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Lpl

Developmental stage

Maximum expression in adipose tissue during early development. In heart, low levels 6 days before birth increasing 278-fold as animals reach adulthood.

Function

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:8675619). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (By similarity). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:20620994, PubMed:24726386, PubMed:27811232).

Post-translational modifications

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

N-glycosylated.

Sequence Similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Tissue Specificity

Detected in white and brown adipose tissue and heart muscle, especially at the lumenal surface of capillaries (PubMed:20620994, PubMed:25066055, PubMed:27811232). Detected on capillary endothelium in the lactating mammary gland (PubMed:27811232). Detected in blood plasma (at protein level) (PubMed:17403372, PubMed:25066055). Expressed in liver, epididymal fat, heart, psoas muscle, lactating mammary gland, adrenal, lung, and ovary. Highest levels in heart and adrenal gland.

Cellular localization

Alternative names

Lipoprotein lipase, LPL, Phospholipase A1, rep, 1a-1b

swissprot:P11152