June 8, 1978New England Journal of Medicine5 citations
ApoC-II Deficiency: A New Mutant
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Key Points
- To elucidate the enzymatic role of lipoprotein lipase and the mechanistic consequences of apolipoprotein C-II deficiency in triglyceride metabolism.
- Assessed lipoprotein lipase localization and release following intravenous heparin administration.
- Characterized the hydrolysis and extrahepatic catabolic pathways of chylomicrons and very-low-density lipoproteins.
- Lipoprotein lipase functions as an endothelial surface exoenzyme essential for hydrolyzing triglyceride-rich chylomicrons and VLDL.
- Apolipoprotein C-II acts as an indispensable cofactor required for activating lipoprotein lipase to clear circulating triglycerides.
Abstract
Lipoprotein lipase (LPL) has a vital role in regulating the catabolism of the triglyceride-rich lipoproteins, which are the chylomicrons and the very-low-density lipoproteins (VLDL)1; LPL catalyzes the hydrolysis of chylomicron and VLDL triglyceride — a crucial step in their extrahepatic catabolism. Since intravenous administration of heparin releases LPL and other enzymes into the plasma, LPL is thought to be an exoenzyme located on the surface of the endothelial cell. Whether LPL is transported to that site from other tissues of the body, as seems likely, or whether it is synthesized by the endothelial cells is not known. Unlike the . . .