Journal of Lipid Research, Vol. 11, 565-570, November 1970
Copyright © 1970 by Lipid Research, Inc.

Activation of lipoprotein lipase by lipoprotein fractions of human serum

Dennis M. Bier and Richard J. Havel

Cardiovascular Research Institute, Department of Medicine and Department of Pediatrics, University of California San Francisco, San Francisco, California 94122

Triglycerides in fat emulsions are hydrolyzed by lipoprotein lipase only when they are "activated" by serum lipoproteins. The contribution of different lipoprotein fractions to hydrolysis of triglycerides in soybean oil emulsion was assessed by determining the quantity of lipoprotein fraction required to give half-maximal hydrolysis. Most of the activator property of whole serum from normolipidemic, postabsorptive subjects was in high density lipoproteins. Low density lipoproteins and serum from which all lipoprotein classes were removed had little or no activity. Also, little activator was present in guinea pig serum or in very low density poor serum from an individual with lecithin:cholesterol acyltransferase deficiency, both of which are deficient in high density lipoproteins. Human very low density lipoproteins are potent activators and are much more active than predicted from their content of high density lipoprotein-protein. Per unit weight of protein, very low density lipoproteins had 13 times the activity of high density lipoproteins. These observations suggest that one or more of the major apoproteins of very low density lipoproteins, present as a minor constituent of high density lipoproteins, may be required for the activation process.

Supplementary key words serum lipoproteins • lecithin:cholesterol acyltransferase deficiency • guinea pig serum

Submitted on June 1, 1970
Accepted on August 12, 1970

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