Lipoproteinlipase

  • OMIM: 238600
  • UniProt: P06858
  • MGI: 96820

The water-soluble enzyme lipoprotein lipase (LPL ) is used as a catalyst in the decomposition (hydrolysis) of triacylglycerols (triglycerides ) from lipoproteins, such as those found in chylomicrons and very low density lipoproteins (VLDL ). The resulting free fatty acids are used by the cells for the synthesis of fat. Mutations in the LPL gene are responsible for the rare Hyperchylomikronämie.

Lipoprotein lipase (LPL ) is a water-soluble protein substance ( enzyme) which is bonded via the proteoglycans on the endothelial cells of the blood capillaries in the liver and manufactured (synthesized ) is. She has the task dissolved in the blood and bound to protein - fat complexes fatty acid storage, the triacylglycerols to split into two fatty acids and monoacylglycerol and to thus utilize them for further metabolism. As the pancreatic lipase and other lipases it is outside of cells, they are called so as extracellular lipases. The released through the cleavage of glycerol can be metabolized in the liver further, while the fatty acids are taken up by the target cells. Thus, the supply of fat cells can be protected with fatty acids. Lipoprotein lipase is stimulated by insulin, a cofactor for this reaction is the apolipoprotein C-II, which is a component of chylomicrons and VLDL ( lipoproteins ) is. After the intravenous injection of heparin may result in a detachment of the LPL from the proteoglycan - binding, resulting in an increased LPL activity in the serum, known as post -heparin lipolytic activity ( pHLA ) leads.

Swell

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Human Genome Organisation Mouse Genome Informatics Endothelium
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