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The medium was replaced with serum-free DMEM containing P/S, and the cells were propagated for an additional 24 h before cell harvesting. Cell pellets were washed using cold 1× PBS and spun down at 4°C. Cell pellets were snap-frozen using liquid nitrogen prior -80°C storage and processing. Cell pellets were lysed in 8 M urea, 100 mM NH4HCO3, 1 mM DTT, pH 8.0. The total protein content of the cell lysate was determined using the BCA Protein Assay Kit (Thermo Scientific). Two hundred µg of total protein per sample were reduced (10 mM DTT, 30 min at 30°C), alkylated (55 mM chloroacetamide, room temperature, 30 min, in the dark) and diluted to 1.3 M urea with 50 mM NH4HCO3. Protein digestion was performed by adding trypsin (Trypsin Gold mass spectrometry grade, Promega, 1:50 enzyme-to-substrate ratio) and incubation overnight at 37°C. Digests were acidified with 1% formic acid (FA) and desalted using 50 mg tC18 reversed-phase (RP) solid-phase extraction cartridges (Sep-Pak, Waters, WAT054960). Peptide solutions were dried and frozen at -80°C until TMT-labeling.  TMT labeling and offline peptide fractionation In total, 10 samples were analyzed, including 5 biological replicates of KPC and AKPC cell lines. The 10 samples were measured in a TMT11-plex experiment, together with one pooled sample. TMT11-plex-labeling was carried out according to Zecha et al. Briefly, peptide solutions (200 μg protein amount per sample) were reconstituted in 20 μL of 100 mM HEPES buffer (pH 8.5). Next, TMT11-plex reagents (Thermo Fisher Scientific) in 100% anhydrous acetonitrile were added in a final concentration of 11.6 mM to all peptide sample. After incubation for 1 h at 25°C and 400 rpm, the labeling reaction was stopped by adding 2 μL of 5% hydroxylamine (15 min, at 25°C and 400 rpm). The 11 peptide samples were pooled and dried down. Subsequently, they were desalted using 500 mg tC18, RP solid-phase extraction cartridges (Sep-Pak, Waters, WAT020805), dried and frozen at -80 °C. Finally, the TMT11-plex experiment was off-line fractionated using basic reverse phase chromatography. Briefly, 150 µg of  peptides were reconstituted in 25 mM ammonium bicarbonate (pH 8.0) and loaded onto a C18 column (XBridge BEH130, 3.5 mm, 2.1 3 150 mm, Waters Corp.). Peptides were eluted with increasing acetonitrile concentration to 96 fractions and subsequently pooled to 32 fractions. All fractions were dried down before LC-MS/MS analysis.  LC-MS/MS measurements Nano-flow LC-MS/MS measurements of the TMT-labeled peptides were performed on a Fusion Lumos Tribrid mass spectrometer (Thermo Fisher Scientific) equipped with an Ultimate 3000 RSLCnano system. For each analysis, peptides were delivered to a trap column (ReproSil-pur C18-AQ, 5 μm, Dr. Maisch, 20 mm × 75 μm, self-packed) at a flow rate of 5 μL/min in 100% solvent A (0.1% formic acid in HPLC grade water). After 10 min of loading, peptides were transferred to an analytical column (ReproSil Gold C18-AQ, 3 μm, Dr. Maisch, 450 mm × 75 μm, self-packed with self-pulled tip using a Laser-Pipette-Puller P-2000) and separated using a 50 min gradient from 8% to 32% of solvent B (0.1% formic acid in acetonitrile and 5% (v/v) DMSO) at 300 nL/min flow rate. Both nanoLC solvents contained 5% DMSO (v/v). The Fusion Lumos was operated in data dependent acquisition (DDA), positive ionization and multi-notch MS3 mode. Full scan MS1 spectra were recorded over a range of 360-1500 m/z at a resolution of 60k using an automatic gain control (AGC) target value of 4e5 and maximum injection time (maxIT) of 50 ms. Precursor ions were filtered according to charge state (2-6), dynamic exclusion (60 s with a ± 10 ppm window), and monoisotopic precursor selection. MS2 spectra were recorded in the orbitrap at 30K resolution and with a quadrupole isolation window of 0.7 m/z (scan range mode: Auto:m/z Normal). Fragmentation was performed with collision induced dissociation (CID) and a normalized collision energy (NCE) of 35% (AGC target value 5e4, maximal injection time 60 ms). For TMT reporter ion quantification an additional MS3 spectrum was acquired in the orbitrap over an m/z range of 100-1000 m/z at 50k resolution. For this, fragment ions were selected by multi-notch isolation, allowing a maximum of 10 notches. MS1 precursor isolation was set to 0.7 m/z, while the MS2 isolation window width was set to 2 m/z. Fragmentation in the orbitrap was performed by HCD at 55% NCE (AGC target value 1e5, maximal injection time 120 ms). The overall cycle time of the method was 3 s."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["MaxQuant database searching Peptide identification and quantification were performed using MaxQuant (version 1.6.17.0) with its built-in search engine Andromeda. Raw files were searched against the UniProt mouse reference database (UP000000589 downloaded from UniProt July 2020, 55,462 protein entries) supplemented with common contaminants. MS3-based TMT quantification was enabled. For all searches, carbamidomethylated cysteine was set as fixed modification and oxidation of methionine and N-terminal protein acetylation as variable modifications. Trypsin/P was specified as the proteolytic enzyme with up to 2 missed cleavage sites. Precursor tolerance was set to ± 4.5 ppm, and fragment ion tolerance to ± 20 ppm. Results were adjusted to a 1% false discovery rate (FDR) on peptide spectrum match (PSM) and protein level employing a target-decoy approach using reversed protein sequences.  Proteomic data normalization and statistical analysis Before statistical analysis, we first log10-transformed and median-centered the protein intensity in each TMT channel, to remove the potential influence resulting from different sample loading amounts. Next, we used Student’s t-test to identify proteins that were significantly differentially expressed between experimental conditions. All analyses were performed using R (version 4.1.2)."],"omics_type":["Proteomics"],"labhead":["Christina Ludwig"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Bavarian Center for Biomolecular Mass Spectrometry (BayBioMS) School of Life Sciences Technical University Munich (TUM) Gregor-Mendel-Straße 4 85354 Freising GERMANY Bavarian Center for Biomolecular Mass Spectrometry Technische Universität München Gregor-Mendel-Straße 4 85354 Freising DEUTSCHLAND / GERMANY"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["tina.ludwig@tum.de"],"submitter_affiliation":["TU Munich"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Exploiting TGF-β-mediated Stromal Programming in Homologous Recombination-Deficient Pancreatic Cancer","description":"The tumor microenvironment (TME) actively contributes to pancreatic ductal adenocarcinoma (PDAC) pathogenesis via a dynamic bidirectional tumor–stroma dialog. Here, we show that homologous recombination-defective (HRD) neoplastic epithelium reprograms its TME in a genotype-specific manner to promote cancer aggressiveness. Autochthonous mouse models, co-culture systems, and human PDAC specimens revealed that tumoral ATM serine/threonine kinase status impacts cancer-associated fibroblast fate towards αSMA+ myofibroblastic (myCAF) differentiation, while P53 operates mostly tumor cell intrinsic. Vice versa, myCAFs foster cancer aggressiveness and specific chemoresistance patterns. Secretomics, proteomics, and in vitro approaches uncovered a greater TGF-β1 release in ATM-deficient cells associated with an enhanced reactive oxygen species/actomyosin-mediated mechanism. Pharmacological interference with TGF-β signaling reverts myofibroblast differentiation, chemoresistance, and tumor promotion in various ATM-deficient PDAC models. Overall, our findings demonstrate specific TME reprogramming by HRD PDACs towards a cancer-promoting fate, and their eligibility for combinatorial therapies targeting intrinsic vulnerabilities and extrinsic tumor–stroma oncogenic crosstalks.","dates":{"publication":"2026-04-27","submission":"2023-06-06"},"accession":"PXD042750","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: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:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","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:1310173","NEWT:161934","NEWT:1148","NEWT:5508","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:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","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:460523","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:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:2003758","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:219798","NEWT:548","NEWT:150475","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:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","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:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:300641","NEWT:39655","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:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:1479235","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:105812","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:9900","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:9979","NEWT:130821","NEWT:2320211","NEWT:27606","NEWT:290610","NEWT:1519788","NEWT:5920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