Small C A, Goodacre J A, Yeaman S J
Department of Biochemistry and Genetics, University of Newcastle upon Tyne, England.
FEBS Lett. 1989 Apr 24;247(2):205-8. doi: 10.1016/0014-5793(89)81335-3.
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 [gamma-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.
抗激素敏感脂肪酶（HSL）免疫球蛋白能从巨噬细胞匀浆中选择性地免疫沉淀出一种单一的84 kDa 32P-磷蛋白，该匀浆先前在[γ-32P]ATP-镁存在的情况下经环磷酸腺苷依赖性蛋白激酶磷酸化。这种免疫球蛋白还能完全去除巨噬细胞匀浆中的中性胆固醇酯水解酶活性。这些数据表明，HSL负责巨噬细胞中的中性胆固醇酯水解酶活性，因此在这些细胞的胆固醇代谢中起关键作用。
