Lipoprotein lipase (LPL) is a key enzyme of lipid metabolism that hydrolysestriglycerides, providing free fatty acids for cells and affecting the maturation of circulating lipoproteins. The enzyme is thought to playa role in the development of obesity and atherosclerosis. Human LPLcontains 448 amino acids; sequence comparison indicates that human LPL,hepatic lipase, and pancreatic lipase are members of a gene family. Defects in LPL are a cause of familial chylomicronemia syndrome (or type Ihyperlipoproteinemia) and also of a form of deficiency characterised byhypertriglyceridemia. Familial chylomicronemia is a recessive disorderusually manifesting in childhood. On a normal diet, patients often presentwith abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptivexanthomata, and massive hypertriglyceridemia, sometimes complicated withacute pancreatitis.LPL and pancreatic lipase share ~30% sequence identity, suggesting a similartertiary fold. Molecular models of LPL have been constructed, based on X-ray crystal structures of pancreatic lipase. These models allowed theauthors to propose hypotheses on the structural determinants of LPL that areresponsible for heparin binding, dimer formation, and phospholipase activity.