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CVS were collected from pregnancies that were normotensive (n=6), preterm preeclamptic (preeclampsia onset <37 weeks gestation, n=4) or term preeclamptic (preeclampsia onset >37 weeks gestation, n=4). Protein was isolated from CVS using TRIZOL as previously described1 before being prepared for mass spectrometry. Briefly, SP3 protocol was carried with 10μg of extracted protein samples in a total volume of 50μL Triethyl ammonium bicarbonate buffer (TEAB) followed by reduction with 10 mM TCEP for 45 minutes at 37°C and alkylation with 55mM Iodoacetamide for 45 minutes at 37°C in dark. Magnetic beads were prepared by combining 20μL of both Sera-Mag Speed Beads  and washed two times with 200μL ddH2O and were re-suspend in 40μL ddH2O for a final working concentration of 50μg/μL. 2μL of pre-washed magnetic beads as well as 50μL 100% ethanol were added to each sample. Protein binding to the beads was facilitated in at 24°C for 5 min at 1,000 r.p.m. After the binding is complete, tubes were placed in a magnetic rack and were incubated until the beads have migrated to the tube wall. The supernatant was removed and beads were washed thrice with 180μL of 80% ethanol. Beads were resuspended in 100μL of 100 mM TEAB and sonicated for 5 minutes in a water bath. The samples were then kept for overnight digestion at 37°C and 1000 rpm in a table-top thermomixer after adding sequencing-grade trypsin in an enzyme:protein ratio of 1:10. Upon digestion, peptides were recovered by collecting the supernatant. These peptides were lyophilized and stored until mass spectrometry analysis . LC-MS/MS analysis for CVS: Samples were reconstituted in 30 μL 2% acetonitrile:0.1% trifluoroacetic acid and were analysed on a LTQ Orbitrap Elite (Thermo Scientific) coupled to an Ultimate 3000 RSLC nanosystem (Dionex). The nanoLC system was equipped with an Acclaim Pepmap nano-trap column and an Acclaim Pepmap analytical column. 6 μl of the peptide mix was loaded onto the trap column at 3% CH3CN containing 0.1% formic acid for 5 min before the enrichment column is switched in-line with the analytical column. The LC gradient used was 3% B to 20% B for 95 min, 20% B to 40% B in 10 min, 40% B to 80% B in 5 min and maintained at 80% B for the final 5 min before equilibration for 10 min at 3% B prior to the next analysis. The LTQ Orbitrap Elite mass spectrometer was operated in the data-dependent mode, spectra acquired first in positive mode at 240k resolution followed by collision induced dissociation (CID) fragmentation. Twenty of the most intense peptide ions with charge states ≥2 were isolated and fragmented using normalized collision energy of 35 and activation Q of 0.25 (CID).  Cytotrophoblast progenitor cells (hCTP) were derived from human blastomeres of donated cleavage-staged embryos. Briefly, the diluted proteins were sonicated for 5 min to before being centrifuged for 8 min at 13,000xg. The cell pellet was resuspended in reductant TCEP before incubation at 37°C for 45 minutes. Peptides were alkylated by the addition of iodoacetamide and incubated in the dark at room temperature for 45 min before phosphoric acid was added to the samples and vortexed briefly. Samples were diluted in binding buffer before proteins were trapped using S-Trap micro columns and digested in sequencing-grade trypsin in an enzyme:protein ratio of 1:20 before peptides were recovered in 50mM TEAB, lypophilized and stored until mass spectrometry analysis performed as described above. LC-MS/MS analysis for MLPH: Samples were reconstituted in 30 μL of 2% acetonitrile/0.1% trifluoroacetic acid. The analysis was performed on an Orbitrap Ascend mass spectrometer (coupled with a nano-flow reversed-phase HPLC system (Ultimate 3000 RSLC, Dionex) equipped with an Acclaim PepMap nano-trap column (C18, 100 Å, 75 μm × 2 cm) and an Acclaim PepMap RSLC analytical column (C18, 100 Å, 75 μm × 50 cm). The mass spectrometer operated in positive ion mode. Full-scan MS spectra were acquired from m/z 375 to 1500 with a resolution of 120K and an automatic gain control (AGC) target of 400,000, with a maximum injection time of 50 ms. Peptide ions with charge states ranging from 2 to 7 were selected for fragmentation using higher-energy collisional dissociation (HCD) with a normalized collision energy of 30. MS2 spectra were acquired at a resolution of 15K, with an AGC target of 50,000 and a maximum injection time of 22 ms. The isolation window was set to 1.6 m/z."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["For CVS samples Raw data files were searched against the Human protein reference proteomes (UniProt Proteome ID: UP000005640) using MaxQuant-Andromeda (version 1.6.7.0). The false discovery rate (FDR) was set at 0.01 for both peptides and proteins. Search parameters were set as follows: variable modifications: Oxidation (M), Acetyl (Protein N-term); fixed modifications: cysteine carbamidomethylation. The analysis of the samples was based on the label-free quantification (LFQ) intensities. Initial analyses and visualization of proteomics data was performed using LFQ-Analyst (22). The data was statistically evaluated using Perseus software (version 1.6.7.0). The protein data was filtered categorically by row for reverse identifications (false positives), contaminants, and proteins “only identified by site”. The fold changes in the protein levels were evaluated by comparing the mean LFQ intensities amid all experimental groups. A protein was considered to be differentially expressed if the difference was statistically significant (p < 0.05), the fold change >1.2 and <0.83 was identified with a minimum of 2 peptides.  Raw LC-MS/MS data files were processed and analyzed using MaxQuant-Andromeda v2.6.2.0). The data were searched against the Human protein reference proteome database (UniProt Proteome ID: UP000005640, Swiss-Prot, Reviewed). Search parameters included variable modifications such as oxidation (M) and acetylation (Protein N-term), while cysteine carbamidomethylation was set as a fixed modification. Trypsin were specified as the proteolytic enzymes, allowing for a maximum of two missed cleavages. The false discovery rate (FDR) was set at 0.01 for both peptides and proteins. For quantification, label-free quantification (LFQ) intensities were used, with the \"match between runs\" option enabled to maximize protein identification across runs. Statistical evaluation of the proteomic data was carried out using Perseus software (2.0.11). Reverse identifications, contaminants, and proteins identified \"only by site\" were excluded from the analysis. Proteins were considered differentially expressed if their LFQ intensity fold change was greater than 1.2 or less than 0.83, with statistical significance set at p < 0.05. Proteins with at least two peptides were considered for differential expression analysis. (Please add the section for R analysis that you have done)."],"omics_type":["Proteomics"],"labhead":["Eva Dimitriadis"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Royal Women's Hospital"],"species":["Homo Sapiens (human)"],"publication":["42253923 Menkhorst E, Yang G, Yu Y, Santos LL, Zhou W, Syngelaki A, Varshney S, Williamson NA, Koga K, Rolnik DL, da Silva Costa F, Nicolaides K, Lê Cao KA, Dimitriadis E. Multi-Omics Reveals Early Pregnancy Placental Dysfunction Associated With Preterm and Term Preeclampsia. MedComm (2020). 2026 7(6):e70784 10.1002/mco2.70784"],"submitter_mail":["yimiaoy1@student.unimelb.edu.au"],"submitter_affiliation":["Royal Women's Hospital"],"submitter_country":["China"],"pubmed_abstract":["Preeclampsia, a severe pregnancy-induced disorder unique to humans, affects ∼2%-8% of pregnancies globally. Strong evidence supports placental dysfunction as central to preeclampsia; however, there is inadequate understanding of the precise pathogenesis of preeclampsia. In this study, we present a comprehensive multi-omics analysis of early pregnancy placental biopsies (chorionic villus samples) from pregnancies that later developed preterm/term preeclampsia, compared to normotensive controls. Using an integrative multivariate approach, we uncovered distinct molecular signatures associated with preeclampsia. Preterm preeclampsia was strongly associated with dysregulated lipoprotein metabolism, while term preeclampsia exhibited alterations in inflammatory pathways, Notch/Kit signaling, and ribosome assembly. These results challenge the prevailing notion that term preeclampsia is unrelated to early placental pregnancy dysfunction. To validate our findings, we focused on melanophilin, a gene downregulated in the early pregnancy placenta of term preeclampsia. Melanophilin expression was reduced during cytotrophoblast syncytialization; however, excessive loss disrupted syncytiotrophoblast function, triggering the production of factors known to drive preeclampsia. Our study provides critical insights into the early pregnancy aberrations underlying preterm and term preeclampsia, paving the way for the development of predictive biomarkers and targeted preventative treatments. This work represents a significant step toward unraveling the complex etiology of preeclampsia and improving maternal and perinatal health outcomes."],"pubmed_title":["Multi-Omics Reveals Early Pregnancy Placental Dysfunction Associated With Preterm and Term Preeclampsia."],"pubmed_authors":["Menkhorst Ellen E, Yang Guannan G, Yu Yimiao Y, Santos Leilani L LL, Zhou Wei W, Syngelaki Argyro A, Varshney Swati S, Williamson Nicholas A NA, Koga Kaori K, Rolnik Daniel Lorber DL, da Silva Costa Fabricio F, Nicolaides Kypros K, Lê Cao Kim-Anh KA, Dimitriadis Evdokia E"],"additional_accession":[]},"is_claimable":false,"name":"Multiomics reveals placental defect underlying preeclampsia","description":"Preeclampsia is a serious pregnancy-induced disorder unique to humans affecting 4.6% of pregnancies worldwide. Advances in the detection, prevention and treatment of preeclampsia have been poor due to our inadequate understanding of its pathogenesis. Here, we perform a multiomics study on early pregnancy placental biopsies (chorionic villus samples) from pregnancies that developed preterm and term preeclampsia compared to normotensive controls. Using an integrative statistical approach we discovered preterm preeclampsia was highly associated with lipoprotein metabolism whereas term preeclampsia was associated with inflammatory pathways and notch signaling. Melanophilin was identified as significantly reduced in early pregnancy placenta from term preeclampsia. Loss of melanophilin was required for syncytialization but excess loss disrupts syncytiotrophoblast function driving the production of antiangiogenic factors known to drive preeclampsia. Our study challenges the dogma that term preeclampsia is not associated with early placental pregnancy dysfunction and provides critical insight into the early pregnancy dysfunction underlying preeclampsia, opening up new avenues for predictive biomarker and preventative treatment discovery.","dates":{"publication":"2026-06-10","submission":"2025-01-21"},"accession":"PXD059993","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:592321","NEWT:1073882","NEWT:6819","NEWT:475174","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","NEWT:1748418","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:3357","NEWT:7719","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","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:2502409","NEWT:212790","NEWT:110368","NEWT:1916073","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:329854","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:1538","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:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","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:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","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:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","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:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","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:299467","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:10804","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","N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