{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["299(3)"],"submitter":["Yachida N"],"pubmed_abstract":["Diacylglycerol kinase (DGK) α, which is a key enzyme in the progression of cancer and, in contrast, in T-cell activity attenuation, preferentially produces saturated fatty acid (SFA)- and/or monounsaturated fatty acid (MUFA)-containing phosphatidic acids (PAs), such as 16:0/16:0-, 16:0/18:0-, and 16:1/16:1-PA, in melanoma cells. In the present study, we searched for the target proteins of 16:0/16:0-PA in melanoma cells and identified heat shock protein (HSP) 27, which acts as a molecular chaperone and contributes to cancer progression. HSP27 more strongly interacted with PA than other phospholipids, including phosphatidylcholine, phosphatidylserine, phosphatidylglycerol, cardiolipin, phosphatidylinositol, phosphatidylinositol 4-monophosphate, and phosphatidylinositol 4,5-bisphosphate. More"],"journal":["The Journal of biological chemistry"],"pagination":["103019"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10023972"],"repository":["biostudies-literature"],"pubmed_title":["Saturated fatty acid- and/or monounsaturated fatty acid-containing phosphatidic acids selectively interact with heat shock protein 27."],"pmcid":["PMC10023972"],"pubmed_authors":["Yachida N","Miura Y","Hoshino F","Murakami C","Ebina M","Sakane F"],"additional_accession":[]},"is_claimable":false,"name":"Saturated fatty acid- and/or monounsaturated fatty acid-containing phosphatidic acids selectively interact with heat shock protein 27.","description":"Diacylglycerol kinase (DGK) α, which is a key enzyme in the progression of cancer and, in contrast, in T-cell activity attenuation, preferentially produces saturated fatty acid (SFA)- and/or monounsaturated fatty acid (MUFA)-containing phosphatidic acids (PAs), such as 16:0/16:0-, 16:0/18:0-, and 16:1/16:1-PA, in melanoma cells. In the present study, we searched for the target proteins of 16:0/16:0-PA in melanoma cells and identified heat shock protein (HSP) 27, which acts as a molecular chaperone and contributes to cancer progression. HSP27 more strongly interacted with PA than other phospholipids, including phosphatidylcholine, phosphatidylserine, phosphatidylglycerol, cardiolipin, phosphatidylinositol, phosphatidylinositol 4-monophosphate, and phosphatidylinositol 4,5-bisphosphate. More","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Mar","modification":"2025-04-04T14:16:35.47Z","creation":"2025-02-19T02:22:41.148Z"},"accession":"S-EPMC10023972","cross_references":{"pubmed":["36791913"],"doi":["10.1016/j.jbc.2023.103019"]}}