An enzyme produced in fat cells (adipocytes) and bound to the walls of capillaries. It breaks down triacylglycerols (triglycerides) into free fatty acids and glycerol, which can enter cells for storage or energy production.
| Sports Science and Medicine: lipoprotein lipase |
An enzyme produced in fat cells (adipocytes) and bound to the walls of capillaries. It breaks down triacylglycerols (triglycerides) into free fatty acids and glycerol, which can enter cells for storage or energy production.
| 5min Related Video: Lipoprotein lipase |
| Medical Dictionary: lipoprotein lipase |
An enzyme that cleaves one fatty acid from a triacylglycerol.
| Wikipedia: Lipoprotein lipase |
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| Lipoprotein lipase | ||||||||||||||
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| Identifiers | ||||||||||||||
| Symbols | LPL; LIPD | |||||||||||||
| External IDs | OMIM: 238600 MGI: 96820 HomoloGene: 200 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| More reference expression data | ||||||||||||||
| Orthologs | ||||||||||||||
| Species | Human | Mouse | ||||||||||||
| Entrez | 4023 | 16956 | ||||||||||||
| Ensembl | ENSG00000175445 | n/a | ||||||||||||
| UniProt | P06858 | n/a | ||||||||||||
| RefSeq | NM_000237 (mRNA) | XM_977885 (mRNA) | ||||||||||||
| NP_000228 (protein) | XP_982979 (protein) | |||||||||||||
| Location | Chr 8: 19.84 - 19.87 Mb |
n/a | ||||||||||||
| PubMed search | [1] | [2] | ||||||||||||
Lipoprotein lipase (EC 3.1.1.34) is an enzyme that hydrolyzes lipids in lipoproteins, such as those found in chylomicrons and very low-density lipoproteins (VLDL), into two free fatty acids and one monoacylglycerol molecule. It requires Apo-CII as a cofactor. [1]
Lipoprotein lipase is specifically found in endothelial cells lining the capillaries.
LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. LPL functions as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Severe mutations that cause LPL deficiency result in type I hyperlipoproteinemia, while less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism.[2]
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Insulin is known to induce LPL synthesis in adipocytes and its placement in the capillary endothelium.
LPL has different isozymes in different tissues. The form that is in adipocytes is activated by insulin, whereas that in muscle and myocardium is not. This helps to explain why adipose cells gain fat in a well-fed state.
Lipoprotein lipase deficiency leads to hypertriglyceridemia (elevated levels of triglycerides in the bloodstream).[3]
Diets high in refined carbohydrates have been shown to cause tissue-specific overexpression of LPL: This has been implicated in tissue-specific insulin resistance and consequent development of type 2 diabetes mellitus.[citation needed]
Lipoprotein lipase has been shown to interact with LRP1.[4][5][6]
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