LPL
GeneName
LPL
Summary
LPL, also known as lipoprotein lipase or lysophospholipase, is a 53kDa enzyme that is primarily expressed on the surface of endothelial cells and in various tissues, including adipose tissue, heart, and muscle. It plays a crucial role in lipid metabolism by hydrolysing triglycerides in lipoproteins, facilitating the uptake of fatty acids by tissues. LPL is secreted into the extracellular space and associates with lipoproteins such as chylomicrons and very-low-density lipoproteins (VLDL), where it acts on the triglycerides they carry. It also participates in various biological processes including cholesterol homeostasis and fatty acid metabolism, and binds to several molecules including apolipoproteins and heparin.
Importance
LPL is relevant to: - Lipid metabolism and cardiovascular health through its role in triglyceride hydrolysis and fatty acid uptake - Obesity and metabolic disorders as it influences adipose tissue development and lipid storage - Inflammatory responses, as it regulates the production of pro-inflammatory cytokines - Atherosclerosis, due to its involvement in lipoprotein remodelling and clearance
Top Products
For researchers investigating LPL, we recommend two primary antibodies that stand out for their performance. The first is the well-cited monoclonal antibody, Anti-Lipoprotein lipase antibody [LPL.A4] (ab21356), which has garnered 61 citations, reflecting its reliability in Western blotting (WB) and flow cytometry (FC). This antibody is a trusted choice for those looking to study LPL in detail. Additionally, we offer the recombinant antibody, Anti-Lipoprotein lipase antibody [EPR1555(2)] (ab172953), which is validated for use in Western blotting (WB) and immunohistochemistry (IHC). With its recombinant nature, this product ensures batch-to-batch consistency, making it an excellent option for researchers seeking dependable results in their experiments.
Abcam Product Citation Summary
The data indicates that the LPL antibody (ab21356) has been effectively used in Western blotting to study lipid homeostasis in mouse tissues, specifically white adipose and heart tissues. The context of the studies revolves around T. cruzi infection and its impact on lipid and cholesterol metabolism.
Abcam Product Citation Table
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: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).
Involvement in disease
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.
Post-translational modifications
Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.
Sequence Similarities
Belongs to the AB hydrolase superfamily. Lipase family.
Tissue Specificity
Detected in blood plasma (PubMed:11893776, PubMed:12641539, PubMed:2340307). Detected in milk (at protein level) (PubMed:2340307).
Cellular localization
- 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).
Alternative names
LIPD, LPL, Lipoprotein lipase, Phospholipase A1