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Qian"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Cortical injury","Plasma","Csf","Lc-ms/ms","Rhesus macaque","Brain tissue","Mesenchymal stromal cell-derived extracellular vesicles"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD059286"],"tissue":["Brain","Blood Plasma","Cerebrospinal Fluid"],"sample_protocol":["During the study, aged female rhesus monkeys (Macaca mulatta, 16-26 years, equivalent to approximately 48-78-year-old humans) were individually housed within visual and auditory range of other monkeys in the colony room. Enrichment procedures used either met or exceeded USDA requirements. Aged monkeys were fed once a day, immediately following testing, and water was available continuously. Diet consisted of a commercial monkey chow that was supplemented with fruits and vegetables. Before entering the study, monkeys were assessed for pre-existing abnormalities in overall health. Monkeys were trained on a fine motor task then randomly assigned to a vehicle control or MSC-EVs treatment before receiving a cortical injury targeted to the hand representation of the primary motor cortex. CSF and plasma samples were collected as baseline samples (T1). Then, cortical injury was induced in each monkey and then they received intravenous vehicle control (PBS) or MSC-EVs treatment (4 × 10^8 particles/g) 24 hours after injury and again at 14 days after surgery. CSF and plasma sample were collected at 24 hours after injury (T2 - prior to treatment or vehicle infusion), 14 days after injury (T3, prior to second treatment or vehicle infusion), and then 6 weeks after surgery (T4). A final blood and CSF sample was collected (T5) immediately prior to euthanasia. All staff were blinded to the treatment groups for all procedures and experiments.  Brain tissue, CSF, plasma and MSC-EVs samples were employed a surfactant cocktail-aided extraction/precipitation/on-pellet digestion (SEPOD) procedure, which achieves highly efficient and reproducible recovery of proteins and peptides from various types of biological samples. Briefly, monkey snap-frozen tissue samples were ground into powder and resuspended in a detergent-cocktail buffer (50 mM Tris-formic acid, 150 mM NaCl, 0.5% sodium deoxycholate, 2% SDS, 2% NP-40, pH8.0) with cOmplete protease inhibitor cocktail tablet (Roche Applied Science, Indianapolis, IN) and a PhosSTOP phosphatase inhibitor cocktail tablet (Roche Applied Science, Indianapolis, IN). The lysate was incubated on ice for 30 min with vortexing every 10 min, and then homogenized ∼10 times with a Polytron homogenizer (Kinematica AG, Switzerland) for 5−10 s at 15,000 rpm with 20 s cooling cycles. The mixture was then sonicated with a probe sonicator (3 cycles of 20 s each) to achieve extensive lysis. For monkey plasma samples, High Select(TM) depletion spin columns were used to deplete most of high-abundance serum proteins for improved detection of low-abundance proteins using LC-MS/MS system. Detergent-cocktail buffer was also added in CSF, depleted plasma, and MSC-EVs samples for protein extraction. Then, all samples were centrifuged at 20,000g for 30 min at 4 °C. The supernatant was collected, protein concentration was quantified by BCA protein assay (Pierce Biotechnology, Inc., Rockford, IL) to determine the protein yield, and then stored at −80 °C until analysis. After reduction/alkylation, the detergents, lipids, fatty acids, salts, and other matrix elements were removed efficiently with organic solvent-mediated precipitation. The protein pellets were then digested robustly and reproducibly as described previously, thereby ensuring reliable quantification of the samples obtained from the experiment. The LC-MS system consists of a Dionex UltiMate 3000 nano-LC system, a Dionex UltiMate 3000 micro LC system with a WPS-3000 autosampler, and an Orbitrap Fusion Lumos mass spectrometer (ThermoFisher Scientific, San Jose, CA, USA). A large-inner diameter (i.d.) trapping column (300-m i.d. 5 mm; Agilent Technologies, Santa Clara, CA, USA) setting was implemented before the analytical column (75-m i.d. 65 cm, packed with 2.5-m XSelect CSH C18 material) for high-capacity sample loading, cleanup and delivery. For each sample, a peptide equivalent to 4g protein was injected for LC-MS analysis. Mobile phases A and B were 0.1% FA in 2% acetonitrile (ACN) and 0.1% FA in 88% ACN. The 180-min LC gradient profile for peptide separation was: 4% B for 3 min, 4–11% B for 5 min, 11–32% B for 117 min, 32–50% B for 10 min, 50–97% B for 1 min, 97% B for 17 min, and then equilibrated to 4% for 27 min. The mass spectrometer was operated under data-dependent acquisition (DDA) mode with a maximal duty cycle of 3 seconds. MS1 spectra were acquired by Orbitrap (OT) under 240k resolution (120k for MSC-EVs samples) for ions in the m/z range of 400-1500. Automatic Gain Control (AGC) target and maximal injection time were set to 175% and 50 ms, and dynamic exclusion was set as 60 s, 10 ppm. Precursor ions were isolated by quadrupole using an m/z window of 1.6 Th and were fragmented by high-energy collisional dissociation (HCD) at 30% energy. MS2 spectra were acquired by OT under 15k resolution with an AGC target of 100% and a maximal injection time of 50 ms. Detailed LC-MS settings and information can be found in our previous publications."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["An in-house developed UHR-IonStar data processing pipeline was adopted for proteomic quantification of monkey tissue, CSF, and plasma samples. Database searching was conducted by matching the LC-MS/MS raw files against the Rhesus Macaque protein sequence database (365 reviewed & 83632 unreviewed entries, March 2024) using the MS-GF+ search engine (v20210108, released in January 2021). The search parameters were set to 20-ppm tolerance for precursor ion mass and 0.02 Da for fragmented ion mass. A max of two missed cleavages were permitted for fully tryptic peptides. Carbamidomethylation of cysteine was set as a static modification, and a dynamic modification was defined as oxidation at methionine and acetylation at the N-terminal. The false discovery rates (FDRs) of identification were estimated using a target−decoy search strategy that was dependent on a concatenated database of forward and reversed sequences. Peptide spectrum match (PSM) filtering, protein inference and grouping, and global FDR control were accomplished by IDPicker (v3.1.18192.0). Protein and peptide FDR were controlled at 1%, and a minimum of 2 unique peptides per protein was set. Proteins with no unique peptides were grouped with a maximal number of 50 proteins per group. The filtered PSM list was generated by the UHR-IonStar APP (https://github.com/JunQu-Lab/UHRIonStarApp) using lists of proteins/peptides/spectra exported from IDPicker.  Protein quantification information was obtained by software SIEVE (v2.2, ThermoFisher Scientific). It performed chromatographic alignment using ChromaAlign algorithm for inter-run retention time correction, following quantitative frame generation based on direct ion current extraction (DICE) strategy with a m/z-RT extraction window. In order to take full advantage of the 240K-resolution MS1 measurement, the defined m/z-RT extraction window was optimized via a narrow m/z window width (i.e., ±5 ppm m/z) coupled with a retention time width (i.e., 1.0 min). One sample run in the middle of the batch is typically selected for the reference of peak alignment. Each set of extracted ion chromatograms with corresponding area under the curve (AUC) in all files is termed as one “frame”. The integration of the frames from SIEVE and the filtered PSM list were merged by a unique identifier combining file name and MS2 scan number. Frames with valid peptide sequences were then subjected to frame-level quality control, total-ion-current (TIC) normalization, peptide level outlier detection/exclusion, and aggregation to the protein level in UHR-IonStar APP. More detailed information about the UHR-IonStar data processing pipeline can be found in our previous publications31, 32, 40. For MSC-EVs sample, LC-MS/MS raw file was searched against the same monkey protein sequence database using SEQUEST-HT search engine in Proteome Discoverer (v1.4, Thermo Scientific) with the same searching parameters. Scaffold (v4.3.2) was used for quality control of identification and quantification information."],"omics_type":["Proteomics"],"labhead":["Jun Qu"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Pharmaceutical Sciences, University at Buffalo, Buffalo, NY, USA"],"species":["Macaca Mulatta (rhesus Macaque)"],"publication":["41032466 Qian S, McCann RP, Shen S, Zhu X, Tsillas CM, Xin H, Wang M, Zhang Y, Zhang ZG, Chopp M, Medalla M, Moore TL, Qu J. Multicompartment Quantitative Proteomics Revealing Potential Mechanisms Underlying the Treatment Effects of Mesenchymal-Derived Extracellular Vesicles in a Monkey Model of Cortical Injury. J Proteome Res. 2025 24(11):5664-5682 10.1021/acs.jproteome.5c00521"],"submitter_mail":["sqian@buffalo.edu"],"submitter_affiliation":["Department of Cell Stress Biology, Roswell Park Comprehensive Cancer Center"],"submitter_country":["United States"],"pubmed_abstract":["Previous studies have demonstrated that mesenchymal stromal cell-derived extracellular vesicles (MSC-EVs) enhance functional recovery after cortical injury in rhesus monkeys by reducing chronic microglial inflammation, neuronal damage, and myelination deficits. However, the signaling pathways underlying these therapeutic effects remain largely unexplored. In this study, employing a reliable quantitative proteomics platform UHR-IonStar, we identified the protein cargo of MSC-EVs infused intravenously to rhesus monkeys 24 h and 2 weeks post-injury to the motor cortex. We then analyzed global protein expression changes across cerebrospinal fluid (CSF), plasma, and brain tissue of MSC-EV-treated versus vehicle-treated female, aged rhesus monkeys. A total of 1241/431/4124 monkey proteins were reliably quantified in CSF/plasma/tissue samples, respectively. Longitudinal analysis of CSF and plasma samples highlighted a shift from MSC-EV modulation of inflammatory and metabolic proteins in plasma at early recovery (2 weeks), toward modulation of plasticity-related proteins in CSF and brain tissue at later stages (4 weeks). Further protein-protein interaction analysis identified potential MSC-EV targets related to complementary signaling, proteolysis, and aminoglycan stability, which aligned with our previous findings. This comprehensive, multicompartment monkey proteomics study advances understanding of MSC-EV contents and treatment effects, paving the way for novel treatment of cortical injury."],"pubmed_title":["Multicompartment Quantitative Proteomics Revealing Potential Mechanisms Underlying the Treatment Effects of Mesenchymal-Derived Extracellular Vesicles in a Monkey Model of Cortical Injury."],"pubmed_authors":["Qian Shuo S, McCann Ryan P RP, Shen Shichen S, Zhu Xiaoyu X, Tsillas Christina M CM, Xin Hongqi H, Wang Mingjin M, Zhang Yi Y, Zhang Zheng Gang ZG, Chopp Michael M, Medalla Maria M, Moore Tara L TL, Qu Jun J"],"additional_accession":[]},"is_claimable":false,"name":"Multi-compartment quantitative proteomics revealing potential mechanisms underlying the treatment effects of mesenchymal-derived extracellular vesicles in a monkey model of cortical injury","description":"Cortical injury frequently causes motor dysfunction, significantly impairing activities of daily living, and currently, there are no effective therapeutic options available. Previous studies demonstrated that intravenous infusion of mesenchymal stromal cell-derived extracellular vesicles (MSC-EVs) exerts beneficial effects following cortical injury in primary motor cortex via reducing injury-induced microglial neuroinflammation, neuronal excitotoxicity, synapse loss, oligodendrocyte damage and myelination deficits in the rhesus monkey. However, the specific molecules within MSC-EVs responsible for these therapeutic effects and the underlying molecular mechanisms remain largely unexplored. In this study, employing quantitative proteomics strategy, we first identified the protein composition of MSC-EVs, then analyzed the global protein expression changes associated with cortical injury and treatment effect in brain tissue, cerebrospinal fluid (CSF), and plasma samples from monkeys following cortical injury. A total of 4124/1241/431 monkey proteins were reliably quantified in tissue/CSF/plasma samples, respectively. Further informatics analysis revealed not only the enriched biological processes aligned with previous findings, but also several potential treatment markers. This first-time comprehensive investigation of quantitative proteomics in multi-compartment samples from rhesus monkey enhanced our understanding of the treatment effects of MSC-EVs, paving the way for novel treatment and biomarker discovery.","dates":{"publication":"2026-06-15","submission":"2024-12-29"},"accession":"PXD059286","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:3715","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257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