The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium. Defects in LPL are the cause of lipoprotein lipase deficiency (LPL deficiency); also known as familial chylomicronemia or hyperlipoproteinemia type I. LPL deficiency chylomicronemia is a recessive disorder usually manifesting in childhood. On a normal diet, patients often present with abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive hypertriglyceridemia, sometimes complicated with acute pancreatitis. Belongs to the AB hydrolase superfamily. Lipase family. Note: This description may include information from UniProtKB.