{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD068422/HM_ObitrapLUMOS_20231222_01_DCD.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD068422/HM_ObitrapLUMOS_20231222_03_NDCD.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD068422/MaxQuant_output.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD068422/MaxQuant_v2.7.3.0.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["hmkhikia@uci.edu"],"submitter":["Haik Mkhikian"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Acute Leukemia"],"software":[""],"submitter_keywords":["Biotinylation","Plasma membrane","Surfaceome","Glycosylation","Intracellular pool"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD068422"],"tissue":["T Cell"],"sample_protocol":["Frozen biotinylated cell pellets were lysed in 8 M urea buffer containing 0.3 M NaCl, 50 mM sodium phosphate (pH 8.0), 0.5% IGEPAL CA-630, and 17.4 mM SDS. Lysates (1 mL per 20 million cells) were homogenized via needle shearing (19G, 21G, and 23G), followed by 30 s sonication. Lysates were centrifuged (15,000 × g, 15 min), and supernatants were incubated overnight at 4°C with streptavidin agarose resin (Thermo Fisher; 112.5 µL slurry per mL of lysate). Beads were washed five times with lysis buffer, followed by five washes in 8 M urea wash buffer (1.22 M NaCl, 7 mM SDS, 125 mM Tris-HCl pH 8.0, 10% ethanol, 10% isopropanol). Beads were washed with 25 mM ammonium bicarbonate (ABC), resuspended in 8 M urea in 25 mM ABC, and reduced with 5 mM TCEP (37°C, 15 min), followed by alkylation with 10 mM iodoacetamide (RT, dark, 30 min). Beads were digested on-bead first with LysC (1.6 µg per 100 µL bead volume, 4 h at 37°C), then diluted to 5.3 M urea and digested with trypsin (3.2 µg per 100 µL, 14 h at 37°C). Supernatants were acidified (TFA to pH 3), desalted using C18 cartridges (pre-conditioned with ACN, 50% ACN, 0.5% acetic acid, and 0.1% TFA), and eluted with 80% ACN. Eluates were dried via vacuum centrifugation and stored at –80°C."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Protein quantification from LC-MS/MS data was performed using MaxQuant software (version 1.6.0.16)(12). Raw mass spectrometry files were searched against the human SwissProt database (22,355 protein entries; July 2024)(14). MS/MS spectra were filtered to retain a maximum of eight fragment peaks per 100 Da interval. The precursor mass tolerance was set to 20 ppm for the initial search and 4.5 ppm for the main search. False discovery rates (FDR) for both peptide spectral matches and protein identifications were controlled at 1%, using the razor peptide approach. Trypsin was specified as the digestion enzyme, allowing up to two missed cleavages, with no allowance for nonspecific cleavage. Carbamidomethylation of cysteine residues was defined as a fixed modification, while methionine oxidation and N-terminal acetylation were set as variable modifications, allowing up to two variable modifications per peptide. Protein intensities were calculated as the integrated peak area across the chromatographic elution profile. For isotopic clusters, intensities from all isotopic peaks were summed. Only peptides classified as unique plus razor were used for quantification to ensure protein-level accuracy."],"omics_type":["Proteomics"],"labhead":["Haik Mkhikian"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Pathology and Laboratory Medicine, School of Medicine, University of california Irvine."],"species":["Homo Sapiens (human)"],"publication":["41453615 Sánchez CD, Balakrishnan A, Krisko B, Ahmmed B, Witchey L, Valenzuela O, Minasyan M, Pak A, Mkhikian H. Improved T Cell Surfaceomics by Depleting Intracellularly Labelled Dead Cells. Mol Cell Proteomics. 2025 25(2):101503 10.1016/j.mcpro.2025.101503"],"submitter_mail":["hmkhikia@uci.edu"],"submitter_affiliation":["Department of Pathology and Laboratory Medicine, School of Medicine, University of California Irvine."],"submitter_country":["United States"],"pubmed_abstract":["Although the plasma membrane (PM) is among the most biologically important and therapeutically targeted cellular compartments, it is among the most challenging to faithfully capture using proteomic approaches. The quality of quantitative surfaceomics data depends heavily on the effectiveness of the cell surface enrichment used during sample preparation. Enrichment improves sensitivity for low abundance PM proteins and ensures that the changes detected reflect PM expression changes rather than whole cell changes. Cell surface biotinylation with PM-impermeable, amine-reactive reagents is a facile, accessible, and unbiased approach to enrich PM proteins. However, it results in unexpectedly high contamination with intracellular proteins, reducing its utility. We report that biotinylating human cells with amine-reactive reagents intracellularly labels a small but reproducible population of nonviable cells. Although these dead cells represent only 5 ± 2% of the total, we find that in T cell preparations the dead cells account for 90% of labelled proteins. Depleting Annexin V positive dead T cells postlabelling removes ∼99% of the intracellularly labelled cells, resulting in markedly improved PM identifications, peptide counts, and intensity-based absolute quantification intensities. Correspondingly, we found substantial depletion of intracellular proteins, particularly of nuclear origin. Overall, the cumulative intensity of PM proteins increased from 4% to 55.8% with dead cell depletion. Finally, we demonstrate that immature ER/Golgi glycoforms of CD11a and CD18 are selectively removed by dead-cell depletion. We conclude that high intracellular labelling of nonviable cells is the major source of intracellular protein contaminants in amine-reactive surface enrichment methods and can be reduced by dead-cell depletion postlabelling, improving both the sensitivity and accuracy of PM proteomics."],"pubmed_title":["Improved T Cell Surfaceomics by Depleting Intracellularly Labelled Dead Cells."],"pubmed_authors":["Sánchez Christofer Daniel CD, Balakrishnan Aswath A, Krisko Blake B, Ahmmed Bulbul B, Witchey Luna L, Valenzuela Oceani O, Minasyan Minas M, Pak Anthony A, Mkhikian Haik H"],"additional_accession":[]},"is_claimable":false,"name":"Improved T cell surfaceomics by depleting intracellularly labelled dead cells","description":"Although the plasma membrane (PM) is among the most biologically important and therapeutically targeted cellular compartments, it is among the most challenging to faithfully capture using proteomic approaches. The quality of quantitative surfaceomics data depends heavily on the effectiveness of the cell surface enrichment used during sample preparation. Enrichment improves sensitivity for low abundance PM proteins and ensures that the changes detected reflect PM expression changes rather than whole cell changes. Cell surface biotinylation with PM-impermeable, amine-reactive reagents is a facile, accessible, and unbiased approach to enrich PM proteins. For unclear reasons however, it results in unexpectedly high contamination with intracellular proteins, reducing its utility. We report that biotinylating human cells with amine-reactive reagents intracellularly labels a small but reproducible population of non-viable cells. Although these dead cells represent only 52 % of the total, we find that in T cell preparations the dead cells account for 90 % of labelled proteins. Depleting Annexin V positive dead T cells post-labelling removes ~99% of the intracellularly labelled cells, resulting in markedly improved PM identifications, peptide counts, and iBAQ intensities. Correspondingly, we found substantial depletion of intracellular proteins, particular of nuclear origin. Finally, we demonstrate that immature ER/Golgi glycoforms of CD11a and CD18 are selectively removed by dead-cell depletion.  We conclude that intracellular labelling of non-viable cells is the major source of intracellular protein contaminants and can be reduced by dead-cell depletion post-labelling, improving both sensitivity and accuracy of PM proteomics.","dates":{"publication":"2026-02-09","submission":"2025-09-16"},"accession":"PXD068422","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","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:10029","NEWT:913645","NEWT:641809","NEWT:44250","NEWT:317447","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:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","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: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: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: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: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: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:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","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: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:13037","NEWT:519","NEWT:941638","NEWT:511","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:529120","NEWT:300641","NEWT:39655","NEWT:38323","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: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:202956","NEWT:483179","NEWT:315750","NEWT:99490","NEWT:632957","NEWT:265619","NEWT:11294","NEWT:754466","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:1479235","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:105812","NEWT:11298","NEWT:4233","NEWT:4236","NEWT:398031","NEWT:196627","NE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