Lovastatin Hydroxy Acid - CAS 75225-51-3
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Molecular Weight:
Lovastatin Hydroxy Acid is an active metabolite of Lovastatin. Lovastatin is a HMG-CoA reductase inhibitor isolated from cultures of Aspergillus terreus. HMG-CoA reductase plays a role in cholesterol biosynthesis.
Lovastatin acid; Mevinolinic acid; Monacolinic K acid; MSD 803 acid; MSD 803 free acid; UNII-5CLV35Y90C; (3R,5R)-7-[(1S,2S,6R,8S,8aR)-2,6-dimethyl-8-[(2S)-2-methylbutanoyl]oxy-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
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1.Lovastatin and sodium phenylacetate normalize the levels of very long chain fatty acids in skin fibroblasts of X- adrenoleukodystrophy.
Singh I1, Pahan K, Khan M. FEBS Lett. 1998 Apr 24;426(3):342-6.
The present study underlines the importance of lovastatin, an inhibitor of 3-hydroxy-3-methyl-glutaryl-coenzyme A (HMG-CoA) reductase, and the sodium salt of phenylacetic acid (NaPA), an inhibitor of mevalonate pyrophosphate decarboxylase, in normalizing the pathognomonic accumulation of saturated very long chain fatty acids (VLCFA) in cultured skin fibroblasts of X-adrenoleukodystrophy (X-ALD) in which the ALD gene is either mutated or deleted. Lovastatin or NaPA alone or in combination stimulated the beta-oxidation of lignoceric acid (C24:0) and normalized the elevated levels of VLCFA in skin fibroblasts of X-ALD. Ability of lovastatin and NaPA to normalize the pathognomonic accumulation of VLCFA in skin fibroblasts of X-ALD may identify these drugs as possible therapeutics for X-ALD.
2.Effects of different inhibitors of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, pravastatin sodium and simvastatin, on sterol synthesis and immunological functions in human lymphocytes in vitro.
Kurakata S1, Kada M, Shimada Y, Komai T, Nomoto K. Immunopharmacology. 1996 Aug;34(1):51-61.
It has been shown previously that 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors (HMG-CoA RIs) such as compactin and lovastatin suppress human lymphocyte functions in vitro (Cuthbert and Lipsky, 1981; Cutts and Bankhurst, 1989). Although it is not fully understood what inhibitory role the HMG-CoA RIs perform in causing this suppression, we show in this study that a certain inhibition threshold (inhibition level > 90%) of lymphocytic HMG-CoA reductase is required for the HMG-CoA RIs to attain effective inhibitory action in human lymphocyte lymphocyte functions in vitro. Thus the inhibitory activity of simvastatin, a lipophilic inhibitor, on sterol synthesis (HMG-CoA reductase activity) in lymphocytes was as much as 430 times more potent than that of pravastatin sodium, a hydrophilic inhibitor (IC50; 0.013 microM and 5.6 microM, respectively), and although pravastatin sodium and simvastatin at concentration levels of 10 and 0.
3.Mode of interaction of beta-hydroxy-beta-methylglutaryl coenzyme A reductase with strong binding inhibitors: compactin and related compounds.
Nakamura CE, Abeles RH. Biochemistry. 1985 Mar 12;24(6):1364-76.
The sodium salts of compactin (1) and trans-6-[2-(2,4- dichloro-6-hydroxyphenyl)ethyl]-3,4,5,6-tetrahydro-4-hydroxy-2H-pyran- 2-one (3) are inhibitors of yeast beta-hydroxy-beta-methylglutaryl coenzyme A (HMG-CoA) reductase. The dissociation constants are 0.24 X 10(-9) and 0.28 X 10(-9) M, respectively. Similar values have been reported for HMG-CoA reductase from mammalian sources [Endo, A., Kuroda, M., & Tanzawa, K. (1976) FEBS Lett. 72, 323; Alberts, A. W., et al. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 3957]. The structures of these compounds marginally resemble that of any substrates of HMG-CoA reductase. We, therefore, investigated the basis for the strong interaction between HMG-CoA reductase and these inhibitors. HMG-CoA and coenzyme A (CoASH), but not reduced nicotinamide adenine dinucleotide phosphate (NADPH), prevent binding of compactin to the enzyme. HMG-CoA, but not CoASH or NADPH, prevents binding of 3 to the enzyme. We also investigated the inhibitory activity of molecules that resemble structural components of compactin.
4.[Action of lovastatin--an inhibitor of cholesterol biosynthesis on bacterial bioluminescence].
Baranova NA1, Krĕier VG, Egorov NS. Antibiot Khimioter. 1995 Aug;40(8):12-6.
The action of lovastatin, a competing inhibitor of 3-hydroxy-3-methylglutaryl CoA reductase, on bacterial bioluminescence was studied. The lovastatin lactone form and sodium salt of mevinolinic acid inhibited bacterial luciferase in vitro but did not affect bioluminescence of the intact cells of the luminous bacteria. The inhibition was found to be of a competing character in regard to aliphatic aldehyde, the bacterial luciferase substrate. Conditions under which the bioluminescence inhibition was proportional to the lovastatin concentration in the incubation mixture and a bioluminescence method for quantitative determination of the inhibitor were developed.
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Lovastatin Hydroxy Acid is an active metabolite of Lovastatin. Lovastatin is a HMG-CoA reductase inhibitor isolated from cultures of Aspergillus terreus. HMG-Co...

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CAS 75225-51-3 Lovastatin Hydroxy Acid

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