Description
LPL (LipoProtein Lipase; also LIPD) is a 53-56 kDa glycoprotein member of the Lipase family, AB Hydrolase superfamily of molecules. It is produced by multiple cell types, including adipocytes, skelelal muscle cells and macrophages. Once secreted, the circulating enzyme ultimately becomes immobilized on the surface of endothelium by binding to cell surface heparan sulfate. Here, it hydrolyzes triglycerides embedded in chylomicrons and VLDLs by homodimerizing and interacting with apoC2. Mature human LPL is 448 amino acids (aa) in length. It contains an enzymatic region (aa 37-334) plus one protein-interaction PLAT domain (aa 341-465). Over aa 28-154, human LPL shares 91% aa identity with mouse LPL