Lipoprotein lipase: an attempt to correlate its molecular properties to its function

Hydrolysis by lipoprotein lipase in capillaries of the adipose tissue is the step that determines the rate at which fatty acids from lipoprotein triacylglycerols are transported into the tissue for storage. Like many other key enzymes, adipose tissue lipoprotein lipase can be regulated both in amount and in activity. The amount of active lipoprotein lipase at the capillary endothelium is under hormonal control. The enzyme molecule itself carries several functional sites. Three of these sites, for interaction with lipid interfaces, with activator protein, and with fatty acids, regulate the action of the enzyme's active site. Another, independent, site on the molecule anchors it to cell surface heparan sulfate chains and thus holds it in place at the endothelium. Together these properties allow for a fine-tuned regulation of the lipoprotein lipase reaction so that lipids are transferred into the adipose tissue at the right rate, at the right time, and in the right place.