<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>299(3)</volume><submitter>Yachida N</submitter><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</pubmed_abstract><journal>The Journal of biological chemistry</journal><pagination>103019</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10023972</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Saturated fatty acid- and/or monounsaturated fatty acid-containing phosphatidic acids selectively interact with heat shock protein 27.</pubmed_title><pmcid>PMC10023972</pmcid><pubmed_authors>Yachida N</pubmed_authors><pubmed_authors>Miura Y</pubmed_authors><pubmed_authors>Hoshino F</pubmed_authors><pubmed_authors>Murakami C</pubmed_authors><pubmed_authors>Ebina M</pubmed_authors><pubmed_authors>Sakane F</pubmed_authors></additional><is_claimable>false</is_claimable><name>Saturated fatty acid- and/or monounsaturated fatty acid-containing phosphatidic acids selectively interact with heat shock protein 27.</name><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</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Mar</publication><modification>2025-04-04T14:16:35.47Z</modification><creation>2025-02-19T02:22:41.148Z</creation></dates><accession>S-EPMC10023972</accession><cross_references><pubmed>36791913</pubmed><doi>10.1016/j.jbc.2023.103019</doi></cross_references></HashMap>