Insulin-stimulated release of lipoprotein lipase by metabolism of its phosphatidylinositol anchor.
Science
; 241(4873): 1670-2, 1988 Sep 23.
Article
em En
| MEDLINE
| ID: mdl-2843987
ABSTRACT
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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Base de dados:
MEDLINE
Assunto principal:
Fosfatidilinositóis
/
Insulina
/
Lipase Lipoproteica
Idioma:
En
Ano de publicação:
1988
Tipo de documento:
Article