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Koomen"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["B cell lymphoma","Interferon","Inos","Macrophages","Chimeric antigen receptor t cell"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD079082"],"tissue":["T Cell"],"sample_protocol":["Sample Preparation:  Cells were lysed in denaturing lysis buffer containing 8M urea, 20 mM HEPES (pH 8), 1 mM sodium orthovanadate, 2.5 mM sodium pyrophosphate and 1 mM β-glycerophosphate. A Bradford assay was carried out to determine the protein concentration. 200 micrograms was used from each sample. The proteins were reduced with 4.5 mM dithiothreitol at 60 °C for 30 minutes and then cysteines were alkylated with 10 mM iodoacetamide for 20 minutes in the dark at room temperature. Trypsin digestion was carried out at room temperature overnight with enzyme to substrate ratio of 1:20, and tryptic peptides were then acidified with 1% trifluoroacetic acid (TFA) and desalted with C18 Sep-Pak cartridges according to the manufacturer’s procedure.  TMT Labeling:  Peptide from each sample was labeled with TMTPro18plex reagent. The label incorporation was checked for each channel by LC-MS/MS and spectral counting. 95% or greater label incorporation was achieved for each channel. The 16 samples were then pooled and lyophilized.  The TMT channel layouts were: No Macrophages samples were placed in 126C/127C/128C, No Macrophages +L-NIL samples were placed in 127N/128N/129N, Post coculture with M0 macrophages samples were placed in 129C/130C/131C, Post coculture with M0 macrophages +L-NIL samples were placed in 130N/131N/132N, Post coculture with M2 macrophages samples were placed in 132C/133C/134C, Post coculture with M2 macrophages +L-NIL samples were placed in 133N/134N/135N.   High pH Reversed Phase Peptide Separation:  After lyophilization, the peptides were re-dissolved in 400 µL of 20 mM Ammonium Formate, pH 10.0 (bRPLC A). The high pH reversed phase separation was performed on an XBridge BEH C18 column (4.6 mm ID x 100 mm length column packed with, 3.5 µm particle size, 130 Å pore size, Waters). The peptides were eluted as follows: 5% bRPLC solvent B (aqueous 5 mM Ammonium Formate, 90% acetonitrile, pH 10.0) for 10 minutes, 5% - 15% B in 5 minutes, 15-40% B in 47 minutes, 40-100% B in 5 minutes and 100% B held for 10 minutes, followed by re-equilibration at 1% B. The flow rate was 0.6 ml/min, and fractions were collected and concatenated into 12 fractions for phosphoproteomics (IMAC). Vacuum centrifugation (Speedvac) was used to dry the peptides.   IMAC enrichment Following lyophilization, the peptides were re-dissolved in aqueous IMAC loading buffer containing 0.1% TFA and 85% acetonitrile. The phosphopeptides in each fraction were enriched using IMAC resin (Cell Signaling Technology.# 20432) on a KingFisher robot (ThermoFisher). Ten microliters of IMAC resin beads was used for each sample.  Briefly, the IMAC resin was washed once with loading buffer (aqueous 85% acetonitrile, 0.1% TFA). The peptides were incubated with the IMAC resin for 30 minutes at room temperature, with gentle agitation. After incubation, the IMAC resin was washed twice with loading buffer followed by 1 wash with wash buffer (aqueous 80% ACN, 0.1% TFA). The phosphopeptides were eluted with elution buffer (aqueous 50% ACN, 2.5% Ammonia). The volume was reduced to 20 µl via vacuum centrifugation.  LC-MS/MS:  A nanoflow ultra high performance liquid chromatograph (RSLCnano, Thermo, , San Jose, CA) and an electrospray bench top orbitrap mass spectrometer with high field asymmetric waveform ion mobility spectrometry for charge state selection (Orbitrap Exploris 480 with FAIMS, Thermo, San Jose, CA) was used for tandem mass spectrometry peptide sequencing experiments.  The sample was first loaded onto a pre-column (C18 PepMap100, 100 µm ID x 2 cm length packed with, 5 µm particles, 100 Å pores) and washed for 8 minutes with aqueous 2% acetonitrile and 0.04% trifluoroacetic acid.  The trapped peptides were eluted onto the analytical column, (C18 PepMap100, 75 µm ID x 25 cm, 2 µm particles, 100 Å pores, Dionex, Sunnyvale, CA).  The 120-minute gradient was programmed as: 95% solvent A (aqueous 2% acetonitrile + 0.1% formic acid) for 8 minutes, solvent B (aqueous 90% acetonitrile + 0.1% formic acid) from 5% to 38.5% in 90 minutes, then solvent B from 50% to 90% B in 7 minutes and held at 90% for 5 minutes, followed by solvent B from 90% to 5% in 1 minute and re-equilibrate for 10 minutes.  The flow rate on analytical column was 300 nl/min. Cycle time was set at 1.5 sec for data dependent acquisition for two FAIMS compensation voltage values (-45 and -65). Spray voltage was 2100 V and capillary temperature was 300 °C. The resolution for MS and MS/MS scans were set at 120,000 and 45,000 respectively. Dynamic exclusion was 15 seconds for previously sampled peptide peaks."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["MaxQuant (version 1.6.14.0) was used to identify peptides and quantify the TMT reporter ion intensities using MaxQuant default settings.  The human protein database was downloaded from UniProt in March 2023. The mass tolerance was 20 ppm first search and 4.5 ppm main search. Reporter ion mass tolerance was set to 0.003 Da. Minimal Precursor intensity fraction 0.75.  Up to 2 missed trypsin cleavages were allowed per peptide. Carbamidomethyl cysteine was set as fixed modification. Phosphorylation on Serine/Threonine/Tyrosine and Methionine oxidation were set as variable modifications. Both peptide spectral match (PSM) and Protein FDR were set at 0.05. The “Match between Runs” feature was activated to identify peptides by MS/MS in at least one sample and LC retention time and accurate mass measurement in other samples.  Similar searches were performed in Mascot to support this data upload."],"omics_type":["Proteomics"],"labhead":["Marco Davila"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Roswell Park Cancer Center Buffalo, NY, USA"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["john.koomen@moffitt.org"],"submitter_affiliation":["Moffitt Cancer Center"],"submitter_country":["United States"],"doi":["10.6019/PXD079082"],"additional_accession":[]},"is_claimable":false,"name":"IFN-γ-driven iNOS induction in macrophages mediates CAR T cell resistance in B cell lymphoma: Phosphoproteomics","description":"Chimeric antigen receptor (CAR) T cell therapies have revolutionized B cell malignancy treatment, but subsets of patients with large B cell lymphoma (LBCL) experience primary resistance or relapse after CAR T cell treatment. To uncover tumor microenvironment (TME)-induced resistance mechanisms, we examined patients’ intratumoral immune infiltrates and observed that elevated levels of immunoregulatory macrophages in pre-infusion tumor biopsies are correlated with poor clinical responses. In murine models, CAR T cell-produced interferon-gamma (IFN-g) promotes the expression of inducible nitric oxide synthase (iNOS, NOS2) in immunoregulatory macrophages, impairing CAR T cell function. Mechanistically, proteomics analysis of CAR T cells revealed that iNOS-expressing macrophages promote the upregulation of genes mediating apoptosis and cell cycle arrest in CAR T cells, while downregulating ribosome biogenesis and protein synthesis. Furthermore, CAR T cell metabolism is compromised by the depletion of glycolytic intermediates and rewiring of the TCA cycle. Pharmacological inhibition of iNOS enhances the CAR T cell treatment efficacy in B cell tumor-bearing mice. Notably, elevated levels of iNOS+CD14+ monocytes were observed in leukaphereses of patients with non-durable response to CAR T cell therapy. These findings suggest that mitigating iNOS in tumor-associated macrophages (TAMs), potentially by modulating IFN-g expression in CAR T cells, could improve outcomes for LBCL patients.","dates":{"publication":"2026-05-30","submission":"2026-05-30"},"accession":"PXD079082","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","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:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","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:1255228","NEWT:410289","NEWT:373153","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:227377","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300273","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:380394","NEWT:226900","NEWT:1266738","NEWT:231490","NEWT:244704","NEWT:7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