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  • Title: A novel assay for cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase activity using reversed-phase ion-pair chromatography: demonstration that Lifibrol (K12.148) modulates the enzyme activity.
    Author: Scharnagl H, März W, Schliack M, Löser R, Gross W.
    Journal: J Lipid Res; 1995 Mar; 36(3):622-7. PubMed ID: 7775873.
    Abstract:
    Cytosolic HMG-CoA synthase and microsomal 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) reductase catalyze two sequential steps in the mevalonate pathway. Both enzymes are negatively regulated by cholesterol. Cytosolic HMG-CoA synthase is responsible for the generation of HMG-CoA from acetyl-CoA and acetoacetyl-CoA). We have developed a new method to determine HMG-CoA synthase activity. In this assay, HMG-CoA is formed from acetoacetyl-CoA and labeled acetyl-CoA. The HMG-CoA product is isolated from the reaction mixture by means of reversed-phase ion-pair chromatography. The recovery of the product was always greater than 90%. The average within-batch coefficient of variation for HMG-CoA synthase activity was 5.1%. Using the new assay, we demonstrate that Lifibrol (K12.148), a new hypolipidemic compound, inhibits HMG-CoA synthase. Because our assay is accurate and precise it may become useful in future studies on the regulation and the pharmacological modulation of cytosolic HMG-CoA synthase.
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