Publication | Closed Access
Insulin-Stimulated Release of Lipoprotein Lipase by Metabolism of Its Phosphatidylinositol Anchor
147
Citations
37
References
1988
Year
Lipoprotein LipaseMetabolic SyndromeInsulin-stimulated ReleaseLipid SynthesisLipid MetabolismBiochemistryRapid ReleaseNatural SciencesDiabetesPhosphatidylinositol AnchorLipoprotein MetabolismPlasma LipoproteinsCellular BiochemistryMetabolismMedicineCell BiologyInsulin SignalingBiomolecular Engineering
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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