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Samples were processed with a modified SP3 method (PMID: 25358341). Proteins (40 µg) were reduced in 10mM dithiothreitol at 56°C for 30min and alkylated in 20mM iodoacetamide at room temperature for 30min. Washed hydrophobic and hydrophilic Sera-Mag™ SpeedBeads (Carboxylate-Modified, Cytiva) were added to the samples with a bead to protein ratio of 10:1. Proteins were precipitated on beads by ethanol (final concentration 70%), washed three times with 80% ethanol and dried at room temperature. Beads were resuspended in 50 mM TEAB and proteins were digested overnight (enzyme:protein ratio of 1:25, Trypsin/LysC, Promega) followed by a two hours digestion (ratio 1:50, Trypsin, Thermo Scientific). Peptide samples were labelled using TMTpro 18-plex isobaric mass tagging reagents (Thermo Scientific). The labelled samples were pooled into one TMT-set and purified using HiPPR Detergent Removal Resin and Pierce peptide desalting spin columns (both Thermo Scientific), according to the manufacturer´s instructions. The TMT-set was fractionated by basic reversed-phase chromatography on a Dionex Ultimate 3000 UPLC system (Thermo Fisher Scientific). Peptide separations were performed using a reversed-phase XBridge BEH C18 column (3.5 μm, 2.1x250 mm, Waters Corporation) and a stepped gradient from 3% to 45% solvent B over 75 min followed by an increase to 80% B for 10 min at a flow of 200 µL/min. Solvent A was 25mM ammonia and solvent B was 84% ACN. 96 primary fractions were combined to 30 final fractions which were evaporated and reconstituted in 3% ACN, 0.1% trifluoroacetic for LC-MS3 analysis.   LC-MS3 analysis The fractions were analysed on an Orbitrap Lumos™ Tribrid mass spectrometer equipped with a FAIMS Pro ion mobility system and interfaced with an Easy-nLC1200 liquid chromatography system (all Thermo Fisher Scientific). Peptides were trapped on an Acclaim Pepmap 100 C18 trap column (100 μm x 2 cm, particle size 5 μm, Thermo Fisher Scientific) and separated on an in-house packed analytical column (40 cm x 75 μm, particle size 3 μm, Reprosil-Pur C18, Dr. Maisch) using a stepped gradient from 4% to 28% acetonitrile in 0.2% formic acid over 77 min at a flow of 300 nL/min. FAIMS Pro was alternating between the compensation voltages (CV) of -50 and -70, and the same data-dependent settings were used at both CVs. The precursor ion mass spectra were acquired at a resolution of 120 000 and an m/z range of 375-1500. Using a cycle time of 1.5 seconds the most abundant precursors with charges 2–7 were isolated with an m/z window of 0.7 and fragmented by collision induced dissociation (CID) at 30%. Fragment spectra were recorded in the ion trap at Rapid scan rate. Dynamic exclusion was set to 45 sec. The ten most abundant MS2 fragment ions were isolated using multi-notch isolation for further MS3 fragmentation. MS3 fragmentation was performed using higher-energy collision dissociation (HCD) at 55% and the MS3 spectra were recorded in the Orbitrap at a resolution of 50 000 and an m/z range of 100–500."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Proteomic data analysis  Raw files were processed with Proteome Discoverer (ver 2.4, Thermo Fisher Scientific) and matched against SwissProt Human (20.422entries, April 2023) using Sequest as a search engine with a precursor tolerance of 5 ppm and a fragment ion tolerance of 0.6 Da. Tryptic peptides were accepted with 1 missed cleavage. Methionine oxidation was set as a variable modifications, cysteine carbamidomethylation, TMTpro on lysine and peptide N-termini were set as fixed modifications. Percolator was used for PSM validation with a strict FDR threshold of 1%. For quantification TMT reporter ions were identified in the MS3 HCD spectra with 3 mmu mass tolerance and the TMT reporter intensity values for each sample were normalized on the total peptide amount. The SPS threshold was set to 65%, a Sequest HT threshold score of 1.2 was chosen. Only unique peptides were used for relative quantification and proteins were required to pass a protein FDR of 1%."],"omics_type":["Proteomics"],"labhead":["Jan Lötvall"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Krefting Research Centre, Institute of Medicine, Sahlgrenska Academy, University of Gothenburg, Sweden"],"species":["Homo Sapiens (human)"],"submitter_mail":["johannes.fuchs@gu.se"],"publication":["41983054 Park KS, Ha DH, Lee JH, Ordouzadeh N, Bergqvist M, Lee HJ, Shin E, Cho BS, Lötvall J. Quantitative proteomic and functional comparison of extracellular vesicles from multiple adipose tissue mesenchymal stem cell donors. Extracell Vesicles Circ Nucl Acids. 2026 7(1):425-440 10.20517/evcna.2025.173"],"submitter_affiliation":["Gothenburg University"],"submitter_country":["Sweden"],"pubmed_abstract":["<b>Aim:</b> Extracellular vesicles (EVs) released by mesenchymal stem cells (MSCs), known as MSC-EVs, have gained attention as potential treatments owing to their immunomodulatory functions. Despite growing clinical interest, donor-to-donor inconsistencies remain key challenges for standardizing MSC-EV production under good manufacturing practice (GMP) conditions. This work aimed to systematically compare the molecular and functional consistency of EVs derived from three independent human adipose tissue-MSC donors. <b>Methods:</b> GMP-grade EVs were initially isolated using tangential flow filtration on a large scale and then characterized by multiple biophysical analyses. To characterize the protein composition of EVs across batches, quantitative proteomic analysis was performed using tandem mass tags and mass spectrometry. For functional validation, an <i>in vitro</i> macrophage inflammation assay was conducted by treating natural lipopolysaccharide-stimulated cells with EVs, and cytokine levels were measured using enzyme-linked immunosorbent assays (ELISA). <b>Results:</b> Quantitative proteomic profiling identified 2,615 proteins, of which 84%-94% were not significantly changed across batches, highlighting a robust core proteome. Notably, 361 membrane-associated proteins were consistently conserved, including transporters, adhesion molecules, and signaling receptors, implicating these components in EV-mediated intercellular communication and immunomodulation. Functional analysis using an <i>in vitro</i> macrophage inflammation model demonstrated that all EV batches reproducibly suppressed pro-inflammatory cytokine production in a dose-dependent manner, with no significant inter-batch differences. <b>Conclusion:</b> Collectively, these findings indicate that MSC-EVs maintain both molecular and functional stability across different donors, and that a conserved proteomic signature underlies their reproducible anti-inflammatory activity. This study provides a foundation for establishing standardized quality criteria and advancing MSC-EVs toward clinical therapeutic applications."],"pubmed_title":["Quantitative proteomic and functional comparison of extracellular vesicles from multiple adipose tissue mesenchymal stem cell donors."],"pubmed_authors":["Park Kyong-Su KS, Ha Dae Hyun DH, Lee Jun Ho JH, Ordouzadeh Negar N, Bergqvist Markus M, Lee Hyun Ju HJ, Shin Ella E, Cho Byong Seung BS, Lötvall Jan J"],"additional_accession":[]},"is_claimable":false,"name":"Quantitative Proteomic and Functional Comparison of Extracellular Vesicles from Three GMP-Grade MSC Donors – Role of Membrane Proteins","description":"Mesenchymal stem cell-derived extracellular vesicles (MSC-EVs) have emerged as promising therapeutic agents due to their anti-inflammatory and regenerative properties. Despite growing clinical interest, donor-to-donor inconsistencies remain key challenges for standardizing MSC-EV production under Good Manufacturing Practice (GMP) conditions. In this study, we aimed to systematically evaluate the molecular and functional consistency of EVs derived from three independent human adipose tissue-MSC donors. GMP-grade EVs were initially isolated using tangential flow filtration on a large scale and then characterized by multiple biophysical analyses. Quantitative proteomic profiling identified 2,615 proteins, of which 84-94% were not significantly changed across batches, highlighting a robust core proteome. Notably, 361 membrane-associated proteins were consistently conserved, including transporters, adhesion molecules, and signaling receptors, implicating these components in EV-mediated intercellular communication and immunomodulation. Functional analysis using an in vitro macrophage inflammation model demonstrated that all EV batches reproducibly suppressed pro-inflammatory cytokine production in a dose-dependent manner, with no significant inter-batch differences. Collectively, these findings indicate that MSC-EVs maintain both molecular and functional stability across different donors, and that a conserved proteomic signature underlies their reproducible anti-inflammatory activity. This study provides a foundation for establishing standardized quality criteria and advancing MSC-EVs toward clinical therapeutic applications.","dates":{"publication":"2026-04-27","submission":"2025-12-10"},"accession":"PXD071815","cross_references":{"TAXONOMY":["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: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: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:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:160620","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:1072569","NEWT:1072568","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","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:550537","NEWT:284812","NEWT:284811","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:1431297","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","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: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:2423","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:85698","NEWT:291146","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:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","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:63367","NEWT:29488","NEWT:215402","NEWT:3726","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:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","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: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:519","NEWT:941638","NEWT:511","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:529120","NEWT:7375","NEWT:300641","NEWT:39655","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:37003","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:280406","NEWT:83906","NEWT:99488","NEWT:99487","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:9938","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:2029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