Activation of rat liver cholesterol ester hydrolase by cAMP-dependent protein kinase and protein kinase C |
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Authors: | Shobha Ghosh W McLean Grogan |
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Affiliation: | (1) Department of Biochemistry and Molecular Biophysics, Virginia Commonwealth University, Box 614-MCV Station, Medical College of Virginia, 23298 Richmond, Virginia |
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Abstract: | Short term regulation of hepatic cholesterol ester hydrolase by reversible phosphorylation is described. Two different kinase
systems seem to be involved in this regulation. The addition of ATP, cyclic AMP and Mg2+ to rat liver 104,000× g supernatant (S104) produced a 100–140% increase in cholesterol ester hydrolase activity. This stimulation
was abolished when protein kinase inhibitor was added prior to the addition of ATP, cyclic AMP and Mg2+. Cholesterol ester hydrolase activity was also stimulated when calcium ions, phosphatidylserine, and diolein were added to
S104 along with ATP and Mg2+. Diolein in this reaction could be substituted by phorbol 12-myristate 13-acetate. Preincubation of S104 with alkaline phosphatase
resulted in a deactivation of cholesterol ester hydrolase. The addition of increasing concentrations of Mg2+ to S104 produced increasing inhibition of cholesterol ester hydrolase activity, and this effect was blocked by NaF.
It is suggested that rat liver cholesterol ester hydrolase is activated by cyclic AMP dependent protein kinase and protein
kinase C. Deactivation is accomplished by dephosphorylation catalyzed by a phosphoprotein phosphatase, dependent on Mg2+.
This work was presented at the Twenty-Third Southeastern Regional Lipid Conference, held October 26–28, in Cashiers, North
Carolina. |
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