Hormone‐sensitive lipase is responsible for the neutral cholesterol ester hydrolase activity in macrophages
- 24 April 1989
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 247 (2) , 205-208
- https://doi.org/10.1016/0014-5793(89)81335-3
Abstract
Anti-hormone-sensitive lipase (HSL) immunoglobulin selectively immunoprecipitates a single 84 kDa 32P-phosphoprotein from macrophage homogenates previously phosphorylated by cyclic AMP-dependent protein kinase in the presence of [γ-32P]ATP-Mg. This immunoglobulin also completely removes the neutral cholesterol ester hydrolase activity from macrophage homogenates. These data demonstrate that HSL is responsible for the neutral cholesterol ester hydrolase activity in macrophages and hence plays a key role in cholesterol metabolism in these cells.Keywords
This publication has 15 references indexed in Scilit:
- Phosphorylation of bovine hormone‐sensitive lipase by the AMP‐activated protein kinaseEuropean Journal of Biochemistry, 1989
- Primary structure of the site on bovine hormone‐sensitive lipase phosphorylated by cyclic AMP‐dependent protein kinaseFEBS Letters, 1988
- Development of the smooth muscle foam cell: uptake of macrophage lipid inclusions.Proceedings of the National Academy of Sciences, 1986
- Regulation of cholesterol ester hydrolase by cyclic AMP‐dependent protein kinaseFEBS Letters, 1986
- Hormone-sensitive lipase from bovine adipose tissueBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1986
- Cytosolic cholesterol ester hydrolase from bovine corpus luteumBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1983
- Properties and purification of the catalytic subunit of cyclic AMP-dependent protein kinase of adipose tissueBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1982
- Direct Evidence that Cholesterol Ester Hydrolase from Adrenal Cortex is the Same Enzyme as Hormone‐Sensitive Lipase from Adipose TissueEuropean Journal of Biochemistry, 1982
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Maturation of the head of bacteriophage T4Journal of Molecular Biology, 1973