{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_Secretome_TMT2pLex_031218.msf"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_3_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_4_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_1_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_5_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_6_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_2_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_3_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_1_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_4_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_2_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_3_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_4_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_5_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_6_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_2_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_6_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_1_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_5_R1.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD011130/Okf6_Shisha_Secretome_TMT2pLex_031218.pdResult"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["harsha@ibioinformatics.org"],"submitter":["Harsha Gowda"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"software":[""],"submitter_keywords":["Oral cancer","Proteomics","Okf6/tert1","Tmt","Secretome","Waterpipe"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD011130"],"tissue":["Immortal Cell Line Cell"],"sample_protocol":["Cells were cultured in keratinocyte serum-free media (KSFM) (Life Technologies, Grand Island, NY) supplemented with bovine pituitary extract (25 mg/ml), calcium chloride (0.4 mM), epidermal growth factor (0.2 ng/ml) and 1% penicillin/streptomycin. To study the effects of shisha on oral keratinocytes, OKF6/TERT1 cells were chronically treated with 0.5% shisha extract for a period of 8 months (termed as OKF6/TERT1-Shisha) and maintained in a humidified CO2 chamber at 37ºC. Alongside, cells which were not treated with shisha were maintained for the same duration under similar conditions (termed as OKF6/TERT1-Parental). OKF6/TERT1-Parental and OKF6/TERT1-Shisha cells were grown to 80% confluence and washed thrice with PBS after removing the supplement-rich media. Cells were then grown in supplement-free media for 8 h. Subsequently, conditioned media was collected and centrifuged at 800 g for 10 min to remove any cell debris. The supernatant was filtered using a 0.22 μm filter and concentrated using a 3 kDa filter (Millipore, Burlington, MA).  Proteins concentrations from OKF6/TERT1-Parental and OKF6/TERT1-Shisha secretome were determined using bicinchoninic acid (BCA) assay (Thermo Scientific, Bremen, Germany) [28] and equal amount of protein was collected from both conditions for further processing. Samples were reduced using dithiothreitol (DTT) at 60ºC for 20 min and alkylated using iodoacetamide (IAA) for 10 min at room temperature. The samples were then precipitated using 6 volumes of chilled acetone at -80oC overnight. Following this, the samples were centrifuged for 15 min at 12,000 rpm, acetone was removed and the pellet was air-dried.  The pellets from both the treated and untreated conditions were then reconstituted in 4M urea. Protein samples were then digested using Lysyl Endopeptidase®, Mass Spectrometry Grade (Catalog#125-05061, Wako, Richmond, VA) in an enzyme-to-protein ratio of 1:100 for 4 h at 37oC. Following this, the urea concentration was reduced from 4M to 2M using 50mM TEABC. The samples were then digested using TPCK-treated trypsin (Worthington, NJ) at an enzyme-to-protein ratio of 1:20 for 16 h at 37ºC. This was followed by sample clean-up using Sep-Pak Classic C18 columns (Catalog#WAT051910, Waters, Milford, MA). The samples were then vacuum-dried and reconstituted in 50mM TEABC for TMT-labeling. Peptide samples were labelled using Tandem Mass Tag (TMT) labels (ThermoScientific, Bremen, Germany) as per manufacturer’s instructions. Peptides derived from OKF6/TERT1-Parental and OKF6/TERT1-Shisha secretome were labelled with TMT tags 130C and 131, respectively. TMT labelled peptides were pooled and subjected to basic pH reverse phase chromatography (bRPLC). The 96 fractions obtained were concatenated into 6 fractions. The fractions were vacuum-dried, desalted using C18 StageTips and subjected to mass spectrometry analysis. Peptide fractions were analysed on Orbitrap Fusion Tribrid mass spectrometer (Thermo Scientific, Bremen, Germany) interfaced with Easy nLC-1000 system (Thermo Scientific, Odense, Denmark). The peptide fractions were reconstituted in 0.1% formic acid (Solvent A) and loaded onto a trap column (75 μm x 2 cm, Magic C18AQ, 5 μm, 100 Å, Michrom Biosciences Inc., Auburn, CA) at a flow rate of 3 µl/min. The peptides were then resolved on an in-house packed analytical column 75 μm x 20 cm, Magic C18 AQ, 3 μm, 100 Å, Michrom Biosciences Inc., Auburn, CA) at a flow rate of 300 nl/min with back pressure of 275 bar using a gradient of 10% –35% solvent B (0.1% formic acid in 95% acetonitrile) for 100 min. Data acquisition on the Orbitrap Fusion was carried out using a data-dependent method with synchronous precursor selection MS3 scanning for TMT tags. The scan sequence was started with the acquisition of a full MS or MS1 one spectrum acquired in the Orbitrap (m/z range, 500-1600; resolution, 1.2x105; AGC target, 4x105; maximum injection time, 50 ms). MS2 scans were done in the linear ion trap using the following settings: quadrupole isolation at an isolation width of 2 m/z; fragmentation method, CID; normalized collision energy, 35%). Using synchronous precursor selection the 10 most abundant fragment ions were selected for the MS3 experiment following each MS2 scan. The fragment ions were further fragmented using the HCD fragmentation (normalized collision energy, 55%) and the MS3 spectrum was acquired in the Orbitrap (m/z range, 110-550; resolution, 5x104; AGC target, 5x104; maximum injection time, 100 ms). The peptide fractions were analysed in triplicate on the mass spectrometer."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Identification and quantification of proteins was carried out using Proteome Discoverer (version 2.1) software suite (Thermo Scientific, Bremen, Germany). Raw files were searched against NCBI human RefSeq protein database (version 75) containing common contaminants, using Sequest HT search algorithm. In the search parameters, carbamidomethylation of cysteine, and TMT label at peptide N-termini and lysine were set as static modifications; while oxidation of methionine was set as a dynamic modification. Trypsin was chosen as the protease with a maximum allowed missed cleavage of 1. Precursor mass tolerance was set to 10 ppm and fragment mass tolerance was set to 0.1 ppm. Decoy database search was carried out and peptide spectrum matches with a false discovery rate (FDR) cut-off of 1% was considered for peptide identification. Quantitative node in Proteome Discoverer was used to calculate protein ratios between OKF6/TERT1-Shisha and OKF6/TERT1-Parental using reporter ion intensities. Protein fold-change ratio was calculated as 131/130C (OKF6/TERT1-Shisha / OKF6/TERT1-Parental). Scatter plots were generated using log2 fold change ratio between replicates. Pearson correlation coefficient (r) was then calculated to evaluate the linear relationship between the technical replicates. A volcano plot was generated to depict the distribution of proteins based on their fold change and corresponding p-value."],"omics_type":["Proteomics"],"labhead":["Harsha Gowda"],"instrument_platform":[""],"labhead_affiliation":["Institute of Bioinformatics 7th floor, Discoverer building, International Tech Park, Bangalore 560 066"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["harsha@ibioinformatics.org"],"publication":["31033461 Patil S, Babu N, Subbannayya T, Mohan SV, Sathe G, Solanki HS, Rajagopalan P, Patel K, Advani J, Bhandi S, Sidransky D, Chatterjee A, Gowda H, Ferrari M. Secretome analysis of oral keratinocytes chronically exposed to shisha. Cancer Biomark. 2019 25(1):29-41 10.3233/cbm-182099"],"curator_keywords":["Biomedical"],"submitter_affiliation":["QIMR Berghofer Medical Research Institute"],"submitter_country":["Australia"],"pubmed_abstract":["<h4>Background</h4>Shisha smoking has been associated with multiple diseases including oral cancer. However, a mechanistic study to investigate alteration of secreted proteins in oral cells due to shisha smoking is lacking.<h4>Objectives</h4>Elucidation of differentially secreted proteins by immortalized human normal oral keratinocytes (OKF6/TERT1) upon chronic exposure to shisha.<h4>Methods</h4>OKF6/TERT1 was chronically treated with 0.5% shisha extract for 8 months. Conditioned media from shisha treated (OKF6/TERT1-Shisha) and untreated (OKF6/TERT1-Parental) cells were subjected to TMT-based quantitative proteomic analysis. Bioinformatics analysis of differentially secreted proteins was carried out using SignalP, SecretomeP and TMHMM. Immunoblot validation of selected proteins was carried out to confirm the proteomics results.<h4>Results</h4>Proteomic analysis of OKF6/TERT1-Parental and OKF6/TERT1-Shisha secretome resulted in the identification of 1,598 proteins, of which 218 proteins were found to be differentially secreted (⩾ 1.5-fold; p-value ⩽ 0.05) in shisha treated cells. Bioinformatics analysis using prediction tools showed secretory potential of differentially secreted proteins identified in OKF6/TERT1-Shisha. Western blotting validated the expression of AKR1C2, HSPH1 and MMP9 in OKF6/TERT1-Shisha secretome in agreement with proteomic data.<h4>Conclusion</h4>This study serves as a useful resource to understand the effect of chronic shisha smoking on the milieu of secreted proteins of oral cells. In vivo studies are warranted to supplement our in vitro data to elucidate the role of these proteins as early diagnostic biomarkers for oral carcinogenesis among shisha smokers."],"pubmed_title":["Secretome analysis of oral keratinocytes chronically exposed to shisha."],"pubmed_authors":["Patil Shankargouda S, Babu Niraj N, Subbannayya Tejaswini T, Mohan Sonali V SV, Sathe Gajanan G, Solanki Hitendra S HS, Rajagopalan Pavithra P, Patel Krishna K, Advani Jayshree J, Bhandi Shilpa S, Sidransky David D, Chatterjee Aditi A, Gowda Harsha H, Ferrari Marco M"],"additional_accession":[]},"is_claimable":false,"name":"Secretome analysis of oral keratinocytes chronically exposed to shisha","description":"Shisha smoking has been associated with multiple diseases including oral cancer. However, a mechanistic study to investigate alteration of secreted proteins in oral cells due to shisha smoking is lacking.  Elucidation of differentially secreted proteins by immortalized human normal oral keratinocytes (OKF6/TERT1) upon chronic exposure to shisha. OKF6/TERT1 was chronically treated with 0.5% shisha extract for 8 months. Conditioned media from shisha treated (OKF6/TERT1-Shisha) and untreated (OKF6/TERT1-Parental) cells were subjected to TMT-based quantitative proteomic analysis. Bioinformatics analysis of differentially secreted proteins was carried out using SignalP, SecretomeP and TMHMM. Immunoblot validation of selected proteins was carried out to confirm the proteomics results. Proteomic analysis of OKF6/TERT1–Parental and OKF6/TERT1-Shisha secretome resulted in the identification of 1,598 proteins, of which 218 proteins were found to be differentially secreted (≥ 1.5-fold; p-value ≤ 0.05) in shisha treated cells. Bioinformatics analysis using prediction tools showed secretory potential of differentially secreted proteins identified in OKF6/TERT1-Shisha. Western blotting validated the expression of AKR1C2, HSPH1 and MMP9 in OKF6/TERT1-Shisha secretome in agreement with proteomic data. This study serves as a useful resource to understand the effect of chronic shisha smoking on the milieu of secreted proteins of oral cells. In vivo studies are warranted to supplement our in vitro data to elucidate the role of these proteins as early diagnostic biomarkers for oral carcinogenesis among shisha smokers.","dates":{"publication":"2026-04-27","submission":"2018-09-18"},"accession":"PXD011130","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","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:224326","NEWT:376619","NEWT:3765","NEWT:3767","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:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:1616117","NEWT:34865","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","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:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:3750","NEWT:291146","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:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","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:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","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","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","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:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","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:4232","NEWT:9922","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","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: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:59202","NEWT:9975","NEWT:8643","NEWT:1801631","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:35231","NEWT:1774208","NEWT:8644","NEWT:1125630","NEWT:202914","NEWT:222523","NEWT:27602","NEWT:502779","NEWT:297246","NEWT:483139","NEWT:101491","NEWT:8639","NEWT:8637","NEWT:1114970","NEWT:285272","NEWT:192222","NEWT:9963","NEWT:197911","NEWT:197912","NEWT:2785785","NEWT:82633","NEWT:129872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