LPL

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:11342582, PubMed:27578112, PubMed:8675619). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (PubMed:12032167, PubMed:7592706). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:11342582, PubMed:27811232).

Hyperlipoproteinemia 1

HLPP1

An autosomal recessive metabolic disorder characterized by defective breakdown of dietary fats, impaired clearance of chylomicrons from plasma causing the plasma to have a milky appearance, and severe hypertriglyceridemia. On a normal diet, patients often present with abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive hypertriglyceridemia, sometimes complicated with acute pancreatitis.

None

The disease is caused by variants affecting the gene represented in this entry.

Hyperlipidemia, familial combined, 3

FCHL3

A disorder characterized by a variable pattern of elevated levels of serum total cholesterol, triglycerides or both. It is observed in a percentage of individuals with premature coronary heart disease. FCHL3 inheritance is autosomal dominant.

None

Disease susceptibility is associated with variants affecting the gene represented in this entry.

Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.

Belongs to the AB hydrolase superfamily. Lipase family.

Detected in blood plasma (PubMed:11893776, PubMed:12641539, PubMed:2340307). Detected in milk (at protein level) (PubMed:2340307).

• Cell membrane
• Peripheral membrane protein
• Extracellular side
• Secreted
• Secreted
• Extracellular space
• Extracellular matrix
• Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells (PubMed:27811232). Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles (By similarity).

LIPD, LPL, Lipoprotein lipase, Phospholipase A1

• entrezGene:4023
• omim:609708
• swissprot:P06858

Proteins

Immunology & Infectious Disease

53162Da