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Dazert"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"disease":["Hepatocellular Carcinoma"],"software":[""],"submitter_keywords":["Human","Super-silac","Sorafenib","Hepatocellular carcinoma (hcc)","(phospho)-proteomics ((p)proteomics)","Biopsies"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD028593"],"tissue":["Hepatocyte","Liver"],"sample_protocol":["Protein extraction and digestion Fresh biopsies were immediately snap-frozen in liquid nitrogen. Biopsies were crushed by cryogenic grinding and lyzed in 150 - 400ul lysis buffer (5 mM Tris-HCl pH 8.0, 8M urea, 150mM NaCl, 1mM PMSF, Complete Mini Protease Inhibitors (Roche) and PhosSTOP (Roche)). Biopsy lysate was vortexed for 5min, sonicated twice in a Ultrasonic cleaner bath for 1min and homogenized in a Heidolph homogenizer (RZR 2052 Control) at 300rpm for 2min. Samples were rotated for 30min at 4°C and centrifuged at 10,000rpm for 10min at 15°C. Protein concentration was measured by Bradford assay. A super-SILAC (Geiger and Mann, 2010; Geiger and Mann, 2011) mix was prepared from the HCC cell lines Huh7 of high and low passage, HepG2, Huh6 and Hep3B. This super-SILAC mix was added in a 1:1 ratio to the biopsy lysate. Proteins were reduced with 10mMDTT for 1h at 37°C and alkylated with 50mM iodoacetamide for 30min at RT in the dark. Urea concentration was lowered to 4M with 50mM Tris-HCl, pH 8.0. Lysates were digested with two rounds of endoproteinase LysC (Wako) at a 1:100 enzyme-to-protein ratio at 37°C for 2h. Next, urea concentration was lowered to 1M.  Lysates were digested with two rounds of trypsin (Promega) at 1:50 ratio overnight and 1:100 ratio for 2h at 37°C. A second trypsin aliquot (1:100 ratio) was added for 2.5h at 37°C. Digestion was stopped with TFA to 0.5%. Digests were centrifuged for 2min at 1,500g and desalted on a C18 SepPak cartridge (Waters) (Dephoure and Gygi, 2011). Peptide concentration was estimated at 280nm and peptides were dried in the SpeedVac. Strong cation exchange chromatography (SCX) SCX fractionation was done according to (Dephoure and Gygi, 2011) with modifications. The dried peptides were resuspended in 1.5ml of SCX buffer A (5mM KH2PO4, pH 2.65, 30% AcCN), briefly sonicated and centrifuged at 10,000rpm. The HiTrap SP cartridge (GE Healthcare) was equilibrated three times with 1ml of SCX buffer A, then washed three times with 1ml of SCX buffer B (5mM KH2PO4, pH 2.65, 30% AcCN containing 500mM KCl) and re-equilibrated three times with 1ml of SCX buffer A. Peptides were loaded and washed three times with 1ml SCX buffer A. Flow through and washes were collected separately. Bound peptides were stepwise desorbed with 1ml each of SCX buffer A containing 50mM, 100mM, 150mM, 250mM, 350mM, and 500mM KCl (optionally 10mM, 25mM) and the fractions were collected individually. The OD of each fraction was measured at 280nm. Fractions were dried in a SpeedVac and desalted on C18 columns (The Nest Group). 20% of each fraction, but maximum 30ug, were measured as proteome. P-peptide enrichment P-peptide enrichment was performed with titanium-dioxide (TiO2) coupled beads (GL Sciences Inc.) (Kettenbach and Gerber, 2011). P-peptides were desalted on MicroSpin columns or Stage Tips and dried in the SpeedVac.  LC-MS/MS analysis The first patient (NR1) was measured with the LC/MS settings described previously (Dazert and Hall, 2016), the second patient (NR2) was measured on a QExactive Plus (Thermo Scientific) with the LC/MS settings as described before (Dazert and Hall, 2016). The remaining patients were analyzed on a QExactive Plus with the following LC/MS settings. The dried p-/peptides were dissolved in 20ul of 0.1% formic acid. Proteomes and p-proteomes were analyzed using a homemade separating column (0.075mm x 38cm for proteome and 0.075mm x 20cm for p-proteome) packed with Reprosil C18 reverse-phase material (2.4μm particle size, Dr. Maisch, Germany). For the proteome, the column was heated to 55°C. Peptides were analyzed on a QExactive Plus coupled to an Easy nLC 1000 capillary pump (Thermo Scientific). The column was connected on-line and the solvents used for peptide separation were 0.1% formic acid in water (solvent A) and 0.1% formic acid/80% AcCN in water (solvent B). Proteome was measured with a metal T-cross and the p-proteome with a rubber T-cross. 2ul of sample were injected to a maximum pressure of 500bar for the proteome and 350bar for the p-proteome. For proteome measurements, a linear gradient from 0 to 40% solvent B in solvent A in 190min was delivered at a flow rate of 200nl/min. After 190min solvent B was increased to 95% in five minutes. For p-proteome measurements, a two-step gradient from 0 to 15% solvent B in solvent A in 55min followed by an increase to 40% solvent B in solvent A in 40min was delivered at a flow rate of 200nl/min. After 95min solvent B was increased to 95% in 25min. Peptides were ionized at 2.5kV and measured in data-dependent mode. Precursor scan was done in the Orbitrap at 70,000 resolution, and MS2 scan was done at 17,500 for the proteome and at 35,000 for the p-proteome. For the proteome, both maximum injection times (precursor scan and fragment ion scan) were set to 120ms, for the p-proteome to 60ms and to 120ms. A top twenty method was run. Each SCX fraction of each sample was measured in triplicates in proteome and p-proteome."],"repository":["Pride"],"quantification_method":[""],"modification":["","2x(15)N labeled L-lysine","4x(15)N labeled L-arginine"],"data_protocol":["Protein identification and data processing  The raw data were analyzed with MaxQuant, version 1.5.1.2 (Cox and Mann, 2008) and searched against the human SwissProt database (29.10.2013). The default settings of MaxQuant were used, except the following deviations: Multiplicity was set to 2 and Arg10 and Lys8 were set as labels; pSTY was set as variable modification; Main search peptide tolerance was set to 10ppm; Match-between-run and Re-quantify option was enabled; PSM FDR, Protein FDR and Site decoy fraction was set to 0.02; Protein quantification minimal ratio count was set to 1. All samples belonging to the same patient were analyzed together, but with an individual analysis for the proteome and p-proteome. An experimental design template was compiled, where all runs belonging to the same biopsy were labeled as one parameter group and all runs belonging to the same fraction were labeled as one fraction. The protein and pSTY datasets were exported into a FileMaker Pro 12 data bank. Normalized ratios H/L were taken for all analyses. Only p-sites with a localization probability of >50% were taken into account (class I/II/III sites). Ratios were log2-transformed and biopsies median subtracted. Quality control The proteome and p-proteome of 48 biopsies from eight patients was measured. Patient NR1 was measured as previously described on an Orbitrap Classic instrument (Thermo Scientific) (Dazert and Hall, 2016). Patient NR2 was measured on a QExactive Plus instrument (Thermo Scientific) with the same settings as previously described (Dazert and Hall, 2016). For the rest of the patients (NR3-NR5 and R1-R3), the settings were optimized as described above to increase ID recovery. Since the number of IDs recovered from NR1 and NR2 were low compared to the rest of the patients, these two patients were excluded from downstream analysis, but are still available as “training patients”, e.g. to validate a hypothesis. All biopsies from NR3-NR5 and R1-R3 passed the QC criteria, namely a clear subgrouping with the same tissue type biopsies in a principal component analysis."],"omics_type":["Proteomics"],"labhead":["Michael N. Hall"],"instrument_platform":[""],"labhead_affiliation":["Biozentrum Basel, University of Basel, Basel, Switzerland"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["eva.dazert@unibas.ch"],"publication":["26787912 Dazert E, Colombi M, Boldanova T, Moes S, Adametz D, Quagliata L, Roth V, Terracciano L, Heim MH, Jenoe P, Hall MN. Quantitative proteomics and phosphoproteomics on serial tumor biopsies from a sorafenib-treated HCC patient. Proc Natl Acad Sci U S A. 2016 113(5):1381-1386 10.1073/pnas.1523434113","41792761 Boot GF, Haak F, Coto-Llerena M, Boldanova T, Dazert E, Sedlaczek P, Rosenberger G, Esposito C, Ercan C, Wieland S, Renne SL, Benjak A, Matter MS, Di Tommaso L, Hall MN, Terracciano LM, Heim MH, Piscuoglio S, Ng CKY. Multi-omics profiling reveals divergent biology and liver microenvironment in HCC of metastatic and de novo origin. Mol Cancer. 2026 25(1):101 10.1186/s12943-026-02604-x"],"submitter_affiliation":["Biozentrum University of Basel"],"submitter_country":["Switzerland"],"pubmed_abstract":["Compensatory signaling pathways in tumors confer resistance to targeted therapy, but the pathways and their mechanisms of activation remain largely unknown. We describe a procedure for quantitative proteomics and phosphoproteomics on snap-frozen biopsies of hepatocellular carcinoma (HCC) and matched nontumor liver tissue. We applied this procedure to monitor signaling pathways in serial biopsies taken from an HCC patient before and during treatment with the multikinase inhibitor sorafenib. At diagnosis, the patient had an advanced HCC. At the time of the second biopsy, abdominal imaging revealed progressive disease despite sorafenib treatment. Sorafenib was confirmed to inhibit MAPK signaling in the tumor, as measured by reduced ribosomal protein S6 kinase phosphorylation. Hierarchical clustering and enrichment analysis revealed pathways broadly implicated in tumor progression and resistance, such as epithelial-to-mesenchymal transition and cell adhesion pathways. Thus, we describe a protocol for quantitative analysis of oncogenic pathways in HCC biopsies and obtained first insights into the effect of sorafenib in vivo. This protocol will allow elucidation of mechanisms of resistance and enable precision medicine."],"pubmed_title":["Multi-omics profiling reveals divergent biology and liver microenvironment in HCC of metastatic and de novo origin.","Quantitative proteomics and phosphoproteomics on serial tumor biopsies from a sorafenib-treated HCC patient."],"pubmed_authors":["Boot Gina F GF, Haak Fabian F, Coto-Llerena Mairene M, Boldanova Tuyana T, Dazert Eva E, Sedlaczek Philip P, Rosenberger George G, Esposito Cinzia C, Ercan Caner C, Wieland Stefan S, Renne Salvatore Lorenzo SL, Benjak Andrej A, Matter Matthias S MS, Di Tommaso Luca L, Hall Michael N MN, Terracciano Luigi M LM, Heim Markus H MH, Piscuoglio Salvatore S, Ng Charlotte K Y CKY","Dazert Eva E, Colombi Marco M, Boldanova Tujana T, Moes Suzette S, Adametz David D, Quagliata Luca L, Roth Volker V, Terracciano Luigi L, Heim Markus H MH, Jenoe Paul P, Hall Michael N MN"],"additional_accession":[]},"is_claimable":false,"name":"(Phospho)-proteomic characterization of longitudinal biopsies from HCC patients treated with sorafenib","description":"Tumor response rates to targeted therapy are generally low. This poses an urgent medical need to identify molecular mechanisms that determine responsiveness, to inform drug development and therapy. Here, we performed a proteomics and phospho-proteomics (p)proteomics analysis on longitudinal tumor biopsies from eight hepatocellular carcinoma (HCC) patients treated with sorafenib. Three of the patients were responders (group R) and five were nonresponders (group NR). Importantly, the patients clustered by therapy response based on proteomics and p-proteomics data. NR tumors showed increased EMT, glycogen storage, splicing and mitochondrial translation, and decreased carbohydrate metabolism. Furthermore, resistance did not correlate with mTOR signaling but with increased MAPK and decreased AMPK pathway activity. Additionally, phosphorylation of uncharacterized sites (p-sites) in NOTCH pathway components might promote resistance. Our findings suggest potential novel biomarkers for sorafenib-resistant HCC.","dates":{"publication":"2026-04-27","submission":"2021-09-17"},"accession":"PXD028593","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:111205","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:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","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: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:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","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:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","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:8655","NEWT:5147","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:40674","NEWT:1194669","NEWT:51329","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: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:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","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:4232","NEWT:416348","NEWT:11298","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:7725","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:72664","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:452467","NEWT:198822","NEWT:36111","NEWT:326424","NEWT:1678078","NEWT:749906","NEWT:418985","NEWT:749907","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