Enzyme that catalyzes the initial step of hydrolyzing the fatty acids from the glycerol backbone.
An enzyme produced by many cells. On the surface of cells lining the vasculature, it hydrolyzes fat (chylomicrons) and very low-density lipoprotein (VLDL) to monoglycerides to free fatty acids and intermediate-density lipoprotein (IDL). This enzyme, similar to plasminogen, is an important regulator of lipid and lipoprotein metabolism. Even though the physiological functions of Lp(a) and apoprotein(a) are not fully understood, there is a positive association of plasma Lp(a) with premature myocardial infarction. Deficiency of this enzyme leads to an increase in chylomicrons and VLDLs, and to low levels of high-density lipoproteins (HDL). Diseases associated with acquired causes of decreased lipoprotein lipase include acute ethanol ingestion, diabetes mellitus, hypothyroidism, chronic renal failure, and nephrotic syndrome.
A proteinaceous catalyst which selectively separates a single fatty acid from a molecule of triglyceride.
There exists an enzyme that allows for the transportation of adipose tissue into the muscular cells where it can be oxidized to produce energy, as well as into the fat cells for storage. The enzyme in question is called lipoprotein lipase (LPL). However, it has been observed that LPL activity is decreased in muscular cells under conditions of high insulin levels, inadequate fat intake, and excessive consumption of saturated fats. Conversely, LPL activity is enhanced in adipose cells under these same conditions, resulting in an increased amount of fat storage in these cells.