Lipoprotein lipase
| Lipoprotein lipase | ||
|---|---|---|
| Properties of human protein | ||
| Mass / length primary structure | 448 amino acids | |
| Cofactor | Apolipoprotein C2 | |
| Identifier | ||
| Gene names | LPL ; LIPD | |
| External IDs | ||
| Enzyme classification | ||
| EC, category | 3.1.1.34 , lipases | |
| Response type | hydrolysis | |
| Substrate | Triacylglycerol + H 2 O | |
| Products | Diacylglycerol + fatty acid | |
| Occurrence | ||
| Homology family | Pancreatic lipase | |
| Parent taxon | Coelomata | |
| Orthologue | ||
| human | House mouse | |
| Entrez | 4023 | 16956 |
| Ensemble | ENSG00000175445 | ENSMUSG00000015568 |
| UniProt | P06858 | P11152 |
| Refseq (mRNA) | NM_000237 | NM_008509 |
| Refseq (protein) | NP_000228 | NP_032535 |
| Gene locus | Chr 8: 19.9 - 19.97 Mb | Chr 8: 68.88 - 68.91 Mb |
| PubMed search | 4023 |
16956
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The water-soluble enzyme lipoprotein lipase (LPL) serves as a catalyst in the breakdown ( 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 fat synthesis. Mutations in the LPL - gene are for the rare hyperchylomicronaemia cause.
Lipoprotein lipase (LPL) is a water-soluble enzyme that is bound to the endothelial cells of the blood capillaries via proteoglycans and is produced (synthesized) in the liver . Its task is to split the fatty acid stores , which are dissolved in the blood and bound to protein-fat complexes , the triacylglycerine, into two fatty acids and monoacylglycerine and thus make them usable for the further metabolism. Like pancreatic lipase and other lipases , it is located outside cells, which is why they are also known as extracellular lipases. The glycerine released by the cleavage can be further metabolized in the liver while the fatty acids are taken up by the target cells. In this way, the supply of fat cells with fatty acids can be ensured. The lipoprotein lipase is stimulated by insulin , the cofactor for this reaction is the apolipoprotein C-II, which is part of chylomicrons and VLDL ( lipoproteins ). After intravenous heparin injection, the LPL can be released from the proteoglycan bond, which leads to increased LPL activity in the serum, called post-heparin lipolytic activity (PHLA).
swell
- Roche Lexicon Medicine, 5th edition; Urban & Fischer bei Elsevier, Munich 2003, ISBN 3-437-15150-9
- Pschyrembel Clinical Dictionary (261st edition), Verlag Walter de Gruyter 2007, ISBN 3-11-018534-2
- Vestweber, Dietmar: Endothelial cells: Barriers between blood and tissue, Activity report 2005, Max Planck Institute for Molecular Biomedicine
- Karlsons Biochemie und Pathobiochemie, 15th edition; by Peter Karlson, Detlef Doenecke, Jan Koolman, Georg Fuchs, Wolfgang Gerok, Georg Thieme Verlag 2005, ISBN 3133578154
- Beck-Sickinger, Hahn: Textbook of Biochemistry, 2nd Edition, Wiley-VCH Verlag 2010, ISBN 3527326677
Web links
- D'Eustachio P: chylomicron → TG-depleted chylomicron + 50 long-chain fatty acids + 50 diacylglycerols. In: reactome.org. EBI, April 30, 2007, accessed September 26, 2010 .