{"database":"JPOST Repository","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Wiff":["https://storage.jpostdb.org/JPST004583/files/cell_shHSP60_1_SWATH30.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shcontrol2_SWATH3.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shHSP60_2_IDA3.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shcontrol2_IDA30.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shcontrol1_IDA30.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shHSP60_2_IDA30.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shHSP60_1_IDA30.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shcontrol2_IDA3.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shHSP60_2_SWATH3.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shHSP60_2_SWATH30.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shcontrol3_SWATH30.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shcontrol1_SWATH3.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shHSP60_1_SWATH3.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shHSP60_1_IDA3.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shcontrol3_SWATH3.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shcontrol1_SWATH30.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shcontrol3_IDA3.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shcontrol1_IDA3.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shcontrol3_IDA30.wiff.scan","https://storage.jpostdb.org/JPST004583/files/cell_shcontrol2_SWATH30.wiff.scan"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Siripat Aluksanasuwan"],"species":["Homo Sapiens (human)"],"full_dataset_link":["https://repository.jpostdb.org/entry/JPST004583"],"submitter_affiliation":["Mahidol University"],"sample_protocol":[""],"repository":["jPOST"],"data_protocol":[""],"additional_accession":[]},"is_claimable":false,"name":"Heat shock protein family D member 1 (HSPD1) sustains ribosome biogenesis and protein synthesis as a component of its oncogenic function in lung adenocarcinoma","description":"Lung adenocarcinoma (LUAD) is the most prevalent histological subtype of lung cancer. Heat shock protein family D member 1 (HSPD1 or HSP60), a multifunctional chaperone, has been implicated in promoting lung cancer progression by regulating tumor cell growth, cancer-associated fibroblast activation, and angiogenesis. Despite these roles, the molecular mechanisms underlying its oncogenic activity remain incompletely understood. In this study, we conducted a proteomic analysis and functional investigations on HSPD1-knockdown and control A549 cells. Knockdown of HSPD1 suppressed cell proliferation, disrupted cell-cycle progression, and had no significant effect on apoptosis. Additionally, HSPD1-knockdown cells exhibited reduced colony formation, migration, and invasion capabilities. SWATH-targeted proteomics revealed 21 significantly altered proteins, mainly involved in ribosome-related functions and associated with overall survival in LUAD patients. Reduced levels of ribosomal proteins and translational capacity were further confirmed by Western blot and protein synthesis assays. A decrease in ribosome abundance in HSPD1-knockdown cells was also observed under transmission electron microscopy. HSPD1 knockdown also sensitized cells to homoharringtonine, a ribosomal-targeting chemotherapeutic. Collectively, these findings indicate that HSPD1 acts as an oncogenic driver in LUAD by modulating ribosome-related pathways and protein synthesis.","dates":{"publication":"Tue Apr 28 00:00:00 BST 2026"},"accession":"PXD077692","cross_references":{"TAXONOMY":["9606"]}}