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Cell culture HepG2 cells were cultured in α-MEM supplemented with 10% FBS, 1 mM of sodium pyruvate and 1% of non-essential amino acids (NEAA) and incubated at 37 °C in a humidified atmosphere with 5% CO 2 . Cell viability was assessed through trypan blue exclusion method2. In vitro cell viability analysis HepG2 were seeded in 96-well plates and exposed to 5, 10, 20, 30, 50, 60, 70 and 90 mM of APAP for 24h, after which APAP cytotoxicity was evaluated using the MTS reduction assay (Promega®), according to manufacturer’s instructions. The absorbance was measured at 490 and 690 nm using microplate reader SPECTROstar Omega (BMG Labtech®). The estimated half- maximal inhibitory concentration (IC 50 ) was calculated through a non-linear regression fit. 3. APAP injury establishment HepG2 in standard monolayer cultures were maintained in α-MEM with 10% FBS, 1 mM of sodium pyruvate and 1% of NEAA until reaching 80% confluence. After this, cells were incubated with 30 mM APAP in its basal medium without FBS (APAP-injury). To produce APAP- recovery, cells were washed two times with PBS after the 8 h APAP exposure and the medium was replaced by fresh basal medium without APAP and FBS in a final volume of 25 mL per 175 cm 2 t-flask for other 24 h. Both APAP-injury and APAP-recovery were collected under sterile conditions and centrifuged at 300xg for 10 minutes at 25 ºC, following 2700xg for 30 minutes at 4 ºC. The collected conditioned media was concentrated using Amicon® Ultra-15 (Millipore®) 3 kDa cut-off, as per manufacture’s recommendations, and used for total protein quantification and proteomics analysis. Cells were harvested for qRT-PCR analysis and protein quantification. Samples were stored at - 80 ºC until further use. HepG2 not exposed to APAP were collected in parallel as control. 4. LC-MS/MS analysis  Peptide mixtures were analyzed using a nanoLC system coupled to a high-resolution Orbitrap mass spectrometer (Thermo Fisher Scientific). Separation was achieved on a C18 column (75 µm × 25 cm, 2 µm particle size) with a linear gradient of 5–35% ACN in 0.1% formic acid over 90 min at a flow rate of 300 nL min⁻¹. The instrument operated in data-dependent acquisition mode with a top-20 method. Raw spectra were processed using MaxQuant (v2.2) against the Homo sapiens UniProt database."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Data filtering was performed based on the identification of at least 2 unique peptides in each protein and the respective protein should be found in at least 5 replicates. All contaminants were removed. Data processing was performed through Log2 transformation of all intensities. List of significantly regulated proteins were calculated with PolyStest (Schwämmle, Hagensen, Rogowska-Wrzesinska, & Jensen, 2020) and statistical significance was considered with a threshold of p < 0.05. Proteins were considered unique when present in more than 4 replicates in the injury conditions whilst not identified in at least 2 replicates in the control condition. Several web-available bioinformatic tools were used for identifying protein-protein interactions and their respective biological roles, namely String-DB (Szklarczyk et al., 2019) , MetaboAnlayst 5.0 (Pang et al., 2022) and GOrilla (Eden, Navon, Steinfeld, Lipson, & Yakhini, 2009) ."],"omics_type":["Proteomics"],"labhead":["Joana Miranda"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Research Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, Universidade de Lisboa, Lisbon, Portugal  rvitorino@ua.pt iBiMED- Department of Medical Siences University of Aveiro"],"species":["Homo Sapiens (human)"],"submitter_mail":["ruimpvitorino@gmail.com"],"publication":["10.3389/FPHAR.2026.1819323"],"submitter_affiliation":["Department of Medical Sciences, Institute of Biomedicine iBiMED, University of Aveiro, Aveiro, Portugal"],"submitter_country":["Portugal"],"additional_accession":[]},"is_claimable":false,"name":"Toxicoproteomics of HepG2 Reveals Translational Biomarkers of Paracetamol-Induced Liver Injury and Recovery","description":"Drug-induced liver injury (DILI) is a leading cause of acute liver failure (ALF) and a major obstacle in drug development, reflecting the limited predictive value of animal models and lack of robust,mechanism-based biomarkers. Human in vitro systems, coupled with unbiased omics approaches, have emerged as a potential alternative strategy. Here, quantitative toxicoproteomics was applied to paracetamol (acetaminophen; APAP)-exposed HepG2 cells to identify translational biomarkers of APAP-induced DILI. Cells were exposed to the IC₅₀ concentration of APAP for 8 h (injury phase), followed by drug withdrawal and a 24 h recovery phase. LC–MS/MS analysis quantified 1,478 proteins and revealed increased protein secretion upon APAP exposure. Notably, comparison of the proteomic dataset against available enriched proteomic profiles of ALF patients’ serum confirmed the clinical relevance of the molecular signature obtained. Injury-phase upregulated proteins, including KRT18 and HMGB1, recapitulated known clinical DILI biomarkers. Conversely, recovery was characterized by enrichment of the liver regeneration markers AFP, APOA1 and HP, enabling discrimination between injury and regeneration. HPD, S100A6 and TXNRD1 emerged as candidate diagnostic biomarkers, while SERPINA1 and complement components (C3, C5) showed prognostic potential. Collectively, this study demonstrates that toxicoproteomics applied to human in vitro hepatic models, validated against patient-derived data, enables the discovery of novel translational biomarkers of liver injury and 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