{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072559/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072559/Reference_File.csv"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072559/MS_mzML_FILES.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072559/DIANN_SEARCH_RESULTS_KRAS.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072559/DIANN_SEARCH_RESULTS.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["amund@omicvision.com"],"submitter":["Lisa Schweizer"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Pancreatic Ductal Adenocarcinoma"],"software":[""],"submitter_keywords":["Spatial","Pathology foundation models","Pancreatic ductal adenocarcinoma","Laser microdissection","Tumor","Deep visual proteomics","Precursor","Mass spectrometry","Artificial intelligence"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072559"],"tissue":["Malignant Cell","Pancreatic Ductal Adenocarcinoma Cell","Panin Cell","Epithelium Of Pancreatic Duct","Pancreatic Duct"],"sample_protocol":["The study cohort included tissue specimens from 20 cancer-free organ donors and 13 patients with PDAC. Tissues used for MS-based proteomics were procured within 4 hours post-mortem through the University of Nebraska Medical Center (UNMC) Normal Organ Recovery Program (NORs), in cooperation with Live On Nebraska, and through Rapid Autopsy Program (NRAP), or were obtained from surgical resections (Patient 6-10 with HG-cPanIN) at UNMC and MD Anderson Cancer Center (MDACC). Organ donor pancreas tissues used for orthogonal validation were obtained from Donor Network West (DNW). Formalin-fixed paraffin-embedded (FFPE) tissue blocks were sectioned at 3μm thickness and mounted on pre-coated 2.0 mm PEN membrane slides (MicroDissect GmbH). A total of 26 tissue specimens were selected based on the availability and quality of FFPE blocks suitable for laser microdissection. All procedures were conducted in accordance with the Declaration of Helsinki and approved by the UNMC (IRB 091-01) and MD Anderson (IRB#) Institutional Review Board, with written informed consent obtained prior to enrollment. All patient and donor data were de-identified and anonymized.  In preparation for tissue deparaffinization, PEN membrane microscopy slides with mounted tissue were incubated at 55°C for 20 min. Slides were then transferred to a series of twice 2 min in xylene and twice 1 min in 100% ethanol, 90% ethanol, 75% ethanol, 30% ethanol, and ddH2O. To achieve H&E staining, tissue was incubated in Hematoxylin (DAKO, CS700) for 45 sec, dipped briefly and then washed twice in ddH2O. The reaction was enhanced by incubation for 1 min in Bluing Buffer (DAKO, CS700), dipped briefly, washed twice in ddH2O and twice in 70% EtOH. Slides were then immersed for 3 min in Eosin (DAKO, CS701), dipped briefly and then washed for 1 min in 96% EtOH. The reaction was finalized by five washes for 1 min in absolute ethanol. Brightfield H&E images of cancer-free panel (iCohort) were acquired on a 3DHistech PANNORAMIC® 250 FLASH III microscope and cancer progression cohort (cCohort) was acquired on a 3DHistech Panoramic MIDI III microscope. Both sets were acquired with a Plan-Apochromat 40x/0.95 NA objective with extended focus ranging 1.6µm. Sample preparation was performed using an automated liquid handling platform (Agilent Bravo) to prepare mass spectrometry samples in a robust- and high-throughput manner, alongside a PCR cycler for incubation. Wells were rinsed with 30 μL of 100% acetonitrile, followed by centrifugation at 1,000 g for 10 min and vacuum evaporation in a SpeedVac system for 20 min at 60°C. For sample lysis, 6 μL of lysis buffer (0.2% n-Dodecyl-β-D-maltoside (DDM, Thermo Fisher Scientific, #89902), 0.1M triethylammonium bicarbonate (TEAB, Sigma-Aldrich, T7408) pH 8.5 in LC-MS grade H2O) were added, followed by an incubation period of one hour at 90°C. The incubation was repeated upon addition of 1 uL 80% acetonitrile (Fisher Scientific, A955-1) for one hour at 75°C. Protein digest into peptides was accomplished by an overnight digest with 10 ng/μL trypsin (Promega, V5117) and 10 ng/μL LysC (TriChem, Wako Chemicals, 129-02541) in MS-grade H2O at 37°C. For all incubation steps, the 384-well plate was sealed with an adhesive aluminum lid (Thermo Scientific, AB0626). The enzymatic reaction was quenched by 1 μL 8% TFA (VWR chemicals, # 153112E) to achieve a final concentration of 1% TFA (v/v) in the sample. In preparation for LC-MS/MS data acquisition, samples were loaded onto Evotips ‘Pure’ according to the manufacturer’s protocol. For standardized and high-throughput data acquisition, an Evosep One liquid chromatography System (Evosep Biosystems) coupled to Orbitrap Astral mass spectrometer (Thermo Fisher Scientific) was used. Liquid chromatography was performed using a 40 samples-per-day (40 SPD) Whisper-zoom standardized gradient (32.5 min) on an Aurora Elite XT 15 cm C18 column (IonOpticks, 75um inner diameter, 1.7um particle size, AUR3-15075C18-XT). The column was maintained at a constant temperature of 50 °C using a column heating unit (IonOpticks). MS data were acquired in DIA mode, where full MS1 scans were acquired in the Orbitrap analyzer (resolution: 240000, scan range: 380-980 m/z, RF Lens: 40 %, AGC target: 5e6 ions, maximum injection time: 5 ms), and 300 sequential MS/MS scans were acquired in Astral analyzer (precursor mass range (m/z): 380-980, isolation window: 2 m/z, HCD normalized collision energy: 25%, scan range: 150-2000 m/z, RF lens: 40%, AGC target: 5e4 ions, maximum injection time: 5 ms). The instrumentation was controlled with Orbitrap Astral Tune 1.1.477.46, Xcalibur 4.7.69, Chronos 4.9.00, and EvoSp One Chronos Plugin 3.0.12."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Data were processed and quantified using the DIA-NN software suite (v1.8.1). To this end, MS raw files were converted mzML files using MSConvert (ProteoWizard 3.0.24145.94d758d) and processed with a precomputed spectral library based on a deep learning-based spectra, RTs and IMs prediction and the human reference FASTA file (UP000005640_9606.fasta) in DIA-NN. Library and samples were processed using the default settings except for a fixed mass and MS accuracy (both 15.0).  Mutational FASTA sequences were generated by in silico mutagenesis of the KRAS reference sequence by substituting the reference amino acid at the specified residue position with the corresponding mutant residue (e.g., G12D). Mutated sequences were annotated with headers reflecting the introduced mutation. The set of mutations was selected based on the most frequently observed KRAS variants reported in Fig. 3 of Huang et al. 2021, encompassing colorectal, pancreatic, and lung cancers: G12A, G12C, G12D, G12R, G12V, G13C, G13D, Q61H, Q61R, and A146T. These variants represent the most frequently observed mutations in KRAS-driven cancers. Combined with the common FASTA file, the custom file was used as additional reference during data processing in DIA-NN 1.8.1 as for the main quantification of this manuscript. To increase identification confidence of altered peptides, KRAS variants were searched without the match-between-runs function."],"omics_type":["Proteomics"],"labhead":["Andreas Mund"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["OmicVision Biosciences ApS"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["admin@omicvision.com"],"submitter_affiliation":["OmicVision Biosciences ApS"],"submitter_country":["Denmark"],"additional_accession":[]},"is_claimable":false,"name":"AI-powered Deep Visual Proteomics unmasks critical molecular transitions in pancreatic cancer precursors","description":"Pancreatic ductal adenocarcinoma (PDAC) evolves through precursors, yet the protein programs that govern early progression remain poorly defined. We applied Deep Visual Proteomics - computational pathology, laser microdissection, and mass spectrometry (MS) - to profile normal ducts, acinar-to-ductal metaplasia (ADM), low- and high-grade pancreatic intraepithelial neoplasia (PanIN), and invasive carcinoma from organ donors and patients with PDAC. Quantifying 9,181 proteins from ~100 cells per region, we uncovered a molecular field effect in histologically normal ducts and showed that low-grade PanINs diverge by cancer context. Four programs - stress adaptation, immune engagement, metabolic reprogramming, and mitochondrial remodeling - emerged early and intensified with progression. High-grade PanINs exhibited distinct metabolic signatures preceding invasion. Notably, mass spectrometry detected KRAS hotspot mutant peptides directly within PanINs and ADM, providing protein-level evidence of oncogenic alteration in precursor lesions. These findings demonstrate that molecular reprogramming precedes histological transformation, creating opportunities for earlier detection of this lethal 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