Lipoprotein-lipase-scholarly-journal.php
Lipoprotein lipase is a member of the lipase
gene family including pancreatic lipase, lipase and endothelial lipase. It is a water-soluble enzyme that hydrolyzes triglycerides into two free fatty acids and one monoacylglycerol molecule in lipoproteins, such as those found in chylomicrons and very low-density lipoproteins (VLDL). It also works to promote the cellular uptake of chylomicron residues, lipoproteins rich in cholesterol, and free fatty acids. LPL is attached by the protein glycosylphosphatidylinositol HDL-binding protein 1 (GPIHBP1) and by heparan sulfated peptidoglycans to the luminal surface of the endothelial
cells in capillaries. Glucosidases then eliminate terminal glucose residues; once thought to be responsible for the conformational shift LPL needed to form homodimers and become catalytically active, this glucose trimming. The oligosaccharides are further altered in the Golgi apparatus to result either in two complex chains, or two complex chains and one high-mannose chain.
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