{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chow RP"],"funding":["Utenriksdepartementet","Eunice Kennedy Shriver National Institute of Child Health and Human Development","NICHD NIH HHS","Queen's University Belfast","Department for International Development, UK Government","USAID","National Institutes of Health","Bill and Melinda Gates Foundation","National Institute of Child Health and Human Development"],"pagination":["177138"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11634635"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["986"],"pubmed_abstract":["Background
Preeclampsia is prevalent in women with diabetes, but the mechanism is unclear. We previously found that oxidized, glycated lipoproteins robustly upregulated soluble fms-like tyrosine kinase-1 (sFlt1), a key mediator of preeclampsia. Here, we determined the role of protein kinase C (PKC) and its subtypes in sFlt1 regulation in placental trophoblasts, and whether this mechanism might mediate the effect of modified lipoproteins.Methods
Cultured human HTR8/SVneo and BeWo trophoblasts were treated with the PKC activator phorbol-12-myristate-13-acetate (PMA) for 24h, ± PKC inhibitors GF109203X (general), Ro31-8220 (PKCα-selective), LY333531 (PKCβ-selective) and rottlerin (PKCδ-selective). The effect of 'heavily oxidized, glycated' low-density lipoproteins (HOG-LDL) vs"],"journal":["European journal of pharmacology"],"pubmed_title":["Modified lipoprotein-induced sFlt1 production in human placental trophoblasts is mediated by protein kinase C."],"pmcid":["PMC11634635"],"funding_grant_id":["R01 HD096501","0703-03"],"pubmed_authors":["Li Y","Lyons TJ","Yu JY","Curtis TM","Chow RP","Zhao J"],"additional_accession":[]},"is_claimable":false,"name":"Modified lipoprotein-induced sFlt1 production in human placental trophoblasts is mediated by protein kinase C.","description":"Background
Preeclampsia is prevalent in women with diabetes, but the mechanism is unclear. We previously found that oxidized, glycated lipoproteins robustly upregulated soluble fms-like tyrosine kinase-1 (sFlt1), a key mediator of preeclampsia. Here, we determined the role of protein kinase C (PKC) and its subtypes in sFlt1 regulation in placental trophoblasts, and whether this mechanism might mediate the effect of modified lipoproteins.Methods
Cultured human HTR8/SVneo and BeWo trophoblasts were treated with the PKC activator phorbol-12-myristate-13-acetate (PMA) for 24h, ± PKC inhibitors GF109203X (general), Ro31-8220 (PKCα-selective), LY333531 (PKCβ-selective) and rottlerin (PKCδ-selective). The effect of 'heavily oxidized, glycated' low-density lipoproteins (HOG-LDL) vs","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2026-06-06T10:23:35.315Z","creation":"2026-05-28T03:13:22.138Z"},"accession":"S-EPMC11634635","cross_references":{"pubmed":["39551338"],"doi":["10.1016/j.ejphar.2024.177138"]}}