ArticleThe Journal of biological chemistry2009
Identification of the active form of endothelial lipase, a homodimer in a head-to-tail conformation.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 43 citations in OpenAlex.
- ApoJ regulates endothelial lipase activity and stability.Protein science : a publication of the Protein Society · 2026Article
- Lowly Expressed Toxin Transcripts in Poorly Characterized Myanmar Russell's Viper Venom Gland.Biotech (Basel (Switzerland)) · 2025Article
- In Silico Description of the Direct Inhibition Mechanism of Endothelial Lipase by ANGPTL3.International journal of molecular sciences · 2024Article
- Serine Hydrolases in Lipid Homeostasis of the Placenta-Targets for Placental Function?International journal of molecular sciences · 2022Review
- Endothelial lipase mediates efficient lipolysis of triglyceride-rich lipoproteins.PLoS genetics · 2021Article
- NAD(H)-mediated tetramerization controls the activity ofProceedings of the National Academy of Sciences of the United States of America · 2021Article
- LIPG: an inflammation and cancer modulator.Cancer gene therapy · 2021Review
- Digenic Inheritance and Gene-Environment Interaction in a Patient With Hypertriglyceridemia and Acute Pancreatitis.Frontiers in genetics · 2021Article
- Endoplasmic reticulum quality control in lipoprotein metabolism.Molecular and cellular endocrinology · 2019Review
- The role of endothelial lipase in lipid metabolism, inflammation, and cancer.Histology and histopathology · 2018Review
- Increased Hepatic Expression of Endothelial Lipase Inhibits Cholesterol Diet-Induced Hypercholesterolemia and Atherosclerosis in Transgenic Rabbits.Arteriosclerosis, thrombosis, and vascular biology · 2017Article
- Oligomerization inhibits Legionella pneumophila PlaB phospholipase A activity.The Journal of biological chemistry · 2014Article
- The endothelial lipase protein is promising urinary biomarker for diagnosis of gastric cancer.Diagnostic pathology · 2013Article
- Biochemistry and pathophysiology of intravascular and intracellular lipolysis.Genes & development · 2013Review
- Genetic and structure-function studies of missense mutations in human endothelial lipase.PloS one · 2013Article
- Measurement of the phospholipase activity of endothelial lipase in mouse plasma.Journal of lipid research · 2013Article
- Transgenic expression and genetic variation of Lmf1 affect LPL activity in mice and humans.Arteriosclerosis, thrombosis, and vascular biology · 2012Article
- Comparative studies of vertebrate lipoprotein lipase: a key enzyme of very low density lipoprotein metabolism.Comparative biochemistry and physiology. Part D, Genomics & proteomics · 2011Article
- Lipase maturation factor 1 is required for endothelial lipase activity.Journal of lipid research · 2011Article
- Vertebrate hepatic lipase genes and proteins: a review supported by bioinformatic studies.Open access bioinformatics · 2011Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Endothelial lipase (EL) is a member of a subfamily of lipases that act on triglycerides and phospholipids in plasma lipoproteins, which also includes lipoprotein lipase and hepatic lipase. EL has a tropism for high density lipoprotein, and its level of phospholipase activity is similar to its level of triglyceride lipase activity. Inhibition or loss-of-function of EL in mice results in an increase in high density lipoprotein cholesterol, making it a potential therapeutic target. Although hepatic lipase and lipoprotein lipase have been shown to function as homodimers, the active form of EL is not known. In these studies, the size and conformation of the active form of EL were determined. Immunoprecipitation experiments suggested oligomerization. Ultracentrifugation experiments showed that the active form of EL had a molecular weight higher than the molecular weight of a simple monomer but less than a dimer. A construct encoding a covalent head-to-tail homodimer of EL (EL-EL) was expressed and had similar lipolytic activity to EL. The functional molecular weights determined by radiation inactivation were similar for EL and the covalent homodimer EL-EL. We previously showed that EL could be cleaved by proprotein convertases, such as PC5, resulting in loss of activity. In cells overexpressing PC5, the covalent homodimeric EL-EL appeared to be more stable, with reduced cleavage and conserved lipolytic activity. A comparative model obtained using other lipase structures suggests a structure for the head-to-tail EL homodimer that is consistent with the experimental findings. These data confirm the hypothesis that EL is active as a homodimer in head-to-tail conformation.
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