Abstract
Intravenous injection of heparin releases lipase activity from tissue sites to the circulating blood (8, 20, 30, 31, 34). One major enzyme activity released is the so-called lipoprotein lipase (LPL). This enzyme is inhibited by high salt concentration, and its activity against long-chain triglycerides is greatly enhanced by a serum component (31) identified as the apolipoprotein CII (also called R-Glu or apo-LP-Glu) of the very low-density lipoproteins (9, 23, 36). Enzymes with these characteristics are present in several tissues — e.g., adipose tissue (34), skeletal and heart muscle (31), and lac- tating mammary gland (47) — and, in some species, in milk (24, 33). They probably have an important role in the metabolism of the triglyceride-rich plasma lipoproteins (42). Electron microscopic and other studies indicate that in some tissues these lipoproteins can attach to the capillary endothelium, where they are then acted on by LPL C5). The triglycerides are hydrolyzed, and fatty acids and possibly also partial glycerides are transferred into the tissue through the capillary endothelium, leaving a remnant lipoprotein, a particle that has lost most of its triglyceride. This remnant lipoprotein is further metabolized by other, less well-known systems.
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Olivecrona, T., Hernell, O., Egelrud, T. (1975). Lipoprotein Lipase. In: Bradshaw, R.A., Wessler, S. (eds) Heparin. Advances in Experimental Medicine and Biology, vol 52. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-0946-8_24
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DOI: https://doi.org/10.1007/978-1-4684-0946-8_24
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