Endothelial Lipase Products

Description

Endothelial lipase (EL) is an essential element of HDL metabolism which catalyzes the hydrolysis of HDL-phospholipids for facilitating their clearance from circulation. EL is synthesized in endothelial cells, however, is also expressed in other cell types such as coronary artery endothelial cells, umbilical vein endothelial cells, hepatocytes, osteosarcoma cell lines etc. with highest levels seen in organs including liver, placenta, lung, thyroid, kidney, testis and corpus luteum of ovary. EL is synthesized as a 55 kD protein, secreted as a 68 kD mature protein and after secretion, a portion of EL is cleaved and inactivated by convertases. Uncleaved EL is bound to heparan-sulfate proteoglycans on the cell surfaces where via its bridging functions, it facilitates HDL particle binding/uptake and selective uptake of HDL cholesteryl esters. Through its marked sn-1 phospholipase activity, EL cleaves lipoprotein-associated phospholipids, primarily HDL-phosphatidylethanolamine (HDL-PE) and -phosphatidylcholine (HDL-PC), generating mostly saturated free fatty acids and sn-1 lyso sn-2 acyl lysophospholipids (LysoPL). By its rather weak lysophospholipase activity, EL further hydrolyzes some of those EL-generated LPL, liberating unsaturated FFA. EL expression increases in cultured endothelial cells exposed to interleukin-1 beta or TNF-alpha as well as in vivo upon LPS exposure suggesting its role in inflammatory conditions. Accordingly, an elevated EL levels are found in patients with subclinical inflammation as encountered in the metabolic syndrome and coronary atherosclerosis.

Bioinformatics

Product By Gene ID	9388
Alternate Names	EC 3.1.1 EC 3.1.1.3 EDLendothelial lipase ELlipoprotein lipase H Endothelial cell-derived lipase lipase, endothelial PRO719

Research Areas for Endothelial Lipase

Find related products by research area and learn more about each of the different research areas below.

Autophagy
Cholesterol Metabolism
Endothelial Cell Markers
Lipid and Metabolism
Microautophagy