Lipoprotein lipase (LPL) (LPL)

Lipoprotein lipase (LPL) is a critical enzyme in lipid metabolism that catalyzes the hydrolysis of triglycerides within triglyceride-rich lipoproteins (TRLs), such as chylomicrons and very-low-density lipoproteins (VLDL) (UniProt: P06858). For LPL to function within the capillary lumen, it must be transported from the interstitial space across endothelial cells by the anchor protein Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1) (PubMed: 28258163). Once localized to the luminal surface, LPL breaks down triglycerides into free fatty acids and glycerol, which are then taken up by adjacent tissues like muscle and adipose for energy or storage (NCBI Gene: 4023). Deficiencies in LPL or its transporter GPIHBP1 lead to severe hypertriglyceridemia and familial chylomicronemia syndrome (FCS), significantly increasing the risk of acute pancreatitis (PubMed: 30609440). Therapeutic strategies include fibrates that increase LPL expression, gene therapies to replace defective LPL, and monoclonal antibodies or antisense oligonucleotides targeting LPL inhibitors like ANGPTL3 and ApoC-III to enhance residual LPL activity (PubMed: 31145631).

Other names

LPLLIPDLipoprotein lipaseTriacylglycerol lipaseGPIHBP1-LPL complex

Hydrolysis of triglycerides in chylomicrons and very-low-density lipoproteins (VLDL) into free fatty acids and monoacylglycerol, facilitated by the endothelial anchor GPIHBP1 and co-factor Apolipoprotein C-II.