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Bund"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Gel-based experiment","Bottom-up proteomics"],"disease":["Lung Carcinoma"],"software":[""],"submitter_keywords":["dietary cancer risk factors","indirect carcinogenesis","Lung cancer","bovine meat and milk factors","Lung cancer; bovine meat and milk factors; chronic inflammation; dietary cancer risk factors; indirect carcinogenesis","chronic inflammation"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077096"],"tissue":["Lung"],"sample_protocol":["Pieces from frozen lung tissue (~100 mg) were dissected on ice and subjected to lysis in 300 µl RIPA buffer containing protease/phosphatase inhibitor (Sigma-Aldrich, USA, Roche, Basel Switzerland) by using tissue homogenization (Bertin instruments, Montigny-le-Bretonneux, France: 3 x 20 s interval, ‘hard’, 4 °C) followed by clarification of the lysate via centrifugation (20 min, 22.000 g, 4 °C). 25 µg of protein were subjected to 4-20% SDS-PAGE gels (Invitrogen, USA), and the gel transfer-blotted on nitrocellulose (Turboblot, Biorad, Hercules, CA) for use in WB as described previously in Bund et al., PNAS 2021 (doi: 10.1073/pnas.2025830118). One peritumor tissue and one tissue adjacent to hamartoma with strong WB band detection were used for Rep immunoprecipitation (IP). 20 µg protein (in 1 ml RIPA buffer) were incubated with each 2 µg of anti-Rep antibody 2 (AB 2) or AB 10 for 1.5 h at 4 °C before addition of 30 µl Protein A/G plus-Agarose slurry and additional 1.5 h incubation. After washing (3x centrifugation at 600 g, 3 min, 4 °C, RIPA buffer), elution was performed with 2.5-fold Lämmli buffer, followed by SDS-PAGE and immunodetection with AB 3. To test IP, WB positive bands were analyzed by mass spectroscopy.   Proteins (20 µl) were run for 4 cm into an SDS-PAGE. After Coomassie staining, target bands were cut and digested with trypsin (Shevchenko, Andrej, et al. \"In-gel digestion for mass spectrometric characterization of proteins and proteomes.\" Nature protocols 1.6 (2006): 2856., adapted to on a DigestPro MSi robotic system [INTAVIS Bioanalytical Instruments AG]. Dried peptide samples were reconstituted (97.4% Water, 2.5% Hexafluoro-2-propanol and 0.1% trifluoroacetic acid) and half the resolubilization volume used for LC-MS/MS analysis on an Ultimate 3000 UPLC system (Thermo Fisher Scientific) with an Orbitrap Exploris 480 mass spectrometer (60 min) and online-desalting (Acclaim PepMap300 C18, 5 µm, 300 Å pore trapping cartridge; Thermo Fisher Scientific, 3 min , 30 µl/min flow of 0.05% TFA in water). The analytical multistep gradient (300 nl/min) was performed with a nanoEase MZ Peptide analytical column (300 Å, 1.7 µm, 75 µm x 200 mm, Waters) using solvent A (0.1% formic acid in water) and solvent B (0.1% formic acid in acetonitrile). Concentration of B was linearly ramped from 5% to 30% for 43 min, followed by a quick ramp to 80%. After one minute, the concentration of B was lowered to 2% followed by equilibration (10 min).  Eluting peptides were analyzed in the mass spectrometer using data dependent acquisition (DDA) mode. A full scan at 60k resolution (380-1400 m/z, 300% AGC target, 45 ms maxIT) was followed by up to 1.5 seconds of MS/MS scans. Peptide features were isolated with a window of 1.4 m/z, fragmented using 26% NCE. Fragment spectra were recorded at 15k resolution (100% AGC target, 54 ms maxIT). Unassigned and singly-charged eluting features were excluded from fragmentation and dynamic exclusion was set to 20 s."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Analysis was carried out by MaxQuant (1.6.14.0, Tyanova, Stefka, Tikira Temu, and Juergen Cox. \"The MaxQuant computational platform for mass spectrometry-based shotgun proteomics.\" Nature protocols 11.12 (2016): 2301) using an organism-specific database extracted from Uniprot.org (human reference database, 79,038 unique entries from 3rd January 2022) and a custom sequencing-based database (containing 4.489 entries) under default settings (except that label-free quantification [LFQ, default settings] and the iBAQ-value generation (Schwanhäusser, B., Busse, D., Li, N. et al. Global quantification of mammalian gene expression control. Nature 473, 337–342 (2011)) (Schwanhäusser et al., 2011) was enabled)."],"omics_type":["Proteomics"],"labhead":["Timo Bund"],"instrument_platform":[""],"labhead_affiliation":["Research Group leader"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["10.1002/IJC.70574"],"submitter_mail":["t.bund@dkfz-heidelberg.de"],"submitter_affiliation":["German Cancer Research Center (DKFZ)"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Lung cancer patients display increased expression of Bovine Meat and Milk Factor (BMMF) proteins in peritumor alveolar macrophages","description":"Besides smoking and exposure to specific environmental risk factors, also diet and in particular red meat consumption/exposure are described as risk factors contributing to lung cancer development.  Incidence of non-smoking associated lung cancer is rising rapidly, globally. Global epidemiology supports an association between lung cancer incidence and consumption of bovine products. The search for meat/milk-associated cancer risk factors led to the isolation of plasmid DNA termed Bovine Meat and Milk Factors (BMMFs). Due to detection of increased expression levels of a conserved BMMF-encoded protein (Rep) in tissues of colorectal cancer patients, BMMFs have been proposed as causal risk factors for cancer acting via inflammation-driven indirect carcinogenesis. Yet, their presence and possible contribution to lung cancer remained elusive. In this study, Rep expression was quantified in paired tumor/peritumor tissues from lung cancer patients (n=35) as well as cancer-free individuals (n=19, tissues adjacent to benign hamartoma) by IHC, co-immunofluorescence microscopy, immunodetection/mass spectroscopy and genomics/transcriptomics screening. In all patients tested, Rep expression was immunohistochemically observed in CD68+ CD163+ alveolar lung macrophages, which were present at higher numbers in peritumor tissues of cancer patients compared to controls. Expression was inversely correlated with smoking intensity, supporting BMMFs’ function as a new, smoking-independent biomarker and possible driver for lung cancer. BMMF+ macrophages revealed a cancer-promoting M2-like phenotype upon scRNA-seq suggesting BMMF as target for both prevention and therapy. BMMFs might contribute to lung cancer by inducing pro-tumorigenic macrophage populations and serve as marker for (early) cancer detection and prevention. Mass Spectroscopy was used to support immunohistologic and immunoblotting data for BMMF Rep protein detection data on the protein level after anti-BMMF Rep-specific  immunoprecipitation of lung tissue 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