The regulation of cholesteryl ester metabolism by 17 beta-estradiol in macrophages. Activation of neutral cholesterol esterase.
The mechanism for antiatherogenic effects of 17 beta-estradiol (E2) was investigated in J774 A.1 cells incubated with beta-VLDL. E2 at physiological concentrations (0.25 and 2.5 nM) inhibited an accumulation of cellular cholesteryl esters and enhanced their hydrolysis in foam cells. These phenomena were preceded by activation of neutral cholesterol esterase through an increase in cyclic AMP-dependent protein kinase activity. 17 alpha-estradiol, progesterone, and testosterone lacked such stimulatory effects on neutral cholesteryl esterase.
Tomita
T
T
University of Shizuoka, Graduate School of Health Sciences, Shizuoka, Japan.
Sawamura
F
F
Uetsuka
R
R
Ikeda
M
M
Tomita
I
I
D002460:Cell Line; D002788:Cholesterol Esters / Q000378:metabolism*; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D004789:Enzyme Activation; D004958:Estradiol / Q000494:pharmacology*; D005487:Foam Cells / Q000378:metabolism; D066298:In Vitro Techniques; D008079:Lipoproteins, VLDL / Q000378:metabolism; D008264:Macrophages / Q000378:metabolism*; D011374:Progesterone / Q000494:pharmacology; D002787:Sterol Esterase / Q000378:metabolism; D013739:Testosterone / Q000494:pharmacology
D002788:Cholesterol Esters; D008079:Lipoproteins, VLDL; D013739:Testosterone; D011374:Progesterone; D004958:Estradiol; D017868:Cyclic AMP-Dependent Protein Kinases; D002787:Sterol Esterase