{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/Bruschi_podociti_A_4_06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/Bruschi_podociti_B_2_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/Bruschi_podociti_C_3_13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/Bruschi_podociti_A_2_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/Bruschi_podociti_C_1_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/Bruschi_podociti_B_3_09.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/Bruschi_podociti_C_4_14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/Bruschi_podociti_B_1_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/Bruschi_podociti_A_1_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/Bruschi_podociti_B_4_10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/Bruschi_podociti_A_3_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/Bruschi_podociti_C_2_12.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/20240715_091753_Bruschi_podociti.sne","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070406/Podociti.zip"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["andreapetretto@gaslini.org"],"submitter":["Nicole Grinovero"],"technology_type":["Mass Spectrometry","Data-independent acquisition","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Podocyte injury","Immunoglobulin m glycosylation","Hyposialylation","Podocytopathies","Sialidase"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070406"],"tissue":["Podocyte"],"sample_protocol":["Podocyte cells were lysed, reduced and alkylated in 50 ul LYSE buffer (Preomics) at 95°C for 10 min and sonicated with an Ultrasonic Processor  UP200St (Hielscher), 3 cycles of 30 sec.  Proteins were isolated and digested by PAC method automated on a KingFisher™ Apex robot (Thermo Fisher Scientific) in 96-well format as described in [ref ]. Briefly, the tip plate was stored in plate #1. Lysate samples were stored in plate #2, in a final concentration of 70% acetonitrile and with magnetic beads in a protein/bead ratio of 1:4 (1:1 SpeedBead Magnetic Carboxylate, 45152105050250 and 65152105050250). Washing solutions were in plates #3–5 (acetonitrile), plate #6 (70% Ethanol) and plate #7 (isopropanol). Plate #8 contained 100 ul digestion solution of 25 mM Tris HCl pH 8, LysC (Wako) in an enzyme/protein ratio of 1:100 (w/w) and trypsin (Promega) in an enzyme:protein ratio of 1:50. The protein aggregation was carried out in two steps of 1 min mixing at medium mixing speed, followed by a 10 min pause each. The sequential washes were performed in 2.5 min and slow speed, without releasing the beads from the magnet. The digestion was set to 4 h at 37 degrees with slow speed. The resulting peptides were analyzed by a nano-UHPLC-MS/MS system using an Ultimate 3000 RSLC coupled to an Orbitrap Q Exactive Plus mass spectrometer (Thermo Scientific Instrument). Elution was performed with an EASY spray column (75 μm × 50 cm, 2 μm particle size, Thermo Scientific) at a flow rate of 250 nL/min using a linear gradient of 2-45% solution B (80% acetonitrile –CAN-, 5% dimethylsulfoxide -DMSO-, 0.1% formic acid -FA- in H2O) in 50 min. Orbitrap detection was used for MS1 measurements at a resolving power of 70 K in a range between 375 and 1500 m/z with a 3∙106 automatic gain control (AGC) target and 50 ms maximum injection time (IT). Precursors were selected for data-independent fragmentation with an isolation window width of 34 m/z and 19 loop count. Higher collisional dissociation (HCD) energy was set to 27%, and MS2 scans were acquired at a resolution of 35 k, 3∙106 AGC target, and 50 ms maximum IT."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["All DIA raw files were processed with Spectronaut version 18 using a library-free approach (directDIA) under default settings. The library was generated against the Uniprot Human database (release UP000005640_9606 June 2024, 104602 Entries). Carbamidomethylation was selected as a fixed modification, while methionine oxidation and N-terminal acetylation were selected as variable modifications. False discovery rate (FDR) of peptide-spectrum match (PSM) and peptide/protein groups were set to 0.01. For quantification, Precursor Filtering was set to Identified (Qvalue) and MS2 was chosen as quantity MS-level.  After log2 conversion, a normal distribution was used to impute missing values, and the entire dataset was normalized using the quantile method. The normalized dataset was analyzed using unsupervised hierarchical clustering, including principal component analysis and k-means clustering, to identify outliers and dissimilarities among samples. ANOVA test for unpaired samples was used to identify statistically significant proteins between podocyte cells treated with iNS IgM-derived (iNS), CTR IgM-derived, without modification (CTR) or desialylated (Desialylated). Then, to identify the proteins that maximized discrimination between iNS and CTR, or Desialylated and CTR, or Desialylated and iNS, we used t-test analysis. For both analyses, proteins were considered statistically significantly expressed for power values of 80% and adjusted p-values ≤ 0.05 after correction for multiple interactions (Benjamini-Hochberg method). Volcano plots were used to visualize the results of the t-test analysis, with the threshold line determined by the function y = |c/(x − x0)|. Gene ontology analysis was performed to identify the enriched pathways through the active subnetworks using the PathFindR package. Kinase enrichment analysis (KEA) was also performed using the statistically significant proteins as substrates to predict kinases potentially involved in regulating the phosphorylation signal in each comparison. The Coral App was used to visualize the kinome tree of proteome profile. For the lectin ELISA, lipid peroxidation, and ATP synthesis differences across all clinical groups were determined using the Kruskal-Wallis test with Dunn's correction. Pearson’s correlation coefficients were calculated to assess the relationships between UPCR, SNA reactivity, and serum NEU1 and NEU3 levels. Paired samples collected at <0.2 and >3.5 gr/day proteinuria were compared using the Wilcoxon test. For the kinome assay, differences across all conditions were determined using a t-test with Benjamini-Hochberg correction. All statistical tests were performed using OriginLab Pro version 2022b and R version 4.3.3 software."],"omics_type":["Proteomics"],"labhead":["Andrea Petretto"],"instrument_platform":[""],"labhead_affiliation":["Core Facility for Omics Sciences, IRCCS Istituto Giannina Gaslini, Genoa, Italy"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["42318532 Spinelli S, Gaudiano S, Garbarino A, Lugani F, La Porta E, Petretto A, Bartolucci M, Lavarello C, Grinovero N, Musante I, Scudieri P, Trivelli A, Piaggio G, Magnasco A, Degl'Innocenti ML, Granata S, Zaza G, Verrina E, Candiano G, Bruschi M. IgM Hyposialylation Modulates Podocyte Vulnerability in Patients With Idiopathic Nephrotic Syndrome. Kidney Int Rep. 2026 11(8):106598 10.1016/j.ekir.2026.106598"],"submitter_mail":["nicolegrinovero@gmail.com"],"submitter_affiliation":["IRCCS Istituto Giannina Gaslini"],"submitter_country":["Italy"],"pubmed_abstract":["<h4>Introduction</h4>Altered Ig glycosylation has been implicated in antibody-mediated podocytopathies; however, the functional relevance of IgM sialylation remains poorly defined. Previous evidence suggests that circulating cationic or hyposialylated IgM may contribute to podocyte vulnerability in idiopathic nephrotic syndrome (iNS).<h4>Methods</h4>Serum IgM from 86 pediatric and adult patients with podocytopathies, 20 patients with membranous nephropathy (MN), 20 patients with lupus nephritis (LN), and 30 healthy controls were analyzed by lectin-based enzyme-linked immunosorbent assay (ELISA) using biotinylated lectins to assess terminal N-glycan residues, including Sambucus nigra agglutinin (SNA) and Ricinus communis agglutinin I (RCA-I). Serum levels of the sialyltransferase ST6GAL1 and the sialidases neuraminidase-1 (NEU1) and neuraminidase-3 (NEU3) were quantified. Cultured human podocytes were exposed to native, desialylated, or resialylated IgM and analyzed by confocal microscopy, quantitative proteomics, phosphoproteomics, and metabolic assays.<h4>Results</h4>IgM from patients with iNS showed reduced SNA binding, which inversely correlated with proteinuria and circulating NEU1/NEU3 levels. In paired samples, SNA reactivity decreased during relapse and increased during remission. ST6GAL1 was undetectable across all groups, whereas phospholipase A2 receptor 1(PLA2R1)-positive MN displayed reduced RCA-I binding. Podocytes exposed to hyposialylated or desialylated IgM exhibited disorganization of the actin cytoskeleton, reduced nephrin signal, increased lipid peroxidation, and decreased ATP levels. Resialylated IgM displayed podocyte morphological and metabolic features not statistically distinguishable from those observed under control conditions. Proteomic and phosphoproteomic analyses highlighted modulation of mitogen-activated protein kinase (MAPK)-, mechanistic Target of Rapamycin (mTOR-), adenosine monophosphate-activated protein kinase (AMPK), and cytoskeleton-related pathways.<h4>Conclusion</h4>IgM sialylation status tracks disease activity and modulates podocyte structural, metabolic, and signaling responses, supporting immune glycan remodeling as a disease-associated modifier of podocyte vulnerability in iNS."],"pubmed_title":["IgM Hyposialylation Modulates Podocyte Vulnerability in Patients With Idiopathic Nephrotic Syndrome."],"pubmed_authors":["Spinelli Sonia S, Gaudiano Sofia S, Garbarino Andrea A, Lugani Francesca F, La Porta Edoardo E, Petretto Andrea A, Bartolucci Martina M, Lavarello Chiara C, Grinovero Nicole N, Musante Ilaria I, Scudieri Paolo P, Trivelli Antonella A, Piaggio Giorgio G, Magnasco Alberto A, Degl'Innocenti Maria Ludovica ML, Granata Simona S, Zaza Gianluigi G, Verrina Enrico E, Candiano Giovanni G, Bruschi Maurizio M"],"additional_accession":[]},"is_claimable":false,"name":"IgM hyposialylation drives podocyte injury in pediatric and young adult patients with podocytopathies","description":"Altered immunoglobulin glycosylation has been implicated in antibody-mediated podocytopathies, yet the functional impact of IgM sialylation remains unclear. Previous evidence suggested that circulating cationic or hyposialylated IgM may contribute to podocyte injury in idiopathic nephrotic syndrome (iNS). Serum IgM from pediatric and young adult patients with podocytopathies, membranous nephropathy (MN), lupus nephritis (LN), and healthy controls were analyzed by lectin-based ELISA using a panel of six biotinylated lectins to detect terminal N-glycan residues. Among these, Sambucus nigra agglutinin (SNA) binds α2,6-linked sialic acid, and Ricinus communis agglutinin I (RCA-I) recognizes β1,4-linked galactose. Serum levels of the α2,6-sialyltransferase ST6GAL1 and the sialidases neuraminidase-1 (NEU1) and neuraminidase-3 (NEU3) were quantified. Cultured human podocytes were exposed to patient-derived, control, or enzymatically modified IgM (desialylated/resialylated) and analyzed by confocal microscopy, quantitative proteomics, phosphoproteomics, and metabolic assays. IgM from patients with podocytopathies showed reduced SNA binding, which inversely correlated with proteinuria (r = −0.69, P < 0.0001) and with serum sialidases NEU1/NEU3 (r = −0.67/−0.59, P < 0.0001). In paired samples, SNA reactivity decreased during relapse and normalized in remission, indicating dynamic modulation with disease activity. ST6GAL1 was undetectable in all groups. In contrast, PLA2R1-positive MN, in which pathogenic antibodies target podocyte PLA2R1, displayed reduced RCA-I binding. Podocytes exposed to hyposialylated or desialylated IgM exhibited actin disorganization, loss of nephrin signal, increased lipid peroxidation, and decreased ATP synthesis. In contrast, resialylated IgM preserved morphology and metabolism comparable to controls. Proteomic and phosphoproteomic profiling revealed enrichment of MAPK, mTOR, AMPK, and cytoskeletal remodeling pathways. IgM hyposialylation, driven by extracellular sialidases up-regulation, correlates with disease activity and promotes oxidative stress, mitochondrial dysfunction, and cytoskeletal remodeling in podocytes, identifying immune glycan remodeling as a modifiable determinant of podocyte injury and a potential biomarker of disease activity.","dates":{"publication":"2026-06-29","submission":"2025-11-06"},"accession":"PXD070406","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: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:55350","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","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:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","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:85692","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:166314","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: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","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491",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