PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2769071-4 1989 Bile salts also suppress the activity of the rate-limiting enzyme for cholesterol synthesis, 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA-R). Cholesterol 70-81 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 93-140 2513368-0 1989 Tissue-selective acute effects of inhibitors of 3-hydroxy-3-methylglutaryl coenzyme A reductase on cholesterol biosynthesis in lens. Cholesterol 99-110 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 48-95 2769071-4 1989 Bile salts also suppress the activity of the rate-limiting enzyme for cholesterol synthesis, 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA-R). Cholesterol 70-81 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 142-151 3415662-1 1988 In rats fed on a diet containing 1% cholesterol for 24 h, the decrease in hepatic non-saponifiable lipid synthesis, cholesterogenesis and 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) reductase activity was accompanied by an increase in the proportion of newly synthesized polar sterols in vivo. Cholesterol 36-47 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 138-188 2794793-2 1989 HMG-CoA (3-hydroxy-3-methylglutaryl coenzyme A) reductase activity, regulating cholesterol biosynthesis, was unaffected by clofibrate and ciprofibrate and slightly decreased (20%) by bezafibrate. Cholesterol 79-90 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 9-57 2841097-2 1988 Cholesterol biosynthetic capacity was assessed by measuring both the activity and the content of the rate-limiting enzyme 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductase and by monitoring [14C]acetate incorporation into luteal sterols. Cholesterol 0-11 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 122-179 2903839-3 1988 The activities of HMG-CoA synthase and HMG-CoA reductase in livers of 17-day-old rat pups reared on the low-cholesterol diet were enhanced three- to five-fold over those observed in the age-matched rats in the normal cholesterol and mother-reared control groups. Cholesterol 108-119 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 39-56 2903839-3 1988 The activities of HMG-CoA synthase and HMG-CoA reductase in livers of 17-day-old rat pups reared on the low-cholesterol diet were enhanced three- to five-fold over those observed in the age-matched rats in the normal cholesterol and mother-reared control groups. Cholesterol 217-228 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 39-56 2836685-0 1987 Short-term changes in hepatic HMG-CoA reductase in rats fed diets containing cholesterol or oat bran. Cholesterol 77-88 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 30-47 3680289-2 1987 This protein activates hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (NADPH) (EC 1.1.1.34), the rate-limiting enzyme in the cholesterol biosynthetic pathway. Cholesterol 131-142 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 23-75 2836685-6 1987 Total HMGR activity was best correlated with apparent demand for cholesterol synthesis. Cholesterol 65-76 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 6-10 3593753-2 1987 The specific activity of 3-hydroxy-3-methylglutaryl CoA reductase, the rate-limiting enzyme in cholesterol biosynthesis, was depressed in hepatic microsomes of silatrane-treated animals. Cholesterol 95-106 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 25-65 3646060-1 1987 Mevinolin is a potent competitive inhibitor of HMG-CoA reductase, the enzyme catalyzing the major rate-limiting step in cholesterol synthesis. Cholesterol 120-131 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 47-64 2885178-6 1987 The activity of 3-hydroxy-3-methylglutaryl CoA reductase, the rate-limiting enzyme in cholesterol biosynthesis, decreased steadily with advancing age, and at 18 months of age, activity was only half of that in 2-month-old control rats. Cholesterol 86-97 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 16-56 3572245-4 1987 Administration of a lipoprotein bolus (20 mg of cholesterol) to rats resulted in a significant decrease in 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and a significant increase in acyl-coenzyme A:cholesterol acyltransferase activity over controls at 1 hr. Cholesterol 48-59 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 107-154 3555431-1 1987 Because the small bowel is a site of significant cholesterol synthesis, we determined the ileal distribution of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase), the rate-limiting enzyme of the cholesterol biosynthetic pathway. Cholesterol 213-224 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 112-159 3784912-6 1986 Cholesterol synthesis, as estimated by HMG-CoA reductase activity, was decreased in the liver of hypothyroid animals. Cholesterol 0-11 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 39-56 3745272-1 1986 3-Hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, a key regulatory enzyme involved in cholesterol biosynthesis, has recently been reported to be present in rat liver peroxisomes (Keller, G.A., M.C. Cholesterol 95-106 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-57 3707981-3 1986 The level of the regulatory enzyme of cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl-CoA reductase, closely follows this pattern (Hahn, P. and Walker, B. Cholesterol 38-49 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 64-104 3742535-0 1986 Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by mevalonate and cholesterol in isolated rat hepatocytes during perinatal development. Cholesterol 80-91 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 14-61 4009174-0 1985 Cholesterol biosynthesis and its regulation in dissociated cell cultures of fetal rat brain: developmental changes and the role of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Cholesterol 0-11 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 131-178 4052444-1 1985 A water-soluble derivative of cholesterol, methoxypolyoxyethylated (MPOE) cholesterol, has been synthesized and used to study the regulation of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, the key regulatory enzyme in cholesterol biosynthesis. Cholesterol 30-41 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 144-201 4052444-1 1985 A water-soluble derivative of cholesterol, methoxypolyoxyethylated (MPOE) cholesterol, has been synthesized and used to study the regulation of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, the key regulatory enzyme in cholesterol biosynthesis. Cholesterol 74-85 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 144-201 4052444-1 1985 A water-soluble derivative of cholesterol, methoxypolyoxyethylated (MPOE) cholesterol, has been synthesized and used to study the regulation of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, the key regulatory enzyme in cholesterol biosynthesis. Cholesterol 74-85 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 144-201 4056052-3 1985 We examined the hypothesis that the rate of biliary cholesterol secretion can be controlled by availability of an hepatic metabolically active free cholesterol pool whose size is determined in part by rates of sterol synthesis, as reflected by activity of the primary rate-limiting enzyme 3-hydroxy-3-methylglutaryl coenzyme A (HMG CoA) reductase and of sterol esterification, as reflected by the activity of the enzyme acyl coenzyme A/cholesterol acyltransferase (ACAT). Cholesterol 52-63 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 289-346 4056052-3 1985 We examined the hypothesis that the rate of biliary cholesterol secretion can be controlled by availability of an hepatic metabolically active free cholesterol pool whose size is determined in part by rates of sterol synthesis, as reflected by activity of the primary rate-limiting enzyme 3-hydroxy-3-methylglutaryl coenzyme A (HMG CoA) reductase and of sterol esterification, as reflected by the activity of the enzyme acyl coenzyme A/cholesterol acyltransferase (ACAT). Cholesterol 148-159 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 289-346 3883347-1 1985 The location inside rat liver parenchymal cells of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase; EC 1.1.1.34), the key regulatory enzyme in cholesterol biosynthesis, has been examined by immunoelectron microscopy and by subcellular fractionation. Cholesterol 162-173 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 51-117 3968683-0 1985 22-Hydroxycholesterol derivatives as HMG CoA reductase suppressors and serum cholesterol lowering agents. Cholesterol 10-21 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 37-54 3968683-2 1985 These agents were evaluated in vitro and in vivo for their ability to suppress HMG CoA reductase, the rate-limiting enzyme of cholesterol biosynthesis. Cholesterol 126-137 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 79-96 4029489-2 1985 The Michaelis constants for HMG-CoA reductase were determined for microsomal enzyme from the liver of normal and cholesterol-fed rats and Morris hepatoma 5123C. Cholesterol 113-124 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 28-45 3968989-7 1985 These data suggest that, in the rat, regulation of cholesterol synthesis in response to decreased total HMGR during fasting and increased levels after a meal results from alterations in the percentage of enzyme which is expressed. Cholesterol 51-62 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 104-108 6736025-0 1984 Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by oxysterol by-products of cholesterol biosynthesis. Cholesterol 90-101 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 14-61 6665743-1 1983 Mevinolin is a fungal metabolite, and in the hydroxyacid form, mevinolinic acid, it is an inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-Co A) reductase, an enzyme essential in cholesterol biosynthesis. Cholesterol 186-197 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 103-161 6707519-1 1984 The influence of membrane cholesterol content on 3-hydroxy-3-methylglutaryl CoA reductase (HMG-CoA reductase, EC 1.1.1.34) in rat liver microsomes was investigated. Cholesterol 26-37 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 91-108 6357898-2 1983 The highest activity of 3-hydroxy-3-methyl glutaryl coenzyme A reductase (HMG-CoA reductase), a key regulatory enzyme in the cholesterol pathway, was associated with highly enriched mitochondrial fractions with recovery of 62% of the total activity and was located on the inner membrane. Cholesterol 125-136 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 74-91 6888156-7 1983 Fenofibric acid is a hypolipidemic drug which inhibits 3-hydroxy-3-methyl-glutaryl coenzyme A reductase (HMGCoA reductase) activity, the limiting step of endogenous cholesterol synthesis. Cholesterol 165-176 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 105-121 6840702-0 1983 Effect of alterations in vitro and in vivo of the cholesterol content in rat liver microsomes on the activity of 3-hydroxy-3-methylglutaryl-CoA reductase. Cholesterol 50-61 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 113-153 6407300-8 1983 The changes in hepatic HMG CoAR and 7 alpha-OH activity imply that during lipid-TPN plasma free cholesterol is cleared by the liver and catabolized to bile acid. Cholesterol 96-107 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 23-31 6403680-4 1983 Activity of 3-hydroxy-3-methylglutaryl coenzyme A reductase, the rate-limiting enzyme of cholesterol synthesis, was elevated. Cholesterol 89-100 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 12-59 6300897-3 1983 Having recently demonstrated that rat liver 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase; EC 1.1.1.34), the major regulatory enzyme in cholesterol biosynthesis, undergoes in vivo phosphorylation and inactivation after a single cholesterol meal, we decided to test the hypothesis that the enzyme ACATase, important in cholesterol utilization and storage, is also subject to regulation by phosphorylation/dephosphorylation. Cholesterol 157-168 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 44-110 6300897-3 1983 Having recently demonstrated that rat liver 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase; EC 1.1.1.34), the major regulatory enzyme in cholesterol biosynthesis, undergoes in vivo phosphorylation and inactivation after a single cholesterol meal, we decided to test the hypothesis that the enzyme ACATase, important in cholesterol utilization and storage, is also subject to regulation by phosphorylation/dephosphorylation. Cholesterol 249-260 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 44-110 6300897-3 1983 Having recently demonstrated that rat liver 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase; EC 1.1.1.34), the major regulatory enzyme in cholesterol biosynthesis, undergoes in vivo phosphorylation and inactivation after a single cholesterol meal, we decided to test the hypothesis that the enzyme ACATase, important in cholesterol utilization and storage, is also subject to regulation by phosphorylation/dephosphorylation. Cholesterol 249-260 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 44-110 6840702-1 1983 3-Hydroxy-3-methylglutaryl-CoA reductase, the regulatory enzyme of cholesterol synthesis in liver, is bound to the microsomal fraction. Cholesterol 67-78 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-40 6840702-2 1983 Lipoprotein-bound cholesterol (from human serum) in vitro inhibits the microsomal bound 3-hydroxy-3-methylglutaryl-CoA reductase. Cholesterol 18-29 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 88-128 6840702-9 1983 The findings suggest that 3-hydroxy-3-methylglutaryl-CoA reductase may be "masked" by a cholesterol-mediated modification of the microsomal membrane. Cholesterol 88-99 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 26-66 7115341-9 1982 The reason why hepatomas fail to regulate 3-hydroxy-3-methylglutaryl-CoA reductase activity in response to dietary cholesterol may be a decreased membrane-enzyme interaction. Cholesterol 115-126 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 42-82 7176824-5 1982 The results appear to be consistent with the possibility that, at low phosphate levels, the biosynthesis of cholesterol is limited by some phosphate-requiring reaction(s) in the pathway after mevalonate, and at higher phosphate levels, the biosynthesis is limited by the 3-hydroxy-3-methylglutaryl coenzyme A reductase-catalyzed step. Cholesterol 108-119 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 271-318 6286363-10 1982 The enzymic activity of HMG-CoA reductase has also been shown to be modulated by cholesterol and mevalonolactone by both short-term and long-term mechanisms. Cholesterol 81-92 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 24-41 6286363-13 1982 Regulation of HMG-CoA reductase by mevalonolactone is of major importance in cellular metabolism because mevalonate serves as precursor for four separate metabolic pathways, including the formation of cholesterol, ubiquinone, dolichols, and isopentenyl tRNA. Cholesterol 201-212 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 14-31 6954516-1 1982 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. Cholesterol 174-185 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 63-80 6948302-0 1982 In vivo regulation of rat liver 3-hydroxy-3-methylglutaryl-coenzyme A reductase: immunotitration of the enzyme after short-term mevalonate or cholesterol feeding. Cholesterol 142-153 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 32-79 7042879-1 1982 We examined the effect of streptozotocin-induced diabetes on the rate-limiting enzyme in cholesterol synthesis, 3-hydroxy-3-methylglutaryl CoA reductase (EC 1.1.1.34), in liver and small intestine of rats. Cholesterol 89-100 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 112-152 6948302-1 1982 In recent studies using either a single dose of mevalonolactone administered by intragastric tube or a single meal containing 2% cholesterol, it was demonstrated that rat liver hydroxymethylglutaryl-coenzyme A reductase [mevalonate: NADP+ oxidoreductase (CoA-acylating), EC 1.1.1.34] (HMG-CoA reductase) the major regulatory enzyme in cholesterol biosynthesis, is subject to two phases of inhibition. Cholesterol 129-140 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 285-302 6948302-4 1982 The results with the technique of immunotitration of HMG-CoA reductase show that, in short-term studies conducted up to 2 hr after the administration of a single dose of mevalonolactone or up to 6 hr after a single meal of rat chow containing 2% cholesterol, the in vivo regulation of rat liver HMG-CoA reductase during the first half of the dark period does not occur by increased enzyme turnover but, instead, existing enzyme is further inactivated. Cholesterol 246-257 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 53-70 7236804-11 1981 Data from stimulation of bile acid biosynthesis under cholesterol feeding suggest that HMG-CoA reductase localized in the soluble fraction of rat liver is involved in bile acid biosynthesis. Cholesterol 54-65 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 87-104 6263029-2 1981 Most of these can be explained by an inhibition of the cholesterol synthesis at the level of the 3-hydroxy-3-methylglutaryl CoA reductase. Cholesterol 55-66 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 97-137 6113854-4 1981 Alimentary cholesterol significantly increased the activity of HMG-CoA reductase, had no effect on the rate of MVA biosynthesis from acetyl-CoA and stimulated the malonyl-CoA incorporation in to MVA in the soluble fraction. Cholesterol 11-22 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 63-80 6113854-5 1981 Starvation an alimentary cholesterol inhibited the HMG-CoA reductase activity and MVA biosynthesis from both substrates in the solubilized microsomal fraction. Cholesterol 25-36 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 51-68 6256360-2 1981 Although substantial evidence supports the conclusion that 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase is the major regulatory enzyme in cholesterol biosynthesis, the molecular events involved in the in vivo regulation of this enzyme have remained obscure. Cholesterol 151-162 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 59-116 7013551-3 1981 The hypercholesterolemia is due in part to a fourfold increase in activity of hepatic HMG-CoA reductase, the rate-limiting step in cholesterol biosyntheses. Cholesterol 9-20 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 86-103 6256737-1 1980 Although substantial evidence supports the conclusion that 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase [mevalonate:NADP+ oxidoreductase (CoA-acylating), EC 1.1.1.34] is the major regulatory enzyme in cholesterol biosynthesis, the molecular events involved in the in vivo regulation of this enzyme have remained obscure. Cholesterol 214-225 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 59-116 6249255-0 1980 3-hydroxy-3-methylglutaryl-coenzyme A reductase A comparison of the modulation in vitro by phosphorylation and dephosphorylation to modulation of enzyme activity by feeding cholesterol- or cholestryamine-supplemented diets. Cholesterol 173-184 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-47 7417482-10 1980 Perfusion of 25-hydroxycholesterol through livers isolated from animals at the circadian peak of cholesterol biosynthesis resulted in a rapid, 75-80% inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Cholesterol 23-34 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 164-211 731132-12 1978 The endogenous formation of cholesterol was increased 6 times and the HMG CoA reductase activity was increased about 20 times. Cholesterol 28-39 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 70-87 489612-2 1979 The possible role of HMG-CoA (3-hydroxy-3-methylglutaryl coenzyme A) reductase (the rate-controlling enzyme of cholesterol biosynthesis) in regulating the rate of dolichyl phosphate biosynthesis in rat liver was investigated. Cholesterol 111-122 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 30-78 687657-0 1978 On the mechanism for the regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase, of cholesterol 7alpha-hydroxylase and of acyl-coenzyme A:cholesterol acyltransferase by free cholesterol. Cholesterol 91-102 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 39-86 687657-2 1978 However, the increased hepatic cholesterogenesis that follows the injection of mevalonic acid resulted in an increase of the size of the intracellular pool of cholesterol that is in the environment of 3-hydroxy-3-methylglutaryl-coenzyme A reductase and acts as substrate for cholesterol 7alpha-hydroxylase. Cholesterol 159-170 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 201-248 190240-1 1977 In the adrenal gland of the rat, the activity of 3-hydroxy-3-methylglutaryl coenzyme A reductase, the rate-controlling enzyme of cholesterol synthesis, is shown to be regulated by cholesteerol carried in plasma lipoproteins. Cholesterol 129-140 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 49-96 856804-8 1977 The stimulation by free fatty acids of hepatic cholesterogenesis, as estimated by the activity of HMG-CoA reductase, probably is the result of stimulation by free fatty acids of secretion of triglyceride in the very low density lipoprotein, and the obligatory requirement for cholesterol as a component of the lipoprotein. Cholesterol 276-287 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 98-115 620042-2 1978 Cholesterol synthesis was evaluated by measuring 3-hydroxy-3-methylglutaryl-CoA reductase and by determining the rate of 3H-labeled sterol production from [3H]mevalonate. Cholesterol 0-11 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 49-89 190240-2 1977 When plasma cholesterol levels were lowered 90% by administration of the drug 4-aminopyrazolopyrimidine, the cholesteryl ester content of the adrenal gland declined by more than 90% and this was associated with a 150- to 200-fold increase in the activity of adrenal 3-hydroxy-3-methylglutaryl coenzyme A reductase and a 30-fold increase in cholesterol synthesis from [14C]acetate. Cholesterol 12-23 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 266-313 190240-5 1977 The current data indicate that the low rate of cholesterol synthesis normally observed in the rat adrenal gland is due to a suppression of the activity of 3-hydroxy-3-methylglutaryl coenzyme A reductase that is mediated by plasma lipoproteins. Cholesterol 47-58 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 155-202 1066664-2 1976 In the current studies, reduction of the plasma cholesterol level by 90% in rats through the administration of aminopyrazolopyrimidine was found to be associated with a 5- to 30-fold increase in the activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase [mevalonate:NADP+ oxidoreductase (CoA-acylating), EC1.1.1.34] in kidney and lung. Cholesterol 48-59 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 211-258 864330-1 1977 Two assays for the quantitative measurement of HMG-CoA reductase, the major regulatory enzyme in hepatic cholesterol biosynthesis, are described. Cholesterol 105-116 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 47-64 965392-2 1976 This paper presents evidence that earlier kinetic determinations of rat liver beta-hydroxy-beta-methylglutaryl coenzyme A (HMG-CoA) reductase, the reported rate-determining enzyme in cholesterol biogenesis, may have substantially underestimated the affinity of this enzyme for HMG-CoA. Cholesterol 183-194 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 78-141 833506-6 1977 Similar treatment of the animals with 7-ketocholesterol, a cholesterol derivative reported to repress HMG CoA reductase activity in tissue cultures, produced no appreciable difference in reductase activity or serum steroid levels in vivo. Cholesterol 44-55 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 102-119 1036900-3 1976 Feeding of cholic acid (or cholesterol) reduces the activity of both enzymes (of HMG-CoA reductase and cholesterol-7 alpha-hydroxylase, respectively). Cholesterol 27-38 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 81-98 1066664-6 1976 These data are consistent with the hypothesis that the low levels of 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity and cholesterol synthesis that are normally observed in certain nonhepatic tissues of the rat are due to an active form of feedback regulation mediated by cholesterol carried in plasma lipoproteins. Cholesterol 281-292 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 69-116 187533-1 1976 HMG CoA reductase, which catalyzes the reaction, HMG CoA + 2 NADAPH2 leads to mevalonate + CoA-SH + 2 NADP, is considered to be the rate-limiting enzyme on cholesterol biosynthetic pathway. Cholesterol 156-167 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-17 945302-12 1976 From the results it is concluded that the major bile salts are not direct regulators of hepatic cholesterol synthesis, but pure cholesterol, in the absence of bile salt or lipoprotein, is able to initiate the mechanism that represses hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase. Cholesterol 128-139 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 242-289 4715323-6 1973 A pronounced (60%) reduction of intestinal HMG CoA reductase activity was observed in rats fed cholesterol and bile acid in combination. Cholesterol 95-106 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 43-60 176160-0 1976 Inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in hepatoma tissue culture cells by pure cholesterol and several cholesterol derivatives. Cholesterol 112-123 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 14-61 176160-0 1976 Inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in hepatoma tissue culture cells by pure cholesterol and several cholesterol derivatives. Cholesterol 136-147 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 14-61 241422-0 1975 Effect of plasma lipoproteins and lecithin-cholesterol dispersions on the activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase of isolated rat hepatocytes. Cholesterol 43-54 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 86-133 241422-8 1975 Our data indicate that in normal rat hepatocytes the relative rates of efflux and influx of cholesterol may be critical to the regulation of 3-hydroxy-3-methylglutaryl-CoA reductase activity and cholesterogenesis. Cholesterol 92-103 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 141-181 33405196-5 2021 The acceleration of cholesterol metabolism via CYP46A1 and the retardation of cholesterol synthesis via HMGCR were observed in the hippocampus of rats treated with either low-dose or high-dose LPS. Cholesterol 78-89 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 104-109 33934680-1 2021 Statins are 3-hydroxy-3-methyl-glutaryl-CoA (HMG-CoA) reductase inhibitor drugs that lead to serum-cholesterol-lowering effects. Cholesterol 99-110 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 45-63 33755739-4 2021 Atorvastatin (ATV), 3-hydroxy 3-methylglutaryl co-enzyme A (HMG Co-A) reductase inhibitor, is a cholesterol-lowering statin possessing beneficial pleiotropic effects, including anti-inflammatory, antioxidant, and anti-apoptotic properties. Cholesterol 96-107 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 20-79 32414094-9 2020 Dietary betaine addition enhanced cholesterol synthesis as well as conversion of bile acid from cholesterol by increasing the levels of HMGCR and CYP7A1. Cholesterol 96-107 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 136-141 32504733-8 2020 RNA-seq and qPCR showed that triphenyltin dose-dependently down-regulated the expression of the genes for cholesterol transport and biosynthesis, including Scarb1, Ldlr, Hmgcs1, Hmgcr, and Hsd17b7. Cholesterol 106-117 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 178-183 32807146-11 2020 These cholesterol-regulating phenomenon might attribute to its effect on down-regulating the expression of lipid-related markers such as SREBP2 and HMGCR, which may exert a protective role in the NAFLD treatment. Cholesterol 6-17 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 148-153 31734306-3 2020 One of the most important regulators of cholesterol homeostasis is HMG-CoA reductase (HMG-CoAR), the rate-limiting enzyme of cholesterol biosynthesis. Cholesterol 40-51 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 67-84 31734306-3 2020 One of the most important regulators of cholesterol homeostasis is HMG-CoA reductase (HMG-CoAR), the rate-limiting enzyme of cholesterol biosynthesis. Cholesterol 40-51 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 86-94 31734306-3 2020 One of the most important regulators of cholesterol homeostasis is HMG-CoA reductase (HMG-CoAR), the rate-limiting enzyme of cholesterol biosynthesis. Cholesterol 125-136 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 67-84 31734306-3 2020 One of the most important regulators of cholesterol homeostasis is HMG-CoA reductase (HMG-CoAR), the rate-limiting enzyme of cholesterol biosynthesis. Cholesterol 125-136 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 86-94 33112815-6 2020 Moreover, PH animals showed alterations in the PPARg system, impaired mRNA levels of cholesterol receptors (Ldl-r and Srb-1) and decreased expression of the rate-limiting enzyme of de novo cholesterol production (Hmgcr). Cholesterol 189-200 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 213-218 32714018-0 2020 Inhibitory effects of tangeretin and trans-ethyl caffeate on the HMG-CoA reductase activity: Potential agents for reducing cholesterol levels. Cholesterol 123-134 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 65-82 32714018-1 2020 One of the pathways to reduce cholesterol production in the liver is through the inhibition of HMG-Coa reductase (HMGCR) by current drugs, statins. Cholesterol 30-41 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 95-112 32714018-1 2020 One of the pathways to reduce cholesterol production in the liver is through the inhibition of HMG-Coa reductase (HMGCR) by current drugs, statins. Cholesterol 30-41 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 114-119 31599939-8 2019 Among the genes upregulated by both LPS and IL-1beta were key regulatory genes involved in the cholesterol and androgen biosynthesis pathways, including Cyp17a1, Cyp11a1, Hsd3b, and Hmgcr. Cholesterol 95-106 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 182-187 32125649-6 2020 Allantoin also suppressed cholesterol biosynthesis by either inducing enzyme inhibition, occupying or blocking the putative binding site to result in non-spontaneous substrate binding, as in the cases of 3-hydroxy-methylglutaryl-coA reductase (HMGCR), mevalonate kinase (MVK) and lanosterol demethylase (LDM) where positive FEBs were reported. Cholesterol 26-37 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 204-242 32125649-6 2020 Allantoin also suppressed cholesterol biosynthesis by either inducing enzyme inhibition, occupying or blocking the putative binding site to result in non-spontaneous substrate binding, as in the cases of 3-hydroxy-methylglutaryl-coA reductase (HMGCR), mevalonate kinase (MVK) and lanosterol demethylase (LDM) where positive FEBs were reported. Cholesterol 26-37 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 244-249 32395205-1 2020 Objectives: Atorvastatin is a cholesterol-lowering agent capable of inhibiting 3-hydroxy-3-methylglutaryl coenzyme A reductase. Cholesterol 30-41 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 79-126 31278332-6 2019 In addition, IO increased plasma cholesterol concentrations, which corresponded with reduced Cyp7a1 expression and increased expression of Hmgcr, the rate-limiting enzyme in de novo cholesterol synthesis. Cholesterol 182-193 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 139-144 29446047-2 2018 SREBP-2 transgenic rats were used to investigate the transcriptional level of SREBP-2 regulated by SIRT-1/FOXO1 and the molecular mechanism of rate-limiting enzyme HMGCR that affects cholesterol synthesis. Cholesterol 183-194 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 164-169 30825513-8 2019 Furthermore, the high levels of histone acetylation (via H3K14ac and H3K27ac) and the expression of genes (Srebf2, Hmgcr, Hmgcs1) were responsible for cholesterol synthesis. Cholesterol 151-162 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 115-120 30423027-4 2019 These effects were accompanied by decreased expression of Hmgcr, Srebp-2, Cox-2 and RelA, indicating downregulation of genes involved in cholesterol synthesis and inflammation. Cholesterol 137-148 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 58-63 29600657-8 2018 These data indicated that leech may affect the expression of ACAT-2, Fas and HMGCR in liver tissue to reduce the synthesis of cholesterol and fatty acid, and promote the cholesterol transforming, then regulate lipid metabolism to decrease the levels of serum lipid, and reduce lipid accumulation in liver tissue and ease liver injury of rats, then slowing down the process of nonalcoholic fatty liver disease(NAFLD) in hyperlipidemia rats. Cholesterol 126-137 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 77-82 30284312-9 2018 In contrast, expression of 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR), involved in cholesterol synthesis, was downregulated in the liver. Cholesterol 89-100 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 27-67 30284312-9 2018 In contrast, expression of 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR), involved in cholesterol synthesis, was downregulated in the liver. Cholesterol 89-100 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 69-74 29193738-8 2018 Cholesterol synthesis regulators (Insig2, Srebp2, Hmgcr) were particularly over-expressed in muscle. Cholesterol 0-11 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 50-55 29164519-1 2018 Atorvastatin is a 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase inhibitor with cholesterol-lowering, anti-inflammatory, and antioxidant properties. Cholesterol 91-102 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 18-75 29718709-9 2018 Furthermore, analysis of PCE offspring in the uterus and in a postnatal basal/chronic stress state and the results of in vitro experiments showed that hepatic cholesterol metabolism underwent GC-dependent changes and was associated with cholesterol synthase via abnormalities in 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR) histone acetylation. Cholesterol 159-170 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 279-319 29718709-9 2018 Furthermore, analysis of PCE offspring in the uterus and in a postnatal basal/chronic stress state and the results of in vitro experiments showed that hepatic cholesterol metabolism underwent GC-dependent changes and was associated with cholesterol synthase via abnormalities in 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR) histone acetylation. Cholesterol 159-170 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 321-326 29843042-2 2018 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoAR) is a key enzyme regulating the pathway of synthesis of cholesterol whereas liver-X-receptor (LXR) regulates lipid, carbohydrate metabolism in various malignancies including mammary carcinogenesis (MC). Cholesterol 114-125 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-47 29843042-2 2018 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoAR) is a key enzyme regulating the pathway of synthesis of cholesterol whereas liver-X-receptor (LXR) regulates lipid, carbohydrate metabolism in various malignancies including mammary carcinogenesis (MC). Cholesterol 114-125 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 49-57 29340834-5 2018 We measured the impact of different DRs on the expression levels of AMPK, glucose transporters (GLUT1, GLUT3, GLUT4), and the rate-limiting enzyme in the cholesterol synthesis pathway (HMGCR). Cholesterol 154-165 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 185-190 28578430-2 2017 Using an experimental autoimmune encephalomyelitis (EAE) model of MS we revealed specific changes in the mRNA and protein expression of key molecules involved in the maintaining of cholesterol homeostasis in the rat spinal cord: 3-hydroxy-3-methylglutaryl-coenzyme-A reductase (HMGCR), apolipoprotein E (ApoE) and cholesterol 24-hydroxylase (CYP46A1) during the course of disease. Cholesterol 181-192 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 229-276 28578430-2 2017 Using an experimental autoimmune encephalomyelitis (EAE) model of MS we revealed specific changes in the mRNA and protein expression of key molecules involved in the maintaining of cholesterol homeostasis in the rat spinal cord: 3-hydroxy-3-methylglutaryl-coenzyme-A reductase (HMGCR), apolipoprotein E (ApoE) and cholesterol 24-hydroxylase (CYP46A1) during the course of disease. Cholesterol 181-192 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 278-283 27684825-6 2016 Except for the inhibition of cholesterol synthesis by inhibiting the 3-hydroxy-3-methyl glutaryl coenzyme A (HMG-COA) reductase, statins can also downregulate the phosphorylation of a series of downstream substrates including the key proteins of the Ras complex pathway, therefore may inhibit the insulin syntheses in pancreatic beta cells. Cholesterol 29-40 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 69-127 27158912-8 2016 In addition, the activity of 3-hydroxy 3-methylglutaryl coenzyme A (HMG-CoA) reductase (0.94 HMG-CoA ratio/(mevalonate) increased significantly in contrast to the activities of lipoprotein lipase (4.87 mumoles of glycerol liberated/h/L) and lecithin cholesterol acyltransferase (54.61 mumoles of cholesterol esterified/h/L) in diabetic rats. Cholesterol 250-261 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 29-86 28397043-1 2017 Simvastatin is a hypolipidemic drug that inhibits hydroxymethylglutaryl coenzyme A (HMG-CoA) reductase to control elevated cholesterol, or hypercholesterolemia. Cholesterol 123-134 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 50-102 27225895-2 2016 In comparison, 3-hydroxy-3-methylglutaryl-coenzyme A reductase inhibitors (e.g., pravastatin) inhibit production of both cholesterol and nonsterol isoprenoids. Cholesterol 121-132 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 15-62 26986474-3 2016 Rosuvastatin lowers the cholesterol levels by inhibiting the key enzyme 3-hydroxy-3-methyl-glutaryl-CoA reductase (HMG-CoA reductase) in the cholesterol producing mevalonate pathway. Cholesterol 24-35 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 115-132 26986474-3 2016 Rosuvastatin lowers the cholesterol levels by inhibiting the key enzyme 3-hydroxy-3-methyl-glutaryl-CoA reductase (HMG-CoA reductase) in the cholesterol producing mevalonate pathway. Cholesterol 141-152 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 115-132 26541177-1 2016 Simvastatin, the fourth drug selected for testing by Operation Brain Trauma Therapy (OBTT), is a 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitor used clinically to reduce serum cholesterol. Cholesterol 187-198 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 97-144 26442440-4 2015 In detail, the receptors involved in plasma lipid uptake, low density lipoprotein (LDL) receptor (LDLR) and scavenger receptor class B type 1 (SRB1), are elevated, intra-adrenal cholesterol stores are depleted, and a key enzyme in de novo cholesterol synthesis, hydroxymethylglutaryl coenzyme A reductase (HMGCR), is downregulated; particularly at mid-lactation. Cholesterol 178-189 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 262-304 26442440-4 2015 In detail, the receptors involved in plasma lipid uptake, low density lipoprotein (LDL) receptor (LDLR) and scavenger receptor class B type 1 (SRB1), are elevated, intra-adrenal cholesterol stores are depleted, and a key enzyme in de novo cholesterol synthesis, hydroxymethylglutaryl coenzyme A reductase (HMGCR), is downregulated; particularly at mid-lactation. Cholesterol 178-189 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 306-311 26007644-2 2015 Statins are the most widely prescribed cholesterol-lowering drugs with the ability to inhibit HMG-CoA (3-hydroxy-3-methylglutaryl-coenzyme A) reductase. Cholesterol 39-50 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 103-151 26375281-12 2015 The combination of cholesterol-lowering probiotics and AC possesses a therapeutic effect on NAFLD in rats by up-regulating CYP7A1, LDL-R, FXR mRNA and PPAR-alpha protein produced in the process of fat metabolism while down-regulating the expression of HMGCR, PPAR-gamma and SREBP-1c, and through normalizing the intestinal dysbiosis and improving the intestinal mucosal barrier function. Cholesterol 19-30 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 252-257 25701719-5 2015 In animals like the Sprague Dawley rat that are resistant to the serum cholesterol raising action of dietary cholesterol, regulation occurs mainly at the level of translation efficiency of hepatic HMG-CoA reductase. Cholesterol 109-120 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 197-214 25701719-8 2015 Thus, decreased transcription of enzymes occurring late in the cholesterol biosynthetic pathway appears to result in decreased translation of hepatic HMG-CoA reductase mRNA. Cholesterol 63-74 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 150-167 24505463-12 2014 The possible mechanism could be attributed to (1) the down-regulation of Hmgcr and Acat2, as well as up-regulation of Cyp7a1 and Ldlr in the liver of hyperlipidemic rats, which was involved in cholesterol biosynthesis, uptake, and efflux pathway; (2) the increase in excretion of cholesterol. Cholesterol 193-204 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 73-78 25542004-8 2014 Chronic consumption led to down-regulation of nine genes in the cholesterol biosynthesis pathway, including HMG-CoA reductase, the rate-limiting step for cholesterol synthesis. Cholesterol 64-75 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 108-125 25542004-8 2014 Chronic consumption led to down-regulation of nine genes in the cholesterol biosynthesis pathway, including HMG-CoA reductase, the rate-limiting step for cholesterol synthesis. Cholesterol 154-165 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 108-125 23147682-10 2013 Conversely, beta-carotene significantly enhanced the expression levels of genes related to cholesterol regulation, including Abca1, Abcg1, Hmgcr as well as Apoe. Cholesterol 91-102 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 139-144 19577561-7 2009 The 3-hydroxy 3-methyl glutaryl Co A (HMG-Co A) reductase activity was significantly inhibited in swertiamarin and atorvastatin treated groups compared to high cholesterol fed control group. Cholesterol 160-171 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 4-57 22274883-3 2012 Previous data demonstrated the crucial role played by 3-hydroxy 3-methylglutaryl coenzyme A reductase (HMGR), the rate-limiting enzyme of cholesterol biosynthetic pathway, in fetal rat myoblast (L6) differentiation. Cholesterol 138-149 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 54-101 22613972-10 2012 Cholesterol synthesizing enzyme HMGCoAR mRNA and protein was reduced in PMN of hypothyroid rats. Cholesterol 0-11 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 32-39 21414721-1 2011 The statins are a well-established class of drugs that lower plasma cholesterol levels by inhibiting HMG-CoA (3-hydroxy-3-methyl-glutaryl-coenzyme A) reductase. Cholesterol 68-79 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 110-159 20648556-2 2010 Here, we demonstrated that in liver cells, TSH promoted the expression of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase (HMGCR), a rate-limiting enzyme in cholesterol synthesis, by acting on the TSH receptor in hepatocyte membranes and stimulating the cyclic adenosine monophosphate / protein kinase A / cyclic adenosine monophosphate-responsive element binding protein (cAMP/PKA/CREB) signaling system. Cholesterol 158-169 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 74-122 20648556-2 2010 Here, we demonstrated that in liver cells, TSH promoted the expression of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase (HMGCR), a rate-limiting enzyme in cholesterol synthesis, by acting on the TSH receptor in hepatocyte membranes and stimulating the cyclic adenosine monophosphate / protein kinase A / cyclic adenosine monophosphate-responsive element binding protein (cAMP/PKA/CREB) signaling system. Cholesterol 158-169 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 124-129 20450981-5 2010 After sacrifice, using the quantitative real-time PCR, we assayed the transcription levels of the HMG-CoA reductase (Hmgcr) for cholesterol biosynthesis, monoacylglycerol O-acyltransferase 1 (Mogat1) as TG synthetase, hepatic triglyceride lipase (Lipc) and lipoprotein lipase (Lpl) as triglycerides (TG) reductase in the liver. Cholesterol 128-139 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 98-115 20450981-5 2010 After sacrifice, using the quantitative real-time PCR, we assayed the transcription levels of the HMG-CoA reductase (Hmgcr) for cholesterol biosynthesis, monoacylglycerol O-acyltransferase 1 (Mogat1) as TG synthetase, hepatic triglyceride lipase (Lipc) and lipoprotein lipase (Lpl) as triglycerides (TG) reductase in the liver. Cholesterol 128-139 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 117-122 22591135-1 2012 AIM: In this study, we investigated the regulatory network of the key and rate-limiting enzyme of cholesterol biosynthetic pathway, the 3-hydroxy 3-methylglutaryl coenzyme A reductase (HMGR) in different brain regions, to add new insight about lipid metabolism and physiology in the central nervous system (CNS). Cholesterol 98-109 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 136-183 23558989-1 2012 Statins reduce cholesterol levels by inhibiting 3-hydroxy-3-methylglutaryl coenzyme A reductase and have a major place in the treatment of atherosclerotic disease. Cholesterol 15-26 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 48-95 22082490-1 2011 BACKGROUND: Inhibitors of 3-hydroxy-3-methylglutaryl-coenzyme A reductase, known as statins, are commonly used as cholesterol-lowering drugs. Cholesterol 114-125 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 26-73 21906051-1 2011 PURPOSE: Statins are selective inhibitors of 3-hydroxyl-3-methyl-glutaryl coenzyme A (HMG-CoA) reductase, the rate-limiting enzyme of the mevalonate pathway for cholesterol biosynthesis. Cholesterol 161-172 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 45-104 21178122-4 2011 HMG-CoA reductase catalyzes the rate-limiting step in cholesterol biosynthesis. Cholesterol 54-65 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-17 21178122-13 2011 These results suggest that berberine regulates hepatic cholesterol biosynthesis via increased phosphorylation of HMG-CoA reductase. Cholesterol 55-66 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 113-130 20028367-5 2010 Hepatic cholesterol increases were concomitant with constantly activated sterol regulatory element-binding protein-2 (SREBP-2) in the liver and increased expression of 3-hydroxy-3-methyl-glutaryl-CoA (HMG-CoA) reductase, a rate-limiting enzyme for cholesterol de novo synthesis, indicating enhanced cholesterol biosynthesis. Cholesterol 8-19 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 168-219 20028367-5 2010 Hepatic cholesterol increases were concomitant with constantly activated sterol regulatory element-binding protein-2 (SREBP-2) in the liver and increased expression of 3-hydroxy-3-methyl-glutaryl-CoA (HMG-CoA) reductase, a rate-limiting enzyme for cholesterol de novo synthesis, indicating enhanced cholesterol biosynthesis. Cholesterol 248-259 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 168-219 20028367-5 2010 Hepatic cholesterol increases were concomitant with constantly activated sterol regulatory element-binding protein-2 (SREBP-2) in the liver and increased expression of 3-hydroxy-3-methyl-glutaryl-CoA (HMG-CoA) reductase, a rate-limiting enzyme for cholesterol de novo synthesis, indicating enhanced cholesterol biosynthesis. Cholesterol 248-259 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 168-219 19931295-6 2010 B[alpha]P-induced depletion of cholesterol in lipid rafts was linked to a reduced expression of 3-hydroxy-3-methylglutaryl-CoA reductase (HMG-CoA reductase). Cholesterol 31-42 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 138-155 19895880-4 2010 Since 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR) is the rate-limiting enzyme of the cholesterol biosynthetic pathway, it plays a pivotal role in cholesterol homeostasis maintenance. Cholesterol 96-107 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 6-53 19895880-4 2010 Since 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR) is the rate-limiting enzyme of the cholesterol biosynthetic pathway, it plays a pivotal role in cholesterol homeostasis maintenance. Cholesterol 157-168 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 6-53 19345949-1 2009 Fenofibrate, a lipid-lowering drug, inhibits hydroxyl-methylglutaryl coenzyme A (HMG-CoA)-reductase activity, thus reducing cholesterol synthesis and increasing the clearance of circulating LDL-cholesterol via the high affinity receptor system. Cholesterol 124-135 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 45-99 19345949-1 2009 Fenofibrate, a lipid-lowering drug, inhibits hydroxyl-methylglutaryl coenzyme A (HMG-CoA)-reductase activity, thus reducing cholesterol synthesis and increasing the clearance of circulating LDL-cholesterol via the high affinity receptor system. Cholesterol 194-205 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 45-99 18721740-10 2008 A cholesterol-enriched diet resulted in a significant decrease in (1) in vivo and in vitro cholesterol synthesis, (2) 3-hydroxy-3-methylglutaryl-CoA reductase gene expression, and (3) the level of liver sterol regulatory element-binding protein-2 mRNA in CRF rats. Cholesterol 2-13 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 118-158 19578821-1 2009 BACKGROUND: Simvastatin is a 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitor commonly known as a cholesterol-lowering drug with additional pleiotropic effects. Cholesterol 107-118 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 29-76 19260951-4 2009 Enzyme activities of acetyl-CoA carboxylase (ACC) and fatty acid synthase (FAS) as well as 3-hydroxy-3-methyl-glutaryl-CoA reductase (HMG-CoA-R), pace-setting steps of de novo fatty acid and cholesterol synthesis, respectively, were in situ measured in digitonin-permeabilized hepatocytes. Cholesterol 191-202 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 91-132 19627175-1 2009 Statins, the inhibitors of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, are most frequently used drugs in the prevention of coronary artery disease due to their cholesterol-lowering activity. Cholesterol 175-186 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 27-84 18603607-8 2008 Our data support that physiological differences in proteins involved in cholesterol balance are present between the sexes and, in particular, 3-hydroxy 3-methylglutaryl coenzyme A reductase shows lower activity and expression in female and 17-beta-estradiol-treated male rats than in adult untreated male. Cholesterol 72-83 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 142-189 19388010-1 2009 3-Hydroxy 3-methylglutaryl coenzyme A reductase (HMG-CoAR) is the key and rate-limiting enzyme of cholesterol biosynthetic pathway. Cholesterol 98-109 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-47 19388010-1 2009 3-Hydroxy 3-methylglutaryl coenzyme A reductase (HMG-CoAR) is the key and rate-limiting enzyme of cholesterol biosynthetic pathway. Cholesterol 98-109 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 49-57 17434618-3 2008 Chronic inhibition of nitric oxide synthase (NOS) induces arteriosclerosis, while HMG-CoA reductase inhibitors (statins) have pleiotropic vascular protective effects besides cholesterol lowering. Cholesterol 174-185 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 82-99 18035423-1 2008 Pleiotropic mechanisms beyond their cholesterol lowering effect of 3-hydroxy 3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitors or statins such as pravastatin are known. Cholesterol 36-47 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 67-124 18490854-5 2008 Inhibitors of 3-hydroxyl-3-methyglutaryl coenzyme A (HMG-CoA) reductase (i.e., statins) exert cholesterol-independent vasoprotective effects that are mediated, in part, through the activation of Akt. Cholesterol 94-105 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 14-71 16581047-8 2006 HMG-CoA reductase mRNA expression decreased significantly on cholesterol-supplemented diet feeding and on 1 ppm Se supplementation the mRNA expression further decreased. Cholesterol 61-72 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-17 16705668-4 2006 The gene expression level of HMGR, a rate-limiting enzyme for cholesterol biosynthesis, significantly increased at 3-48 h in male rats and 12-48 h in female rats. Cholesterol 62-73 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 29-33 16705668-6 2006 The present findings demonstrate that increases in gene expressions of hepatic SREBP-2 and HMGR and the amount of hepatic total cholesterol by LN occur earlier in male rats than in the females, and that increases in the gene expression level of HMGR and the amount of hepatic total cholesterol occur prior to the increase in the gene expression level of SREBP-2 in either sex of rats. Cholesterol 282-293 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 245-249 17324541-5 2007 A comparative study on hepatic mRNA expression indicated that osthol induced a significant increase in 3-hydroxy-3-methylglutaryl coenzymeA (HMG-CoA) reductase mRNA expression, which may lead to decrease in hepatic cholesterol pool through inhibition of the enzyme activity. Cholesterol 215-226 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 103-159 16814791-5 2007 It was associated with enhanced activity and mRNA abundance of liver HMG-CoA reductase, a rate-limiting enzyme for cholesterol biosynthesis. Cholesterol 115-126 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 69-86 16814791-8 2007 This is probably the cause for enhanced HMG-CoA reductase gene expression and, consequently, for increase in liver cholesterol synthesis in CRF rats. Cholesterol 115-126 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 40-57 17132207-1 2006 Statins, the widely used lipid-lowering drugs, are inhibitors of 3-hydroxy-3-methyl-glutaryl coenzyme A (HMG-CoA) reductase, which catalyses a rate-limiting step in the biosynthesis of cholesterol. Cholesterol 185-196 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 65-123 16741953-1 2006 During the ageing process in rats hypercholesterolemia occurs in concert with full activation, lowered degradation rate and an unchanged level of the rate limiting cholesterol biosynthesis enzyme, 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoAR). Cholesterol 39-50 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 197-244 16741953-1 2006 During the ageing process in rats hypercholesterolemia occurs in concert with full activation, lowered degradation rate and an unchanged level of the rate limiting cholesterol biosynthesis enzyme, 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoAR). Cholesterol 39-50 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 246-254 16476028-1 2006 3-Hydroxy-3-methylglutaryl coenzyme A reductase inhibitors (statins) are potent inhibitors of cholesterol biosynthesis. Cholesterol 94-105 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-47 16534557-2 2006 Statins, 3-Hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitors, have effects that extend beyond cholesterol reduction and inhibit vascular smooth muscle cell (VSMC) proliferation and cardiac hypertrophy. Cholesterol 111-122 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 9-66 16720944-1 2006 PURPOSE: The 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitors, or "statins", are used as cholesterol-lowering agents worldwide. Cholesterol 109-120 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 13-70 15967538-6 2005 Subsequent Northern blotting studies confirmed that the expression of p75NTR is associated with the upregulation of cholesterol biosynthetic enzymes including 3-hydroxy-3-methylglutaryl CoA reductase (HMG CoA reductase), farnesyl-diphosphate synthase, and 7-dehydro-cholesterol reductase. Cholesterol 116-127 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 159-199 15364922-3 2004 This question takes on added significance given the potential use of statins, drugs that block the rate-limiting step (3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase)) in mevalonate and cholesterol synthesis, in AD treatment. Cholesterol 206-217 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 119-166 15854590-1 2005 Recent studies suggest that 3-hydroxy-3 methylglutaryl coenzyme A (HMG-CoA) reductase inhibitors, statins, can have direct effects on blood vessels beyond their cholesterol-lowering effects. Cholesterol 161-172 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 28-85 15649292-2 2004 Expression levels of four key enzymes of cholesterol metabolism, namely 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, lanosterol 14-demethylase (CYP51), cholesterol 7alpha-hydroxylase (CYP7A1) and sterol 12alpha-hydroxylase (CYP8B1), in metabolic syndrome model rats (SHR/NDmcr-cp) were examined. Cholesterol 41-52 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 72-129 15644462-12 2005 These results suggested that hyperhomocysteinemia-induced activation of SREBP-2, CREB, and NF-Y was responsible for increased cholesterol biosynthesis by transcriptionally regulating HMG-CoA reductase expression in the liver leading to hepatic lipid accumulation and subsequently hypercholesterolemia. Cholesterol 126-137 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 183-200 15473864-2 2005 The plasma cholesterol-lowering properties of PUFA are due partly to a diminution of cholesterol synthesis and of the activity of the rate-limiting enzyme HMG-CoA reductase (3-hydroxy-3-methylglutaryl-CoA reductase). Cholesterol 11-22 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 155-172 15491682-2 2004 In the liver, cholesterol homeostasis is strictly regulated through the modulation of the 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase), the key enzyme of cholesterol biosynthesis. Cholesterol 14-25 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 90-137 15491682-2 2004 In the liver, cholesterol homeostasis is strictly regulated through the modulation of the 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase), the key enzyme of cholesterol biosynthesis. Cholesterol 177-188 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 90-137 15366788-4 2004 Policosanol is a cholesterol-lowering drug isolated from sugar cane wax that inhibits cholesterol biosynthesis through an indirect regulation of hydroxymethylglutaryl coenzyme A (HMG-CoA) reductase activity. Cholesterol 17-28 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 145-197 15821374-4 2004 The author had previously shown that the hepatic activity of beta-hydroxy-beta-methylglutaryl-CoA (HMG-CoA) reductase, the rate limiting enzyme in cholesterol biosynthesis and the incorporation of radiolabeled (1, 2 14C), acetate into hepatic free and esterified cholesterol was significantly decreased in rat treated with garlic derived organosulphur compounds. Cholesterol 147-158 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 61-117 15821374-4 2004 The author had previously shown that the hepatic activity of beta-hydroxy-beta-methylglutaryl-CoA (HMG-CoA) reductase, the rate limiting enzyme in cholesterol biosynthesis and the incorporation of radiolabeled (1, 2 14C), acetate into hepatic free and esterified cholesterol was significantly decreased in rat treated with garlic derived organosulphur compounds. Cholesterol 263-274 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 61-117 15366788-4 2004 Policosanol is a cholesterol-lowering drug isolated from sugar cane wax that inhibits cholesterol biosynthesis through an indirect regulation of hydroxymethylglutaryl coenzyme A (HMG-CoA) reductase activity. Cholesterol 86-97 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 145-197 15134389-4 2004 D-003 is a mixture of high molecular weight fatty acids isolated from sugar cane wax, which inhibits cholesterol biosynthesis through indirect regulation of HMGCoA reductase activity. Cholesterol 101-112 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 157-173 12510809-1 2003 Statins, which are inhibitors of 3-hydroxy-3-glutaryl-coenzyme A (HMG-CoA) reductase, decrease the hepatic biosynthesis of cholesterol by blocking the mevalonate pathway. Cholesterol 123-134 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 30-84 12713866-1 2003 BACKGROUND/AIMS: 3-Hydroxy-3-methylglutaryl coenzyme A reductase inhibitors called statins, have besides their cholesterol-lowering function, therapeutic value in conditions such as neo-angiogenesis and atherosclerosis. Cholesterol 111-122 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 17-64 15255637-5 2003 In cholesterol diet fed rats, as the atherogenic index and the hepatic bile acid level and the faecal excretion of bile acids and neutral sterols increased, the HMGCoA reductase and lipogenic enzyme activities in liver and lipoprotien lipase activity in heart and adipose tissue and plasma LCAT activity and the incorporation of labelled acetate into free and ester cholesterol in liver decreased significantly. Cholesterol 3-14 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 161-177 12841361-4 2003 Obtained data indicates that the increased activity of HMG-CoA reductase in the liver of rats with experimental CRF parallel enhanced mRNA level and suggests that enhanced cholesterol biosynthesis, observed in experimental CRF is at least in part due to the increased HMG-CoA reductase gene expression. Cholesterol 172-183 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 55-72 12841361-4 2003 Obtained data indicates that the increased activity of HMG-CoA reductase in the liver of rats with experimental CRF parallel enhanced mRNA level and suggests that enhanced cholesterol biosynthesis, observed in experimental CRF is at least in part due to the increased HMG-CoA reductase gene expression. Cholesterol 172-183 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 268-285 12600884-2 2003 Mevastatin is an inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, the rate-limiting step for cholesterol synthesis. Cholesterol 116-127 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 30-87 12689340-1 2003 Statins inhibit 3-hydroxy-3-methylglutaryl (HMG-CoA) reductase, the rate limiting step in cholesterol synthesis. Cholesterol 90-101 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-62 12517434-8 2003 The results suggest that cholesterol biosynthesis and esterification were concomitantly reduced by 2, as indicated by the decreased HMG-CoA reductase and ACAT activities. Cholesterol 25-36 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 132-149 12507911-10 2003 Cholesterol increments were associated with decreased SR-B1, increased ABCA1, and increased HMG CoA reductase (HMGCR) protein and its mRNA. Cholesterol 0-11 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 92-109 12507911-10 2003 Cholesterol increments were associated with decreased SR-B1, increased ABCA1, and increased HMG CoA reductase (HMGCR) protein and its mRNA. Cholesterol 0-11 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 111-116 12482628-7 2003 CONCLUSIONS: These results demonstrated that the hesperetin metabolites played as potent a role as hesperetin in plasma lipid-lowering activities in vivo, and further suggest that cholesterol biosynthesis and esterification were concomitantly reduced by hesperetin and its metabolites, as indicated by the decreased HMG-CoA reductase and ACAT activities. Cholesterol 180-191 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 316-333 12473872-1 2002 BACKGROUND: Recent studies suggest that 3-hydroxy-3-methylglutaryl co-enzyme A reductase inhibitors (statins) exert their protective effects against cardiovascular diseases independently of their cholesterol-decreasing effects. Cholesterol 196-207 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 40-88 12518023-6 2003 The results show that the apoptogenic effect of clofibrate does not depend on induction of peroxisome proliferator activated receptors (PPARs), but on interference with HMG-CoA reductase (HMGR), a key enzyme that regulates cholesterol biosynthesis and production of isoprenoid units for protein farnesylation. Cholesterol 223-234 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 169-186 12518023-6 2003 The results show that the apoptogenic effect of clofibrate does not depend on induction of peroxisome proliferator activated receptors (PPARs), but on interference with HMG-CoA reductase (HMGR), a key enzyme that regulates cholesterol biosynthesis and production of isoprenoid units for protein farnesylation. Cholesterol 223-234 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 188-192 12147302-1 2002 The anti-atherosclerosis mechanisms of 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors (statins) occur via both cholesterol-dependent and cholesterol-independent mechanisms. Cholesterol 149-160 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 39-86 12147302-1 2002 The anti-atherosclerosis mechanisms of 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors (statins) occur via both cholesterol-dependent and cholesterol-independent mechanisms. Cholesterol 123-134 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 39-86 12056585-1 2002 Treatments with high doses of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase inhibitors may induce the expression of sterol regulatory element binding protein (SREBP)-target genes, causing different effects from those attributed to the reduction of hepatic cholesterol content. Cholesterol 268-279 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 30-87 12063635-8 2002 In conclusion, the increased rate of liver cholesterol biosynthesis due to increase of HMG-CoA reductase and NADPH-producing enzyme gene expression could be one of the possible causes of hypercholesterolemia in CRF animals. Cholesterol 43-54 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 87-104 12042421-0 2002 S-alk(en)yl cysteines of garlic inhibit cholesterol synthesis by deactivating HMG-CoA reductase in cultured rat hepatocytes. Cholesterol 40-51 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 78-95 12042421-7 2002 The results suggest that S-alk(en)yl cysteines inhibit cholesterol synthesis by deactivating HMG-CoA reductase via enhanced phosphorylation, but not changing levels of mRNA or the amount of the enzyme. Cholesterol 55-66 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 93-110 10958804-9 2000 These results suggest that the reduction in liver cholesterol involves modulating the size and composition of the bile acid pool via regulation of ileal ASBT, CYP7A and HMGR mRNA levels. Cholesterol 50-61 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 169-173 11323196-5 2001 Major effects were evident in the cholesterol biosynthesis pathway including the induction of enzymes upstream and downstream of the target enzyme HMG CoA reductase. Cholesterol 34-45 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 147-164 11179461-1 2001 3-Hydroxy-3-methylglutaryl coenzyme A reductase inhibitors (statins) may exert pleiotropic effects on vascular cells independent of lowering plasma cholesterol. Cholesterol 148-159 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-47 11171976-3 2001 The high level of SREBP-1c mRNA is abolished when cholesterol synthesis is blocked by compactin, an inhibitor of 3-hydroxy-3-methylglutaryl CoA (HMG CoA) reductase that inhibits cholesterol synthesis. Cholesterol 50-61 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 113-163 11171976-3 2001 The high level of SREBP-1c mRNA is abolished when cholesterol synthesis is blocked by compactin, an inhibitor of 3-hydroxy-3-methylglutaryl CoA (HMG CoA) reductase that inhibits cholesterol synthesis. Cholesterol 178-189 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 113-163 12507226-2 2002 3-Hydroxy-3-methylglutaryl CoA (HMG-CoA) reductase, the rate-limiting enzyme for this pathway, is down regulated by feedback mechanisms due to increased levels of cholesterol and its premetabolites. Cholesterol 163-174 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-50 10912772-1 2000 Recent studies suggest that some of the beneficial effects of 3-hydroxyl-3-methylglutaryl (HMG)-CoA reductase inhibitors such as pravastatin may be through their cholesterol-lowering independent effects on the blood vessels. Cholesterol 162-173 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 62-109 10946069-1 2000 OBJECTIVES: HMG CoA reductase inhibitors reduce cellular availability of mevalonate, a precursor in cholesterol synthesis. Cholesterol 100-111 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 12-29 10946069-2 2000 Since the cholesterol content of cell membranes is an important determinant of Na(+)-K(+) pump function we speculated that treatment with HMG CoA reductase inhibitors affects Na(+)-K(+) pump activity. Cholesterol 10-21 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 138-155 10401660-1 1999 The cholesterol lowering drug lovastatin, a competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, blocks DNA synthesis and proliferation of thyrotropin (TSH) primed FRTL-5 rat thyroid cells. Cholesterol 4-15 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 69-126 10884284-0 2000 Diurnal and dietary-induced changes in cholesterol synthesis correlate with levels of mRNA for HMG-CoA reductase. Cholesterol 39-50 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 95-112 10884284-9 2000 This suggests that diurnal variation of hepatic cholesterol synthesis is driven primarily by varying the steady-state mRNA levels for HMG-CoA reductase. Cholesterol 48-59 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 134-151 10892724-1 2000 Lovastatin is a lipid lowering agent that acts by inhibiting 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, a key regulatory enzyme in cholesterol biosynthesis. Cholesterol 147-158 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 61-118 10753223-2 2000 Uptake of serum low density lipoprotein cholesterol by tissues leads to down-regulation of 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) reductase, the rate limiting enzyme in cholesterol biosynthesis that catalyzes the formation of mevalonate. Cholesterol 40-51 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 91-141 10743676-1 2000 3-Hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitors decrease mevalonate and subsequently cholesterol synthesis competitively. Cholesterol 106-117 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-57 10673069-2 2000 Lovastatin is a 3-hydroxy-3-methylglutaryl CoA reductase inhibitor that inhibits cholesterol biosynthesis and affects the activity of some signal transduction pathways and liver transcription factors. Cholesterol 81-92 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 16-56 10347124-7 1999 Assessment of the activity of intracellular key enzymes for cholesterol homeostasis in these rats disclosed a reduction in 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase (66%, P <.005) and cholesterol 7alpha-hydroxylase (58%, P <.0004) with an increment of acyl-CoA: cholesterol acyltransferase (62%, P <.002). Cholesterol 60-71 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 123-180 10642751-3 2000 The adaptive response of myelinating SC to cholesterol depletion includes cell hypertrophy, the formation of tubular invaginations of proliferating nuclear membranes giving rise to peculiar nuclear inclusions termed crystalloids, and, at the cytoplasmic level, the formation of lamellar bodies of rough ER, proliferation of the smooth ER, and overexpression of HMG CoA reductase and synthase mRNAs. Cholesterol 43-54 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 361-378 10591666-1 1999 Simvastatin, a 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitor, has been shown to lower serum cholesterol levels and normalize endothelial cell function. Cholesterol 114-125 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 15-72 10431389-1 1999 The activities of 3-hydroxy-3-methylglutaryl CoA reductase (HMGCoA reductase; EC 1.1.1.34), rate-limiting enzyme of cholesterol biosynthesis, and cholesterol 7 alpha-hydroxylase (EC 1.14.13.17), key enzyme of the neutral bile acid synthesis pathway, were measured in the microsomal fraction of rat liver and in rat liver cells to investigate the coordinate regulation of the two pathways. Cholesterol 116-127 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 18-58 10431389-1 1999 The activities of 3-hydroxy-3-methylglutaryl CoA reductase (HMGCoA reductase; EC 1.1.1.34), rate-limiting enzyme of cholesterol biosynthesis, and cholesterol 7 alpha-hydroxylase (EC 1.14.13.17), key enzyme of the neutral bile acid synthesis pathway, were measured in the microsomal fraction of rat liver and in rat liver cells to investigate the coordinate regulation of the two pathways. Cholesterol 116-127 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 60-76 10431389-3 1999 Cholesterol-feeding decreased the activity of HMGCoA reductase, increased that of cholesterol 7 alpha-hydroxylase, and concomitantly increased free cholesterol in microsomes. Cholesterol 0-11 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 46-62 10431389-4 1999 In an ex vivo setting using primary hepatocytes from animals fed a high cholesterol diet the activity of HMGCoA reductase was initially low and that of cholesterol 7 alpha-hydroxylase was elevated. Cholesterol 72-83 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 105-121 10431389-5 1999 Release of cholesterol into the medium with ongoing incubation caused HMGCoA reductase activity to increase, and that of cholesterol 7 alpha-hydroxylase to decline. Cholesterol 11-22 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 70-86 10431389-7 1999 The results confirm the idea of a joint regulation of the two key enzymes of cholesterol metabolism in response to the levels of substrate and metabolites, and support the notion that with respect to bile acid and cholesterol levels, respectively, regulation of HMGCoA reductase activity may be secondary to that of cholesterol 7 alpha-hydroxylase. Cholesterol 77-88 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 262-278 10431389-7 1999 The results confirm the idea of a joint regulation of the two key enzymes of cholesterol metabolism in response to the levels of substrate and metabolites, and support the notion that with respect to bile acid and cholesterol levels, respectively, regulation of HMGCoA reductase activity may be secondary to that of cholesterol 7 alpha-hydroxylase. Cholesterol 214-225 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 262-278 9637742-0 1998 Dietary cholesterol regulates hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase gene expression in rats primarily at the level of translation. Cholesterol 8-19 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 38-85 10191291-3 1999 Furthermore, we show that message levels and enzyme activity of rat liver phosphomevalonate kinase are regulated in response to dietary sterol levels and that this regulation is coordinate with 3-hydroxy-3-methylglutaryl coenzyme A reductase, the rate-limiting enzyme of cholesterol biosynthesis. Cholesterol 271-282 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 194-241 9891909-1 1998 NK-104 is a novel potent inhibitor of the rate-limiting enzyme in cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, and has been shown to be a highly effective agent in lowering blood cholesterol. Cholesterol 66-77 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 92-149 9681444-2 1998 We found that, during development of the rat sciatic nerve, expression of mRNA for hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase, the rate-limiting enzyme in cholesterol biosynthesis, was up-regulated in parallel with mRNA for P0, the major structural protein of PNS myelin, and with ceramide galactosyltransferase (CGT), the rate-limiting enzyme in cerebroside biosynthesis. Cholesterol 165-176 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 83-135 9667239-8 1998 Hydroxymethyl glutaryl coenzyme A (HMG-CoA) reductase activity in the liver increased 2.2-fold with BM and declined 95% after adding cholesterol, but did not change in the brain. Cholesterol 133-144 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-53 10204089-2 1999 Toxicological evaluation was performed in serum samples following the administration of the therapeutic dose regimens of the compounds that were previously shown to be effective in inhibition of 3-hydroxy-methylglutaryl coenzyme A (HMG CoA) reductase, the enzyme controlling the rate-limiting step in the synthesis of cholesterol, and acyl-CoA cholesterol acyl transferase (ACAT) which converts intracellular free cholesterol to cholesterol ester. Cholesterol 318-329 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 195-250 10204089-2 1999 Toxicological evaluation was performed in serum samples following the administration of the therapeutic dose regimens of the compounds that were previously shown to be effective in inhibition of 3-hydroxy-methylglutaryl coenzyme A (HMG CoA) reductase, the enzyme controlling the rate-limiting step in the synthesis of cholesterol, and acyl-CoA cholesterol acyl transferase (ACAT) which converts intracellular free cholesterol to cholesterol ester. Cholesterol 344-355 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 195-250 18472903-3 1999 The effects of these agnets on cytoplasmic ATP-dependent citrate lyase, acetyl CoA synthetase and HMG-CoA reductase activities were reduced by a magnitude to explain the reduction of serum cholesterol levels afforded by the compounds. Cholesterol 189-200 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 98-115 9726984-9 1998 Because activated AMPK phosphorylates and inactivates 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) reductase (EC 1.1.1.88), the rate-limiting enzyme in cholesterol synthesis, the strong inhibition of hepatocytic cholesterol synthesis by all three nucleosides confirmed their ability to activate AMPK under the conditions used. Cholesterol 148-159 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 54-104 9726984-9 1998 Because activated AMPK phosphorylates and inactivates 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) reductase (EC 1.1.1.88), the rate-limiting enzyme in cholesterol synthesis, the strong inhibition of hepatocytic cholesterol synthesis by all three nucleosides confirmed their ability to activate AMPK under the conditions used. Cholesterol 208-219 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 54-104 9637742-8 1998 The possibility that dietary cholesterol might act by increasing the rate of turnover of HMG-CoA reductase protein was examined by determining the half-life of the enzyme in livers from rats consuming chow or chow supplemented with 2% cholesterol. Cholesterol 29-40 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 89-106 9637742-8 1998 The possibility that dietary cholesterol might act by increasing the rate of turnover of HMG-CoA reductase protein was examined by determining the half-life of the enzyme in livers from rats consuming chow or chow supplemented with 2% cholesterol. Cholesterol 235-246 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 89-106 9637742-13 1998 These results indicate that cholesterol regulates hepatic HMG-CoA reductase gene expression in rats primarily at the level of translation. Cholesterol 28-39 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 58-75 9307936-7 1997 Liver 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) reductase activity was very low (22 pmol/min/mg protein), owing to cholesterol supplementation, in control rats or in rats fed PHGG, whereas it was markedly higher (+463%) in rats fed GUAR. Cholesterol 114-125 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 6-56 9145201-5 1997 The hydroxymethylglutaryl-CoA (HMG-CoA) reductase (rate-limiting enzyme of cholesterol synthesis) activity of peroxisomes and microsomes was greatly increased by in vivo treatment with gemfibrozil, but was decreased by addition of the agent to the assay mixture of the enzyme. Cholesterol 75-86 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 4-49 9210653-1 1997 The possibility that potent inhibitors of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase may alter the mechanisms by which dietary cholesterol and farnesol regulate this gene was investigated by comparing the regulatory responses of rats maintained on diets with or without 0.04% Lovastatin supplementation to dietary cholesterol. Cholesterol 142-153 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 42-99 9210653-1 1997 The possibility that potent inhibitors of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase may alter the mechanisms by which dietary cholesterol and farnesol regulate this gene was investigated by comparing the regulatory responses of rats maintained on diets with or without 0.04% Lovastatin supplementation to dietary cholesterol. Cholesterol 329-340 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 42-99 9221829-1 1997 In previous studies, inhibition of cholesterol synthesis by HMG CoA reductase inhibitors (HMGRI) was associated with myotoxicity in cultures of neonatal rat skeletal myotubes, and rhabdomyolysis in rats, rabbits, and humans in vivo. Cholesterol 35-46 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 60-77 9049604-1 1997 Crilvastatin, a new drug from the pyrrolidone family, has been previously shown to inhibit the activity of 3-hydroxy-3-methylglutaryl coenzyme A reductase, in vitro and in vivo, to reduce the absorption of dietary cholesterol and to stimulate the activity of cholesterol 7 alpha-hydroxylase in the rat. Cholesterol 214-225 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 107-154 9125163-0 1997 Translational regulation of hepatic HMG-CoA reductase by dietary cholesterol. Cholesterol 65-76 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 36-53 9125163-3 1997 Northern blotting analysis of the individual fractions revealed that cholesterol feeding reduced the portion of HMG-CoA reductase mRNA associated with translationally active polysomes by over 50% and progressively increased the percentage of reductase mRNA present in the monosomal fractions. Cholesterol 69-80 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 112-129 9125163-5 1997 These findings indicate that dietary cholesterol exerts significant feedback regulation on hepatic HMG-CoA reductase at the translational level. Cholesterol 37-48 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 99-116 9629862-6 1997 Tocotrienols are known to inhibit 3-hydroxy, 3-methyl, glutaryl CoA (HMG-COA) reductase (rate limiting enzyme in cholesterol biosynthesis), resulting in hypocholesterolemia. Cholesterol 113-124 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 69-87 8690416-8 1996 In BM 15.766-treated rats, the first and last two enzymatic reactions in the cholesterol biosynthetic pathway catalyzed by 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, lathosterol 5-dehydrogenase, and 7-dehydrocholesterol delta 7-reductase are down-regulated by cholesterol. Cholesterol 77-88 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 123-180 8690416-8 1996 In BM 15.766-treated rats, the first and last two enzymatic reactions in the cholesterol biosynthetic pathway catalyzed by 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, lathosterol 5-dehydrogenase, and 7-dehydrocholesterol delta 7-reductase are down-regulated by cholesterol. Cholesterol 224-235 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 123-180 8764882-8 1996 Cholesterol and triglyceride lowering effects of the agents were correlated with inhibition of the activities of liver acetyl CoA synthetase, HMG CoA reductase, phosphatidylate phosphohydrolase, and lipoprotein lipase, and with elevation of the activity of cholesterol ester hydrolase. Cholesterol 0-11 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 142-159 8683337-2 1996 The key regulatory enzymes in cholesterol and bile acid metabolism, 3-hydroxy-3-methylglutaryl-CoA reductase (HMG-CoA reductase) and cholesterol 7alpha-hydroxylase, were determined. Cholesterol 30-41 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 68-108 8683337-2 1996 The key regulatory enzymes in cholesterol and bile acid metabolism, 3-hydroxy-3-methylglutaryl-CoA reductase (HMG-CoA reductase) and cholesterol 7alpha-hydroxylase, were determined. Cholesterol 30-41 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 110-127 17180086-1 1996 Lovastatin is a very specific and potent inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, which regulates a rate-limiting step in the cellular synthesis of isoprenoid and cholesterol. Cholesterol 194-205 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 54-111 8673732-3 1996 For example, CuZn superoxide dismutase incubated with rat hepatocyte cells in culture inhibits 3-hydroxy-3methylglutaryl CoA reductase, thereby reducing cholesterol synthesis. Cholesterol 153-164 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 95-134 8855081-0 1996 Cholesterol synthesis in the rat brain in course of late development as determined by 3-hydroxy-3-methylglutaryl CoA reductase activity. Cholesterol 0-11 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 86-126 8884563-4 1996 Extremely reduced activities of HMG-CoA reductase, the rate-controlling enzyme for cholesterol biosynthesis, caused by deficient HMG-CoA reductase mRNA is responsible and is the suspected inherited abnormality. Cholesterol 83-94 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 32-49 8884563-4 1996 Extremely reduced activities of HMG-CoA reductase, the rate-controlling enzyme for cholesterol biosynthesis, caused by deficient HMG-CoA reductase mRNA is responsible and is the suspected inherited abnormality. Cholesterol 83-94 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 129-146 7557099-6 1995 In inhibitor-treated rats, feeding cholesterol increased plasma cholesterol concentrations 3.7 times, decreased 7-dehydrocholesterol concentrations 88%, and reduced elevated HMG-CoA reductase activity and messenger RNA levels 74% and 49%. Cholesterol 35-46 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 174-191 7557099-10 1995 CONCLUSIONS: Cholesterol is essential to correct abnormal cholesterol synthesis induced by BM 15.766 in rats by expanding the pool and inhibiting HMG-CoA reductase. Cholesterol 13-24 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 146-163 7811749-10 1995 Although hepatic HMG-CoA reductase was induced almost the same fold in both animals at 50 mg/kg, the induced HMG-CoA reductase activity in rats might overcome the inhibitory capability of pravastatin, resulting in an increase of net cholesterol synthesis, but not in rabbits. Cholesterol 233-244 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 109-126 7585458-1 1995 3-Hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase), is a rate-limiting enzyme in the biosynthesis of not only cholesterol but also a variety of non-sterol isoprenoids. Cholesterol 127-138 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-47 7585458-1 1995 3-Hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase), is a rate-limiting enzyme in the biosynthesis of not only cholesterol but also a variety of non-sterol isoprenoids. Cholesterol 127-138 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 49-66 7666787-5 1995 The hypercholesterolemic effect of soy protein was characterized by a higher cholesterol content in low-density lipoprotein (LDL) and high-density lipoprotein 1 (HDL1) fractions, together with a marked induction of hepatic hydroxymethyl glutaryl coenzyme A (HMG CoA) reductase activity and to a lesser extent cholesterol 7 alpha-hydroxylase. Cholesterol 9-20 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 223-276 7641024-2 1995 Interference with the cholesterol biosynthetic pathway with a 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitor (e.g., lovastatin) may preferentially slow malignant cell growth and offer a new approach to cancer chemotherapy. Cholesterol 22-33 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 62-109 7609606-3 1995 The microsomal activity of 3-hydroxy-3-methylglutaryl coenzyme A reductase, regulating cholesterol biosynthesis, decreased from 577 +/- 46 (SEM) to 367 +/- 38 pmol/min/mg protein compared to the controls. Cholesterol 87-98 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 27-74 7698284-0 1995 Inhibition of cholesterol synthesis ex vivo and in vivo by fluvastatin, a new inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Cholesterol 14-25 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 91-138 7544784-1 1995 PURPOSE: To determine the principle site (epithelium or superficial cortex) of gene transcription and mRNA translation for the regulatory enzyme of lens cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR). Cholesterol 153-164 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 179-226 7911291-8 1994 Feeding cholesterol eliminated the zaragozic acid A-induced increase in HMG-CoA reductase mRNA levels. Cholesterol 8-19 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 72-89 7974251-1 1994 Mevalonic acid is a product of the enzyme HMG-CoA reductase which is essential for cholesterol biosynthesis. Cholesterol 83-94 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 42-59 7958569-1 1994 The HMG-CoA reductase inhibitors are a new and novel class of cholesterol-lowering agents which are widely used worldwide. Cholesterol 62-73 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 4-21 8028508-1 1994 We correlated the activity of the rate-limiting enzyme of cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, with the sterol content and composition of mucosal cells from the ileum of three homozygous sitosterolemic subjects and one control subject. Cholesterol 58-69 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 84-141 7911291-10 1994 The increase in HMG-CoA reductase gene expression was closely related to the degree of inhibition of cholesterol synthesis caused by zaragozic acid A. Cholesterol 101-112 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 16-33 8393338-9 1993 The activity of HMG CoA reductase, the rate limiting enzyme in cholesterol biosynthesis decreased about 70% between 5 and 18 months and fell slightly further as the rats aged to 27 months. Cholesterol 63-74 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 16-33 8159102-3 1994 These increases in HMG CoA reductase protein mass are of a magnitude similar to the previously observed increases in either HMG CoA reductase activity and/or cholesterol synthesis in the small intestine of diabetic animals. Cholesterol 158-169 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 19-36 8399341-7 1993 Cholesterol synthesis as measured with 3H2O or as indicated by 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase activity or the ratio of plasma lathosterol to cholesterol was effectively downregulated by dietary cholesterol (1% w/w) in all three strains. Cholesterol 0-11 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 63-120 8399341-7 1993 Cholesterol synthesis as measured with 3H2O or as indicated by 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase activity or the ratio of plasma lathosterol to cholesterol was effectively downregulated by dietary cholesterol (1% w/w) in all three strains. Cholesterol 221-232 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 63-120 7693842-9 1993 The latter finding is interesting in view of recent reports that dietary cholesterol also seems to down-regulate HMG-CoA reductase predominantly by a post-transcriptional mechanism. Cholesterol 73-84 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 113-130 8218098-8 1993 3-Thiadicarboxylic acid treatment suppressed the activity of the rate-limiting enzyme in cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl-coenzyme A reductase, by 58%, whereas hepatic LDL receptor expression was unaltered. Cholesterol 89-100 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 115-162 8258956-4 1993 Studies involved measurements of specific activities of four enzymes participating in the maintenance of hepatic cholesterol metabolism: HMG-CoA-reductase, the rate limiting enzyme of cholesterol synthesis; cholesterol 7 alpha-hydroxylase, the rate limiting enzyme in bile acid synthesis; acyl CoA: cholesterol acyltransferase, the enzyme responsible for esterification of cholesterol; and cholesterol ester hydrolase (CEH), an enzyme which hydrolyzes cholesterol. Cholesterol 113-124 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 137-154 8258956-4 1993 Studies involved measurements of specific activities of four enzymes participating in the maintenance of hepatic cholesterol metabolism: HMG-CoA-reductase, the rate limiting enzyme of cholesterol synthesis; cholesterol 7 alpha-hydroxylase, the rate limiting enzyme in bile acid synthesis; acyl CoA: cholesterol acyltransferase, the enzyme responsible for esterification of cholesterol; and cholesterol ester hydrolase (CEH), an enzyme which hydrolyzes cholesterol. Cholesterol 184-195 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 137-154 8258956-4 1993 Studies involved measurements of specific activities of four enzymes participating in the maintenance of hepatic cholesterol metabolism: HMG-CoA-reductase, the rate limiting enzyme of cholesterol synthesis; cholesterol 7 alpha-hydroxylase, the rate limiting enzyme in bile acid synthesis; acyl CoA: cholesterol acyltransferase, the enzyme responsible for esterification of cholesterol; and cholesterol ester hydrolase (CEH), an enzyme which hydrolyzes cholesterol. Cholesterol 184-195 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 137-154 8258956-4 1993 Studies involved measurements of specific activities of four enzymes participating in the maintenance of hepatic cholesterol metabolism: HMG-CoA-reductase, the rate limiting enzyme of cholesterol synthesis; cholesterol 7 alpha-hydroxylase, the rate limiting enzyme in bile acid synthesis; acyl CoA: cholesterol acyltransferase, the enzyme responsible for esterification of cholesterol; and cholesterol ester hydrolase (CEH), an enzyme which hydrolyzes cholesterol. Cholesterol 184-195 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 137-154 8325896-4 1993 Inhibition of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, the rate-limiting enzyme in isoprenoid and sterol biosynthesis, by the cholesterol-lowering drug, lovastatin, blocks Fc epsilon RI-dependent [3H] serotonin ([3H]5HT) release from the mast cell line, RBL-2H3. Cholesterol 144-155 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 14-71 1474430-7 1992 Our results also provide suggestive evidence that the mechanism responsible for the elevation of plasma cholesterol following intraperitoneal injection of a poloxamer 407 solution (30% w/w) to rats may be due to stimulation of 3-hydroxy-3-methylglutaryl-co-enzyme A (HMG-CoA) reductase activity in the liver by the poloxamer vehicle. Cholesterol 104-115 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 227-285 8446927-1 1993 3-Hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase (EC 1.1.1.34) is the rate limiting step in the mevalonate pathway that produces isoprenoids and cholesterol. Cholesterol 154-165 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-57 1385253-5 1992 All three bile acids also suppressed activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (rate-limiting for cholesterol synthesis). Cholesterol 116-127 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 49-96 8466946-10 1993 The activity of acyl-CoA:cholesterol acyltransferase (ACAT) was reduced by the two hypocholesterolemic analogues, in contrast to the rate-limiting enzyme in cholesterol biosynthesis, HMG-CoA reductase, which tended to increase. Cholesterol 25-36 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 183-200 8434028-2 1993 The Na salt of RG 12561 (RG 12561-Na) is a potent inhibitor of 3-hydroxy-3-methyl-glutaryl-coenzyme A (HMG-CoA) reductase, the rate-limiting enzyme in the cholesterol biosynthetic pathway. Cholesterol 155-166 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 63-121 1514609-7 1992 The elevated HMG-CoA reductase activity in obese rats results from the lower liver microsomal free cholesterol content. Cholesterol 99-110 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 13-30 1483925-1 1992 3-Hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase inhibitor is known to have an inhibitory effect on cell growth in addition to a cholesterol-lowering effect. Cholesterol 138-149 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-57 1297647-12 1992 Two genes whose mRNAs and protein products accumulate according to a strong circadian rhythm with a phase compatible with regulation by DBP encode enzymes with key functions in cholesterol metabolism: HMG-coA reductase is the rate-limiting enzyme in cholesterol synthesis; cholesterol 7-alpha hydroxylase performs the rate-limiting step in the conversion of cholesterol to bile acid. Cholesterol 177-188 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 201-218 1431598-1 1992 We investigated the effects of cholesterol, cholestyramine, and taurocholate feeding on steady state specific activities and mRNA levels of hepatic 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase and cholesterol 7 alpha-hydroxylase in the rat. Cholesterol 31-42 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 140-194 1619360-4 1992 Inhibition of cholesterol synthesis with a bolus dose of mevinolin (lovastatin) a competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, profoundly decreases the specific activity of cholesterol 7 alpha-hydroxylase and rate of bile acid synthesis in rats with complete biliary diversion. Cholesterol 14-25 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 107-164 1544932-8 1992 Changes in 7 alpha-hydroxylase activity were always accompanied by parallel changes in mRNA, whereas mRNA levels for 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase were reduced by 50% or less, even when cholesterol synthesis was suppressed by 98%. Cholesterol 214-225 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 117-174 1297647-12 1992 Two genes whose mRNAs and protein products accumulate according to a strong circadian rhythm with a phase compatible with regulation by DBP encode enzymes with key functions in cholesterol metabolism: HMG-coA reductase is the rate-limiting enzyme in cholesterol synthesis; cholesterol 7-alpha hydroxylase performs the rate-limiting step in the conversion of cholesterol to bile acid. Cholesterol 250-261 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 201-218 1297647-12 1992 Two genes whose mRNAs and protein products accumulate according to a strong circadian rhythm with a phase compatible with regulation by DBP encode enzymes with key functions in cholesterol metabolism: HMG-coA reductase is the rate-limiting enzyme in cholesterol synthesis; cholesterol 7-alpha hydroxylase performs the rate-limiting step in the conversion of cholesterol to bile acid. Cholesterol 250-261 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 201-218 1915674-1 1991 The effects of long-term dosing with inhibitors of 3-hydroxy-3-methyl-glutaryl coenzyme A (HMG-CoA) reductase on the rate of cholesterol biosynthesis were examined in the lens and liver of rats and hamsters. Cholesterol 125-136 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 51-109 1940906-3 1991 This tissue specificity was further explored by examining, in various tissues, gene expression and enzyme activity of 3-hydroxy-3-methylglutaryl-CoA reductase, the rate-limiting enzyme in cholesterol biosynthesis. Cholesterol 188-199 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 118-158 1805095-3 1991 Cholesterol feeding reduced beta-hydroxy-beta-methylglutaryl (HMG)-CoA reductase (72%) and cholesteryl ester hydrolase (48%) and increased acyl-CoA:cholesterol acyltransferase (184%), whereas ODS and progesterone reversed these compensatory responses in cholesterol-fed rats. Cholesterol 0-11 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 28-80 1765816-1 1991 Previous studies from this laboratory have demonstrated that 20% rather than 5% (wt/wt) safflower oil or addition of 5% (wt/wt) cholestyramine to the diet of pregnant rats leads to an increase in the activity of 3-hydroxy-3-methylglutaryl CoA reductase, the rate-limiting enzyme of cholesterol synthesis, in the fetal liver. Cholesterol 282-293 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 212-252 1776669-1 1991 A rapid, easy, and sensitive method is described in this paper for the assay of 3-hydroxy-3-methylglutaryl CoA (HMG CoA) reductase, a key enzyme in cholesterol biosynthesis. Cholesterol 148-159 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 80-130 2247048-9 1990 It is concluded that the hypocholesterolemic action of the compound rested entirely on the inhibition of cholesterol biosynthesis in vivo by inactivation of the rate-limiting enzyme HMGCoA reductase. Cholesterol 29-40 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 182-198 1895886-12 1991 The effect on serum cholesterol may be partly due to inhibition of HMG-CoA reductase. Cholesterol 20-31 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 67-84 2044640-2 1991 The activities of the three key enzymes involved in cholesterol metabolism [3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, cholesterol 7 alpha-hydroxylase, and acyl-coenzyme A: cholesterol acyltransferase (ACAT)] were suppressed by bezafibrate treatment in rats, but only the ACAT activity was significantly decreased when the activity was related to total liver weight. Cholesterol 52-63 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 76-133 2090709-12 1990 A corresponding infusion of cholesterol-enriched Intralipid led to inhibition of HMG-CoA reductase without effect on cholesterol 7 alpha-hydroxylase activity. Cholesterol 28-39 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 81-98 2090709-16 1990 The stimulatory effect of cholestyramine on HMG-CoA reductase also in lymph fistula rats shows that the previously demonstrated suppressive effect of bile acids on HMG-CoA reductase is not only due to the effect of bile acids on intestinal absorption of cholesterol. Cholesterol 254-265 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 44-61 2380640-5 1990 Cholesterol synthesis was elevated about twofold in the livers of rats treated with ethionine as was the activity of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, its rate limiting enzyme. Cholesterol 0-11 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 117-174 2351103-1 1990 The present study was undertaken to investigate the mechanism for control of hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase and cytochrome P-450 side chain cleavage (P-450scc), enzymes involved in the synthesis and processing of cholesterol in the corpus luteum of pregnant rats. Cholesterol 235-246 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 77-129 10386582-2 1999 Whereas their cholesterol-reducing effect involves inhibition of de novo biosynthesis of cellular cholesterol through competitive inhibition of its rate-limiting enzyme 3-hydroxy-3-methylglutaryl CoA reductase, the mechanism by which they lower triglycerides remains unknown and forms the subject of the current study. Cholesterol 14-25 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 169-209 15539161-1 1990 The effect of copper deficiency on hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase, the key enzyme regulating cholesterol biosynthesis, was investigated in the rat. Cholesterol 118-129 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 43-90 2362431-2 1990 3-Hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase could have a key function in controlling uterine mitosis through its control of mevalonic acid and cholesterol synthesis as the rate-limiting enzyme in their synthetic pathways. Cholesterol 157-168 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-57 10386582-2 1999 Whereas their cholesterol-reducing effect involves inhibition of de novo biosynthesis of cellular cholesterol through competitive inhibition of its rate-limiting enzyme 3-hydroxy-3-methylglutaryl CoA reductase, the mechanism by which they lower triglycerides remains unknown and forms the subject of the current study. Cholesterol 98-109 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 169-209 34081950-1 2021 3-Hydroxy-3-methyl glutaryl-coenzyme A reductase (Hmgcr) encodes the rate-limiting enzyme in the cholesterol biosynthesis pathway. Cholesterol 97-108 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 0-48 35559917-0 2022 Astrocytic PTEN regulates neuropathic pain by facilitating HMGCR-dependent cholesterol biosynthesis. Cholesterol 75-86 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 59-64 35559917-8 2022 Furthermore, PTEN directly interacted with enzymes, including 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR), in the cholesterol biosynthesis pathway. Cholesterol 119-130 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 62-102 35559917-8 2022 Furthermore, PTEN directly interacted with enzymes, including 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR), in the cholesterol biosynthesis pathway. Cholesterol 119-130 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 104-109 35420345-3 2022 Furthermore, Pb toxicity can also alter the regulation of various hormones involved in the synthesis of 3-hydroxy-methyl glutaryl CoA (HMG-CoA reductase), leading to an impairment in normal levels of serum cholesterol and other associated conjugated lipid molecules such HDL-cholesterol, LDL-cholesterol and VLDL-cholesterol. Cholesterol 206-217 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 135-152 35420345-3 2022 Furthermore, Pb toxicity can also alter the regulation of various hormones involved in the synthesis of 3-hydroxy-methyl glutaryl CoA (HMG-CoA reductase), leading to an impairment in normal levels of serum cholesterol and other associated conjugated lipid molecules such HDL-cholesterol, LDL-cholesterol and VLDL-cholesterol. Cholesterol 275-286 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 135-152 35420345-3 2022 Furthermore, Pb toxicity can also alter the regulation of various hormones involved in the synthesis of 3-hydroxy-methyl glutaryl CoA (HMG-CoA reductase), leading to an impairment in normal levels of serum cholesterol and other associated conjugated lipid molecules such HDL-cholesterol, LDL-cholesterol and VLDL-cholesterol. Cholesterol 292-303 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 135-152 35420345-3 2022 Furthermore, Pb toxicity can also alter the regulation of various hormones involved in the synthesis of 3-hydroxy-methyl glutaryl CoA (HMG-CoA reductase), leading to an impairment in normal levels of serum cholesterol and other associated conjugated lipid molecules such HDL-cholesterol, LDL-cholesterol and VLDL-cholesterol. Cholesterol 313-324 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 135-152 34081950-1 2021 3-Hydroxy-3-methyl glutaryl-coenzyme A reductase (Hmgcr) encodes the rate-limiting enzyme in the cholesterol biosynthesis pathway. Cholesterol 97-108 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 50-55 34081950-12 2021 Indeed, chromatin immunoprecipitation assays confirm differential binding of Runx3 and Srebf1 to Hmgcr promoter leading to reduced expression of Hmgcr in SHR as compared to WKY under basal as well as cholesterol-modulated conditions. Cholesterol 200-211 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 97-102 34081950-12 2021 Indeed, chromatin immunoprecipitation assays confirm differential binding of Runx3 and Srebf1 to Hmgcr promoter leading to reduced expression of Hmgcr in SHR as compared to WKY under basal as well as cholesterol-modulated conditions. Cholesterol 200-211 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 145-150 34081950-13 2021 Taken together, this study provides, for the first time, molecular basis for diminished Hmgcr expression in SHR animals, which may account for the reduced circulating cholesterol level in this widely-studied model for cardiovascular diseases. Cholesterol 167-178 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 88-93