| Tissue Specificity | Detected in blood plasma. Detected in milk (at protein level). |
| Post Translational Modifications | Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity. |
| Function | Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans. |
| Protein Name | Lipoprotein LipaseLplPhospholipase A1 |
| Database Links | Reactome: R-HSA-381340Reactome: R-HSA-8963889Reactome: R-HSA-8963901Reactome: R-HSA-975634 |
| Cellular Localisation | Cell MembranePeripheral Membrane ProteinExtracellular SideSecretedExtracellular SpaceExtracellular MatrixNewly Synthesized Lpl Binds To Cell Surface Heparan Proteoglycans And Is Then Released By HeparanaseSubsequentlyIt Becomes Attached To Heparan Proteoglycan On Endothelial CellsLocates To The Plasma Membrane Of Microvilli Of Hepatocytes With Triglyceride-Rich Lipoproteins (Trl)Some Of The Bound Lpl Is Then Internalized And Located Inside Non-Coated Endocytic Vesicles |
| Alternative Antibody Names | Anti-Lipoprotein Lipase antibodyAnti-Lpl antibodyAnti-Phospholipase A1 antibodyAnti-LPL antibodyAnti-LIPD antibody |
Information sourced from Uniprot.org
