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Science 23 September 1988:
Vol. 241. no. 4873, pp. 1670 - 1672
DOI: 10.1126/science.2843987
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Articles

Science, Vol 241, Issue 4873, 1670-1672
Copyright © 1988 by American Association for the Advancement of Science

articles

Insulin-stimulated release of lipoprotein lipase by metabolism of its phosphatidylinositol anchor

BL Chan, MP Lisanti, E Rodriguez-Boulan, and AR Saltiel

Laboratory of Biochemical Endocrinology, Rockefeller University, New York, NY 10021.

Lipoprotein lipase (LPL) plays a critical role in the metabolism of plasma lipoproteins. In 3T3-L1 adipocytes, insulin elicits the rapid release of LPL through mechanisms that are independent of energy metabolism and protein synthesis. Some of the metabolic actions of insulin may be mediated by the activation of a specific phospholipase that hydrolyzes a glycosyl phosphatidylinositol (PI) molecule. The insulin-sensitive glycosyl-PI is structurally similar to the glycolipid membrane anchor of a number of proteins. LPL appears to be anchored to the 3T3-L1 cell surface by glycosyl-PI, and its rapid release by insulin may be due to activation of a glycosyl-PI-specific phospholipase C.


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