Lipoprotein lipase

Lipoprotein lipase

Lipoprotein lipase (EC number| is an enzyme that hydrolyzes lipids in lipoproteins, like those found in chylomicrons and very low-density lipoproteins (VLDL), into three free fatty acids and one glycerol molecule. It requires Apo-CII as a cofactor. cite journal |author=Kim SY, Park SM, Lee ST |title=Apolipoprotein C-II is a novel substrate for matrix metalloproteinases |journal=Biochem. Biophys. Res. Commun. |volume=339 |issue=1 |pages=47–54 |year=2006 |pmid=16314153 |doi=10.1016/j.bbrc.2005.10.182]

Lipoprotein lipase is specifically found in endothelial cells lining the capillaries.

section_title =
summary_text = 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. [cite web | title = Entrez Gene: LPL lipoprotein lipase| url =| accessdate = ]


Insulin is known to enhance 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).cite journal |author=Okubo M, Horinishi A, Saito M, "et al" |title=A novel complex deletion-insertion mutation mediated by Alu repetitive elements leads to lipoprotein lipase deficiency |journal=Mol. Genet. Metab. |volume=92 |issue=3 |pages=229–33 |year=2007 |pmid=17706445 |doi=10.1016/j.ymgme.2007.06.018]

High-fat diets 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.Fact|date=January 2008


Further reading

citations =
*cite journal | author=Zechner R |title=The tissue-specific expression of lipoprotein lipase: implications for energy and lipoprotein metabolism |journal=Curr. Opin. Lipidol. |volume=8 |issue= 2 |pages= 77–88 |year= 1997 |pmid= 9183545 |doi=10.1097/00041433-199704000-00005
*cite journal | author=Fisher RM, Humphries SE, Talmud PJ |title=Common variation in the lipoprotein lipase gene: effects on plasma lipids and risk of atherosclerosis |journal=Atherosclerosis |volume=135 |issue= 2 |pages= 145–59 |year= 1998 |pmid= 9430364 |doi=10.1016/S0021-9150(97)00199-8
*cite journal | author=Beisiegel U |title=Lipoprotein metabolism |journal=Eur. Heart J. |volume=19 Suppl A |issue= |pages= A20–3 |year= 1998 |pmid= 9519338 |doi=
*cite journal | author=Pentikäinen MO, Oksjoki R, Oörni K, Kovanen PT |title=Lipoprotein lipase in the arterial wall: linking LDL to the arterial extracellular matrix and much more |journal=Arterioscler. Thromb. Vasc. Biol. |volume=22 |issue= 2 |pages= 211–7 |year= 2002 |pmid= 11834518 |doi=10.1161/hq0102.101551
*cite journal | author=Mead JR, Irvine SA, Ramji DP |title=Lipoprotein lipase: structure, function, regulation, and role in disease |journal=J. Mol. Med. |volume=80 |issue= 12 |pages= 753–69 |year= 2003 |pmid= 12483461 |doi= 10.1007/s00109-002-0384-9

*cite journal | author=Lichtenstein L, "et al."|title=Angptl4 up-regulates cholesterol synthesis in liver via inhibition of LPL- and HL-dependent hepatic cholesterol uptake. |journal=Arterioscler Thromb Vasc Biol. |volume=27|issue= 11 |pages= 2420-27 |year= 2007 |pmid= 17761937 |doi= 10.1161/ATVBAHA.107.151894

External links


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