{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W4_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W5_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W2_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W4_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W3_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W2_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W5_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W5_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W2_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W4_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W3_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W3_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W2_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W3_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W5_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W3_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W4_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W4_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W4_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W3_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W5_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W2_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_W5_4.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059613/XA08740DA_post_H282.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["Zh1944145081@163.com"],"submitter":["Hui Zhang"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD059613"],"tissue":["Liver"],"sample_protocol":["The samples were immediately frozen in liquid nitrogen and then lysed with lysis buffer (1% Triton X-100, 1% protease inhibitor cocktail) using a high-intensity ultrasonic processor for 3 min on ice. Then, the protein samples were digested with trypsin and reduced and alkylated with 5 mM dithiothreitol (DTT) and 11 mM iodoacetamide, and finally desalted using Strata X SPE columns (catalog #8B-S100-AAK, Phenomenex). Next, the tryptic peptides were dissolved in solvent A (0.1% formic acid, 2% acetonitrile/in water) and solvent B (0.1% formic acid, 90% acetonitrile/in water). Peptide separation was performed using a linear gradient of solvent B, where the percentage indicates the proportion of the strong elution solvent B in the mobile phase. The gradient profile was as follows: 0 to 22.5 min, 6% to 22% B; 22.5 to 26.5 min, 22% to 34% B; 26.5 to 28.5 min, 34% to 80% B; and 28.5 to 30 min, 80% B. This separation was performed on an Easy-nLC 1200 nanoflow ultrahigh-pressure liquid chromatography (UPLC) system (Thermo Fisher Scientific) at a constant flow rate of 700 nl/min. The separated peptides were analyzed in Orbitrap Exploris 480 (Thermo Fisher Scientific) with a nano-electrospray ion source."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["1.Database Search The DIA data were processed using DIA-NN search engine (v.1.8). Tandem mass spectra were searched against Homo sapiens 9606 SP 2023120.asta (20429 entries) concatenated with reverse decoy database."],"omics_type":["Proteomics"],"labhead":["Hui zhang"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Clinical Laboratory, Key Laboratory of Molecular Biology for Infectious Diseases (Ministry of Education), The Second Affiliated Hospital, Chongqing Medical University, Chongqing, China."],"species":["Homo Sapiens (human)"],"publication":["42147354 Zhang H, Gu L, Su X, Chen W, Tan M, Yu H, Zhou H, Gao T, Wang Z, Chen X, Chen W, Chen J, Cheng S. Dysregulated Proline Metabolism Exacerbates Hepatocellular Carcinoma Metastasis via EPRS1-Mediated mRNA Translation. Cancer Commun (Lond). 2026 46:0028 10.34133/cancomm.0028"],"submitter_mail":["zh1944145081@163.com"],"submitter_affiliation":["Department of Clinical Laboratory, Key Laboratory of Molecular Biology for Infectious Diseases (Ministry of Education), The Second Affiliated Hospital, Chongqing Medical University, Chongqing, China."],"submitter_country":["China"],"pubmed_abstract":["<b>Background:</b> Metabolic reprogramming is a hallmark of hepatocellular carcinoma (HCC), and amino acid reprogramming plays an important role in its metastatic progression. However, the function of amino acid reprogramming in HCC metastatic progression remains unclear. This study aimed to elucidate the function and mechanism of amino acid reprogramming, particularly focusing on proline metabolism, in driving HCC metastasis. <b>Methods:</b> HCC cohort and multiple HCC models were enrolled to investigate the role of amino acid reprogramming in HCC metastatic progression. The pro-metastatic effect of l-proline in HCC was consistently validated across in vitro and in vivo studies. Ribosome profiling (Ribo-seq) and l-proline pull-down were used to investigate the mechanism of proline-mediated HCC metastasis. <b>Results:</b> Based on metabolomics and proteomics, we found that proline metabolism was enhanced during HCC metastasis, as evidenced by increased proline levels and proline metabolism-related enzymes in both HCC metastatic patients and mice. Moreover, high levels of proline were found to promote HCC metastasis. Mechanistically, l-proline directly interacted with glutamyl-prolyl-tRNA synthetase 1 (EPRS1) at its Glu<sup>1123</sup> residue, thereby selectively enhancing the translation of phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit α (PIK3CA), AKT serine/threonine kinase 3 (AKT3), and integrin subunit β1 (ITGB1). Importantly, the enhanced protein translation could be abolished by bersiporocin, an EPRS1 inhibitor that prevents l-proline binding to EPRS1. Finally, the inhibitory effect of bersiporocin on HCC metastasis was confirmed in patient-derived orthotopic xenograft models. <b>Conclusions:</b> Our findings not only revealed the critical role of l-proline-bound EPRS1 in promoting HCC metastasis but also indicated that inhibiting this binding could be a promising strategy to prevent metastasis."],"pubmed_title":["Dysregulated Proline Metabolism Exacerbates Hepatocellular Carcinoma Metastasis via EPRS1-Mediated mRNA Translation."],"pubmed_authors":["Zhang Hui H, Gu Leirong L, Su Xiameng X, Chen Wanjin W, Tan Ming M, Yu Haibo H, Zhou Hongzhong H, Gao Tingting T, Wang Zhiling Z, Chen Xinyan X, Chen Weixian W, Chen Juan J, Cheng Shengtao S"],"additional_accession":[]},"is_claimable":false,"name":"Liver tumor tissues extracted from a mouse model of hepatocellular carcinoma were subjected to proteomics","description":"The highly metastatic MHCC-97H HCC cell line was orthotopic transplanted into the liver of nude mice to induce orthotopic tumor formation, and lung metastasis was observed. This experimental model not only reproduces the metastasis process of HCC in vivo, but also provides an important biological material for studying the tumor microenvironment and metastasis mechanism.  Subsequently, we collected liver cancer tissues, and further conducted in-depth proteomic analysis of the collected liver tumor tissue samples, in order to reveal the key protein expression changes and potential signaling pathway regulation mechanisms during tumor development and metastasis, and lay the foundation for subsequent targeted therapy 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