initially high but declined as HMG-CoA reductase became activated. Glucagon prevented the loss of activity, whereas insulin promoted inactivation of the enzyme. Similar affects on the activity of HMG-CoA reductase kinase. and the state of phosphorylation of HMG-CoA reductase in liver have been reported after injection of rats with glucagon (Beg el al., 1979). Thus insulin and glucagon have conc...

Introduction: The aim of this study was to investigate the effect of aerobic training and consumption of L-carnitine supplements on HMG-CoA reductase and low density lipoprotein receptor (LDL-R) in the liver of male Wistar rats toxicated by boldenone. Materials and methods: In this clinical study, 30 male Wistar rats aged 12 weeks (weight 195±7.94g) were randomly divided into five groups: cont...

Protein phosphatase C was purified 1500-fold from rat liver by a six-step procedure including a fractionation step with 80% ethanol at room temperature and two successive chromatographic separations on DEAESephadex. This preparation restored hydrox~ethyl glutaryl-CoA (HMG-CoA) reductase activity in liver microsomes pretreated with MgATP and also inactivated HMG-CoA reductase kinase. The relativ...

Rat liver microsomal 3-hydroxy-3-methylglutaryl-CoA reductase [HMG-CoA reductase; mevalonate:NADP+ oxidoreductase (CoA-acylating), EC 1.1.1.34], the key regulatory enzyme in cholesterol biosynthesis, has been purified to apparent homogeneity. Purified HMG-CoA reductase yields a single diffuse band when NaDodSO4/polyacrylamide gels are stained with Coomassie blue and yields two adjacent bands wh...

3-Hydroxy-3-methylglutaryl CoA reductase (HMG-CoA reductase) plays a rate-limiting role in isoprenoid biosynthesis and is associated with cell proliferation and transformation. Although an elevated level of HMG-CoA reductase activity is consistently detected in cancer cell lines and tumors, the question remains whether HMG-CoA reductase activity may have a causative role in cell transformation....

The activity of microsomal 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) [mevalonate:NADP+ oxidoreductase (CoA-acylating); EC 1.1.1.34] was inhibited by ATP+Mg2+. Inactivation of HMG-CoA reductase by ATP+Mg2+ was dependent on time, temperature, and ATP concentration. Incubation of microsomal HMG-CoA reductase with [gamma-32P]ATP+Mg2+ was associated with a reciprocal increa...

The gene (hmgA) for 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase (EC 1.1.1.34) from the thermophilic archaeon Sulfolobus solfataricus P2 was cloned and sequenced. S. solfataricus HMG-CoA reductase exhibited a high degree of sequence identity (47%) to the HMG-CoA reductase of the halophilic archaeon Haloferax volcanii. Phylogenetic analyses of HMG-CoA reductase protein sequences sug...

Atherosclerotic plaque regression and HMG-CoA reductase inhibition potential of curcumin: An integrative omics in-vivo studyPriyanka Riyad, Ashok Purohit, Karishma Sen, Heera Ram

Regulation of the expression of hepatic 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase by the major end product of the biosynthetic pathway, cholesterol, and by various hormones is critical to maintaining constant serum and tissue cholesterol levels in the face of an ever-changing external environment. The ability to downregulate this enzyme provides a means to buffer the body agains...

A simple and rapid mixed-phase method for the quantitative assay of 3-hydroxy-3-methylglutaryl (HMG)CoA reductase and a procedure for the efficient reactivation of Mg-ATP-inactivated microsomal HMG-CoA reductase by potato acid phosphatase are described. The mixed-phase assay entails the direct addition of the acidified, deproteinized incubation mixture to a toluene-based scintillation fluor. Th...