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Lovastatin Hydroxy Acid (sodium salt) Sale

(Synonyms: 洛伐他汀钠,Mevinolinic acid sodium) 目录号 : GC44082

A potent HMG-CoA reductase inhibitor

Lovastatin Hydroxy Acid (sodium salt) Chemical Structure

Cas No.:75225-50-2

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1mg
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5mg
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产品描述

Lovastatin hydroxy acid is a potent and competitive inhibitor of HMG-CoA reductase (Ki = 0.6 nM). It is the more potent, open ring, hydroxy acid form of its prodrug, lovastatin .

Chemical Properties

Cas No. 75225-50-2 SDF
别名 洛伐他汀钠,Mevinolinic acid sodium
Canonical SMILES C[C@H]1C=CC2=C[C@H](C)C[C@H](OC([C@@H](C)CC)=O)[C@]2([H])[C@H]1CC[C@@H](O)C[C@@H](O)CC([O-])=O.[Na+]
分子式 C24H37O6•Na 分子量 444.5
溶解度 DMF: 10 mg/ml,DMSO: 10 mg/ml,Ethanol: 10 mg/ml 储存条件 Store at -20°C
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1 mg 5 mg 10 mg
1 mM 2.2497 mL 11.2486 mL 22.4972 mL
5 mM 0.4499 mL 2.2497 mL 4.4994 mL
10 mM 0.225 mL 1.1249 mL 2.2497 mL
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Research Update

Lovastatin and sodium phenylacetate normalize the levels of very long chain fatty acids in skin fibroblasts of X- adrenoleukodystrophy

FEBS Lett 1998 Apr 24;426(3):342-6.PMID:9600263DOI:10.1016/s0014-5793(98)00370-6.

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.

Mode of interaction of beta-hydroxy-beta-methylglutaryl coenzyme A reductase with strong binding inhibitors: compactin and related compounds

Biochemistry 1985 Mar 12;24(6):1364-76.PMID:3886005DOI:10.1021/bi00327a014.

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. Compactin consists of a moiety resembling 3,5-dihydroxyvaleric acid that is attached to a decalin structure. The sodium salt of DL-3,5-dihydroxyvaleric acid inhibits HMG-CoA reductase competitively with respect to HMG-CoA and noncompetitively with respect to NADPH. The dissociation constant for DL-3,5-dihydroxyvaleric acid, derived from protection against inactivation of enzyme by iodoacetic acid, is (2.1 +/- 0.9) X 10(-2) M. Two decalin derivatives (structurally identical with or closely related to the decalin moiety of compactin) showed no detectable inhibition. If the lack of inhibition is due to their limited solubility, the dissociation constant of these decalin derivatives may be conservatively estimated to be greater than or equal to 0.5 mM. Simultaneous addition of decalin derivatives and DL-3,5-dihydroxyvaleric acid does not lead to enhanced inhibition. The sodium salt of (E)-6-[2-(2-methoxy-1-naphthalenyl)ethenyl]-3,4,5,6- tetrahydro-4-hydroxy-2H-pyran-2-one (6) inhibits HMG-CoA reductase competitively with respect to HMG-CoA and noncompetitively with respect to NADPH. The inhibition constant (vs. HMG-CoA) is 0.8 microM. CoASH does not prevent binding of 6 to enzyme. Compound 6, therefore, behaves analogously to compound 3. We propose that these inhibitors occupy two sites on the enzyme: one site is the hydroxymethylglutaryl binding domain of the enzyme active site and the other site is a hydrophobic pocket located adjacent to the active site.(ABSTRACT TRUNCATED AT 400 WORDS)

Lipid metabolism as a target for brain cancer therapy: synergistic activity of lovastatin and sodium phenylacetate against human glioma cells

J Neurochem 1996 Feb;66(2):710-6.PMID:8592143DOI:10.1046/j.1471-4159.1996.66020710.x.

Malignant gliomas, the most common form of primary brain tumors, are highly dependent on the mevalonate (MVA) pathway for the synthesis of lipid moieties critical to cell replication. Human glioblastoma cells were found to be uniquely vulnerable to growth arrest by lovastatin, a competitive inhibitor of the enzyme regulating MVA synthesis, 3-hydroxy-3-methylglutaryl coenzyme A reductase. The sodium salt of phenylacetic acid (NaPA), an inhibitor of MVA-pyrophosphate decarboxylase, the enzyme that controls MVA use, acted synergistically with lovastatin to suppress malignant growth. When used at pharmacologically attainable concentrations, the two compounds induced profound cytostasis and loss of malignant properties such as invasiveness and expression of the transforming growth factor-beta 2 gene, coding for a potent immunosuppressive cytokine. Supplementation with exogenous ubiquinone, an end product of the MVA pathway, failed to rescue the cells, suggesting that decreased synthesis of intermediary products are responsible for the antitumor effects observed. In addition to blocking the MVA pathway, lovastatin alone and in combination with NaPA increased the expression of the peroxisome proliferator-activated receptor, a transcription factor implicated in the control of lipid metabolism, cell growth, and differentiation. Our results indicate that targeting lipid metabolism with lovastatin, used alone or in combination with the aromatic fatty acid NaPA, may offer a novel approach to the treatment of malignant gliomas.

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

Immunopharmacology 1996 Aug;34(1):51-61.PMID:8880225DOI:10.1016/0162-3109(96)00108-7.

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 0.016 microM respectively, inhibited the sterol synthesis in just over 50%, they failed to inhibit the lymphocyte functions. Significant inhibition (P < 0.01) of lymphocyte functions, including lymphocyte proliferative response to a variety of stimuli and activated natural killer-cell cytotoxicity, was demonstrated only when greater than 90% of the sterol synthesis in lymphocytes was inhibited by either simvastatin or simvastatin sodium salt at concentrations above 2 microM. This simvastatin-induced inhibition of lymphocyte functions was almost completely reversed by the addition of a 1 mM solution of mevalonate. Although simvastatin at a lower clinical blood concentration of 0.016 microM failed to inhibit either lymphocyte functions or HMG-CoA reductase activity sufficiently, at this level it caused a significant increase in cyclosporin A-induced suppression of T-cell response. These results infer that insufficient inhibition (in the 50% region) of HMG-CoA reductase activity by a low clinical blood concentration of HMG-CoA RIs, could still render the lymphocytes susceptible to immunosuppressive treatments. Pravastatin sodium on the other hand, is inactive in inhibiting lymphocyte functions in vitro, and such inactivity can be explained solely of the basis of its failure to inhibit HMG-CoA reductase activity in lymphocytes sufficiently.

HMG-CoA reductase inhibitors: design, synthesis, and biological activity of tetrahydroindazole-substituted 3,5-dihydroxy-6-heptenoic acid sodium salts

J Med Chem 1993 Nov 12;36(23):3674-85.PMID:8246237DOI:10.1021/jm00075a024.

Compounds comprising a series of 7-[2-(4-fluorophenyl)-4,5,6,7-tetrahydro-2H-indazol-3-yl]-3,5- dihydroxy-6-heptenoic acid sodium salts (18) were synthesized and tested for their ability to inhibit HMG-CoA reductase in a partially purified enzyme preparation and cholesterol biosynthesis from acetate in cultured HEP-G2 cells. Changing the size of the saturated ring of the tetrahydroindazole nucleus did not improve potency, but incorporation of substituents at the 7-position resulted in up to 1700-fold improvement in inhibitory potency. Structure-activity studies revealed that the most potent compounds possess a substituted benzyl group at the 7-position, with a preference for steric bulk at the para position of the benzene ring. The most potent enzyme inhibitor (18t, IC50 = 3.0 nM) is approximately 3-fold more potent than lovastin sodium salt (2). The most potent cholesterol biosynthesis inhibitor in HEP-G2 cells (18q, IC50 = 0.078 microM) is slightly less potent than 2 (sodium salt). Molecular modeling studies suggested that, when compared to the parent compound (18b) lacking the appropriate 7-substituent, 18t overlaps better with 2 and literature inhibitors 5 and 6 in a hydrophobic binding region adjacent to the enzyme active site.