 5) at room temperature overnight.  Homogenate was spun at 18,000 x g (4°C) for 15 min and the supernatant was collected as the soluble ECM (sECM) fraction. Pellets were then treated with freshly prepared hydroxylamine (HA) buffer (1 M NH2OH−HCl, 4.5 M Gnd−HCl, 0.2 M K2CO3, pH adjusted to 9.0 with NaOH).  Samples were homogenized at power 8 for 1 min and incubated at 45°C with shaking (1000 rpm) for 4 h. Following incubation, the samples were spun for 15 min at 18,000 x g and the supernatant was removed and stored as the insoluble ECM (iECM) fraction.  All collected fractions were immediately frozen and stored at −80°C until further proteolytic digestion.  Fractions were subsequently subjected to enzymatic digestion overnight (16 h) at 37°C with trypsin (1:100 enzyme to protein ratio) using a filter aided sample preparation (FASP) approach as previously described (Wiśniewski et al., 2009) and desalted during Evotip loading.   LC-MS/MS analysis.  Digested peptides were loaded onto individual Evotips following the manufacturer‘s protocol and separated on an Evosep One chromatography system (Evosep, Odense, Denmark) using a Pepsep column, (150 µm inter diameter, 15 cm) packed with ReproSil C18 1.9 µm, 120Å resin.  Samples were analyzed using the instrument default “30 samples per day” LC gradient.  The system was coupled to the timsTOF Pro mass spectrometer (Bruker Daltonics, Bremen, Germany) via the nano-electrospray ion source (Captive Spray, Bruker Daltonics).  The mass spectrometer was operated in PASEF mode.  The ramp time was set to 100 ms and 10 PASEF MS/MS scans per topN acquisition cycle were acquired.  MS and MS/MS spectra were recorded from m/z 100 to 1700.  The ion mobility was scanned from 0.7 to 1.50 Vs/cm2.  Precursors for data-dependent acquisition were isolated within ± 1 Thomson and fragmented with an ion mobility-dependent collision energy, which was linearly increased from 20 to 59 eV in positive mode.  Low-abundance precursor ions with an intensity above a threshold of 500 counts but below a target value of 20000 counts were repeatedly scheduled and otherwise dynamically excluded for 0.4 min."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Global proteomic data analysis.  Data was searched using MSFragger v4.1 via FragPipe v22.0. Precursor tolerance was set to ±15 ppm and fragment tolerance was set to ±25 ppm. Data was searched against UniProt restricted to Mus musculus with added common contaminant sequences (17,268 total sequences). Enzyme cleavage was set to semi-specific trypsin for all samples. Fixed modifications were set as carbamidomethyl (C). Variable modifications were set as oxidation (M), oxidation (P) (hydroxyproline), deamidation (NQ), Gln->pyro-Glu (N-term Q), and acetyl (protein N-terminus). Label free quantification was performed using IonQuant v1.10.27 with match-between-runs enabled and default parameters. Cellular, sECM, and iECM fractions were searched separately and merged after database searching. Results were filtered to 1% FDR at the peptide and protein level. The raw intensity of each protein from each fraction was analyzed using MetaboAnalyst 6.0 (Pang et al., 2024). Differentially expressed proteins defined as FDR < 0.05 and log2FC > 0.5 or < -0.5 were plotted as volcano plots in RStudio using ggplot2."],"omics_type":["Proteomics"],"labhead":["Alexis Demonbreun"],"instrument_platform":[""],"labhead_affiliation":["Center for Genetic Medicine, Northwestern University Feinberg School of Medicine, Chicago, IL, USA Department of Pharmacology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["kirk.hansen@cuanschutz.edu"],"submitter_affiliation":["Univeristy of Colorado"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Excess muscle plasma membrane leak disrupts extracellular matrix content and shifts macrophage-mediated muscle repair","description":"Plasma membrane repair is critical for tissue integrity, especially for elongated contractile muscle cells. Genetically-mediated defects in plasma membrane resealing produce persistent leak, leading to a disordered extracellular matrix.  Loss of the membrane repair protein dysferlin slows sarcolemmal resealing and promotes excess leak.  Annexin A6 is also implicated in sarcolemmal repair, forming repair caps at the site of membrane disruption.  On its own, deletion of the gene for annexin A6, Anxa6, had little effect on muscle health.  In contrast, combined loss of dysferlin and annexin A6 (DysfA6) generated muscle fibers with profoundly defective membrane leak.  Strikingly, Anxa6 deletion in the context of loss of dystrophin (mdxA6) did not exacerbate muscle defects.  The persistent membrane leak in DysfA6 muscle resulted in marked macrophage infiltration with disordered macrophage polarization.  Injured muscle fibers were targets of macrophage efferocytosis.  Loss of Anxa6 was associated with increased expression of annexins A1 and A2, both of which were heavily deposited into the extracellular matrix.  In vitro, macrophages exposed to annexins A1 and A2 expressed increased Csf1, consistent with a model where excess leak results in annexins A1 and A2 in the extracellular matrix, where this protein composition elicits macrophage proliferation and efferocytosis.","dates":{"publication":"2026-06-15","submission":"2026-04-29"},"accession":"PXD077779","cross_references":{"TAXONOMY":["NEWT:3555","NEWT:71647","NEWT:330879","NEWT:260201","NEWT:35554","NCBITaxon:12939","NEWT:32046","NEWT:544496","NEWT:59529","NEWT:2042546","NEWT:32049","NEWT:1392696","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:45351","NEWT:445974","NEWT:43179","NEWT:180454","NEWT:5722","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:10245","NEWT:55153","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:351581","NEWT:43186","NEWT:428146","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:498019","NEWT:1351","NEWT:1438992","NEWT:1352","NEWT:2649997","NEWT:1147161","NEWT:661410","NEWT:638632","NEWT:263737","NEWT:224326","NEWT:1333499","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:5702","NEWT:95648","NEWT:1589","NEWT:135622","NEWT:1349","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:383379","NEWT:1401257","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:44491","NEWT:641809","NEWT:27933","NEWT:556484","NEWT:317447","NEWT:4688","NEWT:7955","NEWT:111225","NEWT:7719","NEWT:7959","NEWT:2261","NEWT:868565","NEWT:94323","NEWT:31156","NEWT:3112","NEWT:79329","NEWT:4442","NEWT:192875","NEWT:1214915","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:284218","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:1316931","NEWT:224308","NEWT:3347","NEWT:511145","NEWT:160621","NEWT:212790","NEWT:931281","NEWT:4432","NEWT:5762","NEWT:5763","NEWT:658457","NEWT:1310161","NEWT:77133","NEWT:295358","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:2246","NEWT:2652724","NEWT:5757","NEWT:68415","NCBITaxon:4563","NEWT:5755","NEWT:44688","NEWT:44689","NEWT:44447","NEWT:752555","NEWT:498211","NEWT:5759","NEWT:347256","NEWT:1736231","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:1392","NEWT:498217","NEWT:498216","NEWT:2242","NEWT:11320","NEWT:286","NEWT:391619","NEWT:246196","NEWT:287","NEWT:246197","NEWT:145458","NEWT:633149","NEWT:1149786","NEWT:10239","NEWT:68895","NEWT:44685","NEWT:161934","NEWT:4897","NEWT:1148","NEWT:5744","NEWT:72901","NEWT:213863","NEWT:5508","NEWT:3329","NEWT:5507","NEWT:410661","NEWT:55571","NEWT:35500","NEWT:1235816","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:4896","NEWT:1287689","NEWT:1390","NEWT:11557","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:294","NEWT:1773","NEWT:1182590","NEWT:3712","NEWT:82380","NEWT:3711","NEWT:935293","NEWT:375146","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:1772","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:263","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:11988","NEWT:284812","NEWT:8175","NEWT:400667","NEWT:43330","NEWT:1603293","NEWT:408169","NEWT:44664","NEWT:47946","NEWT:459758","NEWT:3702","NEWT:1245466","NEWT:243277","NEWT:1246791","NEWT:7067","NEWT:118694","NEWT:586722","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:274","NEWT:7070","NCBITaxon:287","NEWT:408172","NEWT:408170","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1436733","NEWT:460519","NEWT:1247411","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:9483","NEWT:333760","NEWT:34607","NEWT:56636","NEWT:1513458","NEWT:1233681","NCBITaxon:40559","NEWT:506599","NEWT:2853422","NEWT:81077","NEWT:84588","NEWT:1679718","NEWT:480","NEWT:65349","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:300852","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:508771","NEWT:1883446","NEWT:253","NCBITaxon:2759","NEWT:1233435","NEWT:93061","NEWT:93062","NEWT:34613","NCBITaxon:4932","NEWT:109760","NEWT:29031","NEWT:943274","NEWT:644223","NEWT:235443","NEWT:108458","NEWT:5936","NEWT:272623","NEWT:272624","NEWT:320637","NEWT:886559","NEWT:3750","NEWT:55521","NEWT:983964","NEWT:118499","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:1130798","NEWT:55529","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:476272","NEWT:3747","NEWT:195051","NEWT:3988","NEWT:1116234","NEWT:561007","NEWT:1255228","NEWT:649908","NEWT:410289","NEWT:373153","NEWT:3983","NEWT:203696","NEWT:472","NEWT:352472","NEWT:97441","NEWT:1071661","NEWT:1202531","NEWT:1202532","NEWT:360094","NEWT:1408223","NEWT:470","NEWT:1408224","NEWT:41364","NEWT:5911","NEWT:1313","NEWT:1218097","NEWT:1080348","NCBITaxon:50557","NEWT:1314","NEWT:39251","NEWT:39491","NEWT:212142","NCBITaxon:5811","NEWT:29491","NEWT:101841","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:571256","NEWT:40483","NEWT:63366","NEWT:63367","NEWT:688333","NEWT:215402","NCBITaxon:548681","NEWT:318586","NCBITaxon:5820","NEWT:1547","NEWT:272634","NEWT:198107","NEWT:9031","NEWT:27292","NEWT:1872122","NEWT:1308","NEWT:7091","NEWT:1034015","NEWT:760568","NEWT:141262","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:4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