Abstract
Circulating lipoprotein triglyceride is cleared in extrahepatic tissues by lipoprotein lipase (LpL). The enzyme is normally attached to the capillary endothelium, but is released into the plasma by the injection of heparin. LpL has been purified and characterized from post-heparin plasma, from tissues and from milk (Augustin and Greten 1979). The characteristic feature of LpL is that it is stimulated by apolipoprotein C-II (apoC-II), a protein (Jackson et al. 1977) present in chylomicrons, very low density lipoproteins (VLDL) and high density lipoproteins (HDL). This report describes the role of apoC-II and lipid structure in the mechanism of action of bovine milk lipoprotein lipase.
This work was supported by NIH grants HL-22619, 23019 and 20882, by Training grant HL-07382 (ADC), by the American Heart Association, by the Lipid Research Clinic Program (NHLBI 72-2914), by GCRC grant RR-00068-15, and by the Muscular Dystrophy Association (JDJ).
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References
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Jackson, R.L. et al. (1980). Lipoprotein Structure and the Mechanism of Action of Lipoprotein Lipase. In: Gotto, A.M., Smith, L.C., Allen, B. (eds) Atherosclerosis V. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-6071-4_39
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DOI: https://doi.org/10.1007/978-1-4612-6071-4_39
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