{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD071066/Tears_Gal3_enrich_250808_VC_G3_3_DTT_IAA_postelution.raw.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD071066/Tears_blockedbeads_ctrl_250808_VC_ctrlbeads_3.raw.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD071066/Tears_blockedbeads_ctrl_250808_VC_ctrlbeads_1.raw.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD071066/Tears_Gal3_enrich_250808_VC_G3_1_DTT_IAA_postelution.raw.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD071066/Tears_Gal3_enrich_250808_VC_G3_2_DTT_IAA_postelution.raw.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD071066/Tears_blockedbeads_ctrl_250808_VC_ctrlbeads_2.raw.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD071066/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD071066/250808_VC_G3_2_DTT_IAA_postelution.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD071066/250729_VC_ctrl_tears_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD071066/250808_VC_G3_3_DTT_IAA_postelution.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD071066/250808_VC_G3_1_DTT_IAA_postelution.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD071066/250729_VC_ctrl_tears_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD071066/250729_VC_ctrl_tears_3.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["stacy.malaker@yale.edu"],"submitter":["Vincent Chang"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Tear fluid","Lc-ms/ms","Galectin-3"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD071066"],"tissue":["Tear"],"sample_protocol":["Preparation of Galectin-3 beads The pET28 plasmids for His-tagged SmE and Gal-3 was kindly provided by the Bertozzi laboratory. NHS-activated beads were first washed 3x with 1mL of PBS. Next, Gal-3 (1 mg/mL in 1mL PBS) was conjugated to NHS-activated beads (500 µL bead slurry) overnight with agitation at 4 °C. After removing the supernatant the following day, free NHS-esters were capped by adding 100 mM Tris, pH 7.4, to the bead slurry for 20 min at 4 °C. BCA assays were performed after the reactions in order to determine the sufficient binding efficiency. After capping, beads were washed 3x with a high-salt buffer (20 mM Tris and 500 mM NaCl) followed by a buffer without salt (20 mM Tris).  Galectin-3 affinity-based enrichment Tears (diluted to 500 µL with PBS with a final concentration of 0.5 mg/mL) were loaded onto Gal-3-conjugated NHS beads (or NHS beads blocked with 100mM tris for control enrichments), washed 3 times with 20 mM Tris and 500 mM NaCl, and eluted with 0.5% SDC. Following elution, the mucin-enriched tear fluid was subjected to reduction (2mM DTT at 65 °C for 1 hour), alkylation (5mM IAA at 23 °C in the dark for 15 minutes), and proteolytic digestion with mucinase SmE (E:S ratio of 1:20 overnight at 37 °C) and trypsin (E:S ratio of 1:50 for 6 hours at 37 °C). All reactions were quenched by adding 1 µL of formic acid and diluted to a volume of 200 µL prior to desalting. Addition of formic acid also caused SDC to precipitate out of solution, and the resulting supernatant was transferred to a new tube before desalting. Desalting was performed using 10 mg Strata-X 33 µm polymeric reversed phase SPE columns (Phenomenex). Each column was activated using 500 µL of acetonitrile (ACN) (Honeywell) followed by of 500 µL of 0.1% formic acid, 500 µL of 0.1% formic acid in 40% ACN, and equilibration with two additions of 500 µL of 0.1% formic acid. After equilibration, the samples were added to the column and rinsed twice with 200 µL of 0.1% formic acid. The columns were transferred to a 1.5 mL tube for elution by two additions of 150 µL of 0.1% formic acid in 40% ACN. The eluent was then dried using a vacuum concentrator (LabConco) prior to reconstitution in 10 µL of 0.1% formic acid. The resultant peptides were then injected onto a Dionex Ultimate3000 coupled to a Thermo Orbitrap Eclipse Tribrid mass spectrometer. We employed a higher-energy collision dissociation product-dependent electron transfer dissociation (HCD-pd-ETD) method; in some cases, we used supplemental activation in ETD (EThcD). The files were searched using Byonic, followed by manual data curation.  Unenriched tear fluid processing Tear fluid proteins from each patient were diluted to a final concentration of 0.2 mg/mL in 100 µL of PBS. DTT was then added to a concentration of 2 mM and reacted at 65 °C for 1 hour followed by alkylation in 5 mM IAA for 15 min in the dark at RT. Subsequently, digestion with trypsin was done at a 1:50 E:S ratio for 6 hours at 37 °C. All reactions were quenched by adding 1 µL of formic acid and diluted to a volume of 200 µL prior to desalting. Desalting and sample injection into the mass spectrometer was performed as previously described in the GlycoFASP methods section."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw files were searched using Byonic (version 4.5.2, Protein Metrics, Inc.) against the UniProtKB/Swiss-Prot Homo sapiens proteome (Query: proteome:up000005640 AND reviewed:true) and a curated mucin database which was generated from a previous study. Briefly, the mucin database consists of nearly 350 proteins from Uniprot’s annotated human proteome predicted to bear the dense O-glycosylation characteristic of mucin domains. For all samples, we used the default O-glycan database containing 9 common structures. Raw files were first searched against the human proteome and then the curated mucin database. In both cases, files were searched with semi-specific cleavage N-terminal to Ser and Thr and six allowed missed cleavages. Samples treated with trypsin were searched with the same parameters but also allowed cleavage C-terminal to Arg or Lys. Mass tolerance was set to 10 ppm for MS1’s and 20 ppm for MS2’s. Met oxidation was set as a variable modification and carbamidomethyl Cys was set as a fixed modification. From the Byonic search results, glycopeptides were filtered to a score of >200 and a logprob of >2. From the remaining list of glycopeptides, the extracted ion chromatograms, full mass spectra (MS1s), and fragmentation spectra (MS2s) were investigated in XCalibur QualBrowser (Thermo) to generate a list of true-positive glycopeptides, as reported in Table 1. Each reported glycopeptide listed in Table 1 was manually validated from the filtered list of Byonic’s reported peptides (score>200 and logprob >2) according to the following steps: The MS1 was first used to confirm the precursor mass and chosen isotope was correct. This also allowed us to identify any co-isolated species that could interfere with the MS2s and/or explain unassigned peaks. The HCD and EThcD fragmentation spectra were then investigated to identify sufficient coverage to make a sequence assignment. When possible, multiple MS2 scans were averaged to obtain a stronger spectrum. For HCD, an initial glycopeptide identification was confirmed if the presence of the precursor mass without a glycan present (i.e., Y0), along with coverage of b and y ions without glycosylation. For longer peptides, we required the presence of Y0 and fragments that were expected to be abundant (e.g., N-terminally to Pro, C-terminally to Asp). When the peptide contained a Pro at the C-terminus, the bn-1 was considered sufficient. Further, when the sequence contained oxidized Met, the Met loss from the bare mass was considered as representative of the naked peptide mass. We then used electron-based fragmentation MS2 spectra for localization. Here, all plausible localizations were considered, regardless of search result output. We confirmed the presence of fragment ions in ETD or EThcD that were between potential glycosylation sites, if sufficient c/z ions were present then a glycan mass was considered localized. For glycopeptide manual validation, extracted ion chromatograms are evaluated at the MS1 level to determine the charge and m/z of the highest abundance precursor species."],"omics_type":["Proteomics"],"labhead":["Stacy Malaker"],"instrument_platform":[""],"labhead_affiliation":["Yale University"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["vincent.chang@yale.edu"],"publication":["10.1101/2025.11.24.690288"],"submitter_affiliation":["Yale University"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Galectin-3 binds isoform- and glycoform-specific lacritin in tear fluid","description":"Galectin-3 (Gal-3) is a carbohydrate-binding protein which plays crucial roles in inflammation, immune response, cell migration, autophagy, and signaling. At the ocular surface, Gal-3 is also known to crosslink transmembrane mucins across the epithelial cell glycocalyx, forming lattice structures important for barrier function. However, the biological role of Gal-3 in circulating tear fluid remains largely unexplored. Similarly, whether Gal-3 engages extracellular glycoproteins in tears to affect downstream biological processes has yet to be investigated. As increased Gal-3 levels in tears are known to correlate with ocular pathologies such as dry eye disease (DED), we sought to elucidate the Gal-3 interactome in tear fluid and uncover biological insights into the function of Gal-3 beyond adhesion to the epithelial cell surface. Here, we combined ELISA, lectin affinity enrichment, mass spectrometry (MS) glycoproteomics, and lectin blotting to uncover Gal-3 interactors and their associated glycoepitopes. Overall, we report nearly 100 proteins enriched from tear fluid across 3 different patients, identifying proteins involved in immune response, inflammation, and antimicrobial activity. Most notably, we report lacritin as a novel ligand for Gal-3 and demonstrate that specific glycoforms of lacritin bearing core 2 O-glycans preferentially engage with Gal-3. Lastly, we show that the Gal-3-lacritin axis is spliceoform-specific and dependent on lacritin multimerization. Taken together, this study elucidates new ligands for Gal-3 in tear film and reveals mRNA splicing and multimerization as new biochemical mechanisms which fine-tune Gal-3 binding events.","dates":{"publication":"2026-04-22","submission":"2025-11-22"},"accession":"PXD071066","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","NEWT:193528","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:57577","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:10031","NEWT:82569","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:109376","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:1190602","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:143292","NEWT:2767842","NEWT:314345","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NCBITaxon:5204","NEWT:1916073","NEWT:1303873","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:160620","NCBITaxon:77643","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:32224","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:1336794","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3710","NEWT:65125","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:32201","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:10882","NEWT:1431297","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3707","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:223074","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:2422","NEWT:2423","NEWT:3755","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:1195466","NEWT:2483192","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","NEWT:106299","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:427924","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:1120755","NEWT:1862567","NEWT:591090","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:29471","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:52694","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:366497","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:771875","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:480020","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:518","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:8086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