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Journal articles on the topic '3-Hydroxy-3-methylglutaryl coenzyme A reductase'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

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1

Ness, G. C., C. E. Sample, M. Smith, L. C. Pendleton, and D. C. Eichler. "Characteristics of rat liver microsomal 3-hydroxy-3-methylglutaryl-coenzyme A reductase." Biochemical Journal 233, no. 1 (1986): 167–72. http://dx.doi.org/10.1042/bj2330167.

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A procedure for the preparation of rat liver microsomal fractions essentially devoid of contaminating lysosomes is described. When this preparation was examined by immunoblotting with a rabbit antiserum to rat 3-hydroxy-3-methylglutaryl-CoA reductase, a single band corresponding to an Mr of 100000 was observed. No evidence was found for glycosylation of rat liver-3-hydroxy-3-methylglutaryl-CoA reductase. Native rat liver microsomal 3-hydroxy-3-methylglutaryl-CoA reductase differs from the purified proteolytically modified species in that it displays allosteric kinetics towards NADPH.

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2

Chin, D. J., G. Gil, J. R. Faust, J. L. Goldstein, M. S. Brown, and K. L. Luskey. "Sterols accelerate degradation of hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase encoded by a constitutively expressed cDNA." Molecular and Cellular Biology 5, no. 4 (1985): 634–41. http://dx.doi.org/10.1128/mcb.5.4.634.

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A recombinant plasmid containing a full-length cDNA for hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase was introduced by calcium phosphate-mediated transfection into UT-2 cells, a mutant line of Chinese hamster ovary cells that lack 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and thus require low density lipoprotein-cholesterol and mevalonate for growth. We selected a line of permanently transfected cells, designated TR-36 cells, that expressed high levels of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and thus grew in the absence of low density lipoprotein a

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3

Chin, D. J., G. Gil, J. R. Faust, J. L. Goldstein, M. S. Brown, and K. L. Luskey. "Sterols accelerate degradation of hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase encoded by a constitutively expressed cDNA." Molecular and Cellular Biology 5, no. 4 (1985): 634–41. http://dx.doi.org/10.1128/mcb.5.4.634-641.1985.

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A recombinant plasmid containing a full-length cDNA for hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase was introduced by calcium phosphate-mediated transfection into UT-2 cells, a mutant line of Chinese hamster ovary cells that lack 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and thus require low density lipoprotein-cholesterol and mevalonate for growth. We selected a line of permanently transfected cells, designated TR-36 cells, that expressed high levels of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and thus grew in the absence of low density lipoprotein a

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4

Jones, Peter H. "Tachyphylaxis in 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors." American Journal of Cardiology 87, no. 8 (2001): 1032. http://dx.doi.org/10.1016/s0002-9149(01)01543-0.

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5

Pasco, J. A. "Falls and 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Inhibitors." Archives of Internal Medicine 162, no. 20 (2002): 2381. http://dx.doi.org/10.1001/archinte.162.20.2381.

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6

Heise, Norton, and Fred R. Opperdoes. "Localisation of a 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase in the Mitochondrial Matrix of Trypanosoma brucei Procyclics." Zeitschrift für Naturforschung C 55, no. 5-6 (2000): 473–77. http://dx.doi.org/10.1515/znc-2000-5-626.

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Contrary to Leishmania spp. and Trypanosoma cruzi, Trypanosoma brucei bloodstream forms do not synthesise their own sterols but take these compounds in the form of cholesterol directly from the mammalian host. However, procyclic insect stages synthesise ergosterol rather than cholesterol. Here the sub-cellular localisation of the first committed enzyme of this pathway of isoprenoid synthesis 3-hydroxy-3-methylglutaryl-coenzyme A reductase in T. brucei procyclics (0.9 nmol. min-1 . mg-1 protein) was carried out using both cell-fractionation by isopycnic centrifugation and digitonin-titration ex

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7

Desager, Jean-Pierre, and Yves Horsmans. "Clinical Pharmacokinetics of 3-Hydroxy-3-Methylglutaryl-Coenzyme A Reductase Inhibitors." Clinical Pharmacokinetics 31, no. 5 (1996): 348–71. http://dx.doi.org/10.2165/00003088-199631050-00003.

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8

Dreyer, Geoffrey B., Clare T. Garvie§, Brian W. Metcalf, Thomas D. Meek, and Ruth J. Mayer. "Phosphinic acid inhibitors of 3-hydroxy-3-methylglutaryl-coenzyme a reductase." Bioorganic & Medicinal Chemistry Letters 1, no. 3 (1991): 151–54. http://dx.doi.org/10.1016/s0960-894x(01)80788-5.

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9

Wu, Yan, Fang-Jun Xiong, and Fen-Er Chen. "Stereoselective synthesis of 3-hydroxy-3-methylglutaryl–coenzyme A reductase inhibitors." Tetrahedron 71, no. 45 (2015): 8487–510. http://dx.doi.org/10.1016/j.tet.2015.07.059.

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10

Moghadasian, Mohammed H. "Clinical pharmacology of 3-hydroxy-3-methylglutaryl coenzyme a reductase inhibitors." Life Sciences 65, no. 13 (1999): 1329–37. http://dx.doi.org/10.1016/s0024-3205(99)00199-x.

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11

Louis-Flamberg, Pearl, Catherine E. Peishoff, Deborah L. Bryan, et al. "Slow binding inhibition of 3-hydroxy-3-methylglutaryl-coenzyme A reductase." Biochemistry 29, no. 17 (1990): 4115–20. http://dx.doi.org/10.1021/bi00469a014.

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12

Maurey, Karen, Fred Wolf, and John Golbeck. "3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Activity in Ochromonas malhamensis." Plant Physiology 82, no. 2 (1986): 523–27. http://dx.doi.org/10.1104/pp.82.2.523.

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13

Leivar, Pablo, Víctor M. González, Susanna Castel, et al. "Subcellular Localization of Arabidopsis 3-Hydroxy-3-Methylglutaryl-Coenzyme A Reductase." Plant Physiology 137, no. 1 (2004): 57–69. http://dx.doi.org/10.1104/pp.104.050245.

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14

Trapani, Laura, Marco Segatto, Piergiorgio La Rosa, et al. "3-hydroxy 3-methylglutaryl coenzyme a reductase inhibition impairs muscle regeneration." Journal of Cellular Biochemistry 113, no. 6 (2012): 2057–63. http://dx.doi.org/10.1002/jcb.24077.

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15

LUSKEY, KENNETH L. "Structure and Expression of 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase." Annals of the New York Academy of Sciences 478, no. 1 Metabolic Reg (1986): 249–54. http://dx.doi.org/10.1111/j.1749-6632.1986.tb15535.x.

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16

Takemoto, Masao, and James K. Liao. "Pleiotropic Effects of 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Inhibitors." Arteriosclerosis, Thrombosis, and Vascular Biology 21, no. 11 (2001): 1712–19. http://dx.doi.org/10.1161/hq1101.098486.

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17

van Besien, Herman, Antonella Sassano, Jessica K. Altman, and Leonidas C. Platanias. "Antileukemic properties of 3-hydroxy-3-methylglutaryl-coenzyme A reductase inhibitors." Leukemia & Lymphoma 54, no. 12 (2013): 2601–5. http://dx.doi.org/10.3109/10428194.2013.790022.

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18

Evans, Joseph L., and Michael A. Gealt. "The 3-hydroxy-3-methylglutaryl-coenzyme A reductase of Aspergillus nidulans." Experimental Mycology 12, no. 2 (1988): 132–40. http://dx.doi.org/10.1016/0147-5975(88)90002-3.

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19

Dimster-Denk, D., M. K. Thorsness, and J. Rine. "Feedback regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in Saccharomyces cerevisiae." Molecular Biology of the Cell 5, no. 6 (1994): 655–65. http://dx.doi.org/10.1091/mbc.5.6.655.

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In eukaryotic cells all isoprenoids are synthesized from a common precursor, mevalonate. The formation of mevalonate from 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) is catalyzed by HMG-CoA reductase and is the first committed step in isoprenoid biosynthesis. In mammalian cells, synthesis of HMG-CoA reductase is subject to feedback regulation at multiple molecular levels. We examined the state of feedback regulation of the synthesis of the HMG-CoA reductase isozyme encoded by the yeast gene HMG1 to examine the generality of this regulatory pattern. In yeast, synthesis of Hmg1p was subject

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20

Manzi, Pamela, Giovannella Bruscalupi, Flavia Castellano, and Anna Trentalance. "Seasonal commitment of HMGCoA reductase activity to vitellogenin production." Bioscience Reports 12, no. 3 (1992): 215–19. http://dx.doi.org/10.1007/bf01121791.

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In female frogs (Rana Esculenta) during gametogenesis the cholesterol synthesized in the liver by 3-hydroxy-3-methylglutaryl coenzyme A reductase is mostly exported into the blood and taken up by the oocytes.In order to understand the fate of the neosynthesized cholesterol, female and male frogs and estrogenized male controls were injected with the labelled precursor14C mevalonate.In females and in estrogenized controls, mevalonate-derived radioactivity is found in a plasmatic lipoprotein that has been identified as vitellogenin by immunological detection.The increased 3-hydroxy-3-methylglutar

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21

Wilding, E. Imogen, Dong-Yul Kim, Alexander P. Bryant, et al. "Essentiality, Expression, and Characterization of the Class II 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase ofStaphylococcus aureus." Journal of Bacteriology 182, no. 18 (2000): 5147–52. http://dx.doi.org/10.1128/jb.182.18.5147-5152.2000.

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Sequence comparisons have implied the presence of genes encoding enzymes of the mevalonate pathway for isopentenyl diphosphate biosynthesis in the gram-positive pathogen Staphylococcus aureus. In this study we showed through genetic disruption experiments that mvaA, which encodes a putative class II 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, is essential for in vitro growth of S. aureus. Supplementation of media with mevalonate permitted isolation of an auxotrophic mvaAnull mutant that was attenuated for virulence in a murine hematogenous pyelonephritis infection model. The mva

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22

Reddy Palvai, Vanitha, and Asna Urooj. "Inhibition of 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase (Ex Vivo) by Morus indica (Mulberry)." Chinese Journal of Biology 2014 (September 23, 2014): 1–5. http://dx.doi.org/10.1155/2014/318561.

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Phytochemicals are the bioactive components that contribute to the prevention of cardiovascular and other degenerative diseases. Inhibition of 3-hydroxy-3-methylglutaryl coenzyme A (HMG CoA) reductase would be an effective means of lowering plasma cholesterol in humans. The present study explores the HMG CoA reductase inhibitory effect of extracts from leaves of Morus indica varieties, M5, V1, and S36, compared with the statin, using an ex vivo method. The assay is based on the stoichiometric formation of coenzyme A during the reduction of microsomal HMG CoA to mevalonate. Dechlorophyllised ex

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23

Trapani, Laura, and Valentina Pallottini. "Hypercholesterolemia and 3-Hydroxy 3-Methylglutaryl Coenzyme A Reductase Regulation during Ageing." Scientific World JOURNAL 9 (2009): 564–74. http://dx.doi.org/10.1100/tsw.2009.81.

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We present here a brief description of the path that cholesterol covers from its intestinal absorption to its effect exerted on some enzyme regulation. Some mechanisms underlying hypercholesterolemia onset and, in particular, the role and the regulation of 3-hydroxy 3-methylglutaryl Coenzyme A reductase (HMGR) during adult life and during aging, have been described. In addition some pharmacological interventions to control proper HMGR regulation and, in turn, cholesterol homeostasis maintenance will be introduced.

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24

Hedl, Matija, Lydia Tabernero, Cynthia V. Stauffacher, and Victor W. Rodwell. "Class II 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductases." Journal of Bacteriology 186, no. 7 (2004): 1927–32. http://dx.doi.org/10.1128/jb.186.7.1927-1932.2004.

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25

Thorsness, M., W. Schafer, L. D'Ari, and J. Rine. "Positive and negative transcriptional control by heme of genes encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase in Saccharomyces cerevisiae." Molecular and Cellular Biology 9, no. 12 (1989): 5702–12. http://dx.doi.org/10.1128/mcb.9.12.5702.

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Responses of the yeast genes encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase, HMG1 and HMG2, to in vivo changes in heme concentrations were investigated. Expression of the genes was determined by direct measurement of the mRNA transcribed from each gene, by direct assay of the enzyme activity encoded by each gene, and by measurement of the expression of lacZ fusions to the control regions of each gene. These studies indicated that expression of HMG1 was stimulated by heme, whereas expression of HMG2 was repressed by heme. The effect of heme on HMG1 expression was mediated by the HAP1

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26

Thorsness, M., W. Schafer, L. D'Ari, and J. Rine. "Positive and negative transcriptional control by heme of genes encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase in Saccharomyces cerevisiae." Molecular and Cellular Biology 9, no. 12 (1989): 5702–12. http://dx.doi.org/10.1128/mcb.9.12.5702-5712.1989.

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Responses of the yeast genes encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase, HMG1 and HMG2, to in vivo changes in heme concentrations were investigated. Expression of the genes was determined by direct measurement of the mRNA transcribed from each gene, by direct assay of the enzyme activity encoded by each gene, and by measurement of the expression of lacZ fusions to the control regions of each gene. These studies indicated that expression of HMG1 was stimulated by heme, whereas expression of HMG2 was repressed by heme. The effect of heme on HMG1 expression was mediated by the HAP1

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27

Grahek, Rok, Dušan Milivojevič, Andrej Bastarda, and Matjaž Kračun. "Chromatographic purification of some 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors." Journal of Chromatography A 918, no. 2 (2001): 319–24. http://dx.doi.org/10.1016/s0021-9673(01)00767-1.

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28

Pfefferkorn, Jeffrey A. "Novel 3-hydroxy-3-methylglutaryl-coenzyme A reductase inhibitors: a patent review." Expert Opinion on Therapeutic Patents 21, no. 2 (2011): 187–203. http://dx.doi.org/10.1517/13543776.2011.547478.

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29

Shen, Pei-Ming, Ming-Shi Shiao, Huey-Ru Chung, Kuan-Rong Lee, Yu-Sheng Chao, and Vincent M. Hunt. "Liquid Chromatographic Determination of 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase Inhibitors." Journal of the Chinese Chemical Society 43, no. 5 (1996): 451–57. http://dx.doi.org/10.1002/jccs.199600065.

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30

Lopez, Dayami, Christopher M. Chambers, and Gene C. Ness. "3-Hydroxy-3-methylglutaryl Coenzyme A Reductase Inhibitors Unmask Cryptic Regulatory Mechanisms." Archives of Biochemistry and Biophysics 343, no. 1 (1997): 118–22. http://dx.doi.org/10.1006/abbi.1997.0162.

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31

Rogers, Kenneth S., Victor W. Rodwell, and Paul Geiger. "Active Form ofPseudomonas mevalonii3-Hydroxy-3-methylglutaryl Coenzyme A Reductase." Biochemical and Molecular Medicine 61, no. 1 (1997): 114–20. http://dx.doi.org/10.1006/bmme.1997.2596.

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32

Gertler, F. B., C. Y. Chiu, L. Richter-Mann, and D. J. Chin. "Developmental and metabolic regulation of the Drosophila melanogaster 3-hydroxy-3-methylglutaryl coenzyme A reductase." Molecular and Cellular Biology 8, no. 7 (1988): 2713–21. http://dx.doi.org/10.1128/mcb.8.7.2713.

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The enzyme 3-hydroxy-3-methylglutaryl coenzyme A (HMG CoA) reductase in Drosophila melanogaster synthesizes mevalonate for the production of nonsterol isoprenoids, which are essential for growth and differentiation. To understand the regulation and developmental role of HMG CoA reductase, we cloned the D. melanogaster HMG CoA reductase gene. The nucleotide sequence of the Drosophila HMG CoA reductase was determined from genomic and cDNA clones. A 2,748-base-pair open reading frame encoded a polypeptide of 916 amino acids (Mr, 98,165) that was similar to the hamster HMG CoA reductase. The C-ter

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33

Gertler, F. B., C. Y. Chiu, L. Richter-Mann, and D. J. Chin. "Developmental and metabolic regulation of the Drosophila melanogaster 3-hydroxy-3-methylglutaryl coenzyme A reductase." Molecular and Cellular Biology 8, no. 7 (1988): 2713–21. http://dx.doi.org/10.1128/mcb.8.7.2713-2721.1988.

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The enzyme 3-hydroxy-3-methylglutaryl coenzyme A (HMG CoA) reductase in Drosophila melanogaster synthesizes mevalonate for the production of nonsterol isoprenoids, which are essential for growth and differentiation. To understand the regulation and developmental role of HMG CoA reductase, we cloned the D. melanogaster HMG CoA reductase gene. The nucleotide sequence of the Drosophila HMG CoA reductase was determined from genomic and cDNA clones. A 2,748-base-pair open reading frame encoded a polypeptide of 916 amino acids (Mr, 98,165) that was similar to the hamster HMG CoA reductase. The C-ter

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34

Rosser, D. S. E., M. N. Ashby, J. L. Ellis, and P. A. Edwards. "Coordinate Regulation of 3-Hydroxy-3-methylglutaryl-coenzyme A Synthase, 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase, and Prenyltransferase Synthesis but Not Degradation in HepG2 Cells." Journal of Biological Chemistry 264, no. 21 (1989): 12653–56. http://dx.doi.org/10.1016/s0021-9258(18)63906-7.

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35

Ness, Gene. "Physiological and Pharmacological Regulation of Hepatic 3-Hydroxy-3- Methylglutaryl Coenzyme A Reductase." Current Medicinal Chemistry-Immunology, Endocrine & Metabolic Agents 3, no. 3 (2003): 219–27. http://dx.doi.org/10.2174/1568013033483366.

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36

HASUMI, KEIJI, MASAOMI ARAHIRA, KAORU SAKAI, and AKIRA ENDO. "Irreversible inhibition of 3-hydroxy-3-methylglutaryl coenzyme a reductase by phenicin (phoenicine)." Journal of Antibiotics 40, no. 2 (1987): 224–26. http://dx.doi.org/10.7164/antibiotics.40.224.

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37

Kennelly, P. J., and V. W. Rodwell. "Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by reversible phosphorylation-dephosphorylation." Journal of Lipid Research 26, no. 8 (1985): 903–14. http://dx.doi.org/10.1016/s0022-2275(20)34292-9.

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38

Gebhard, R. L., B. G. Stone, and W. F. Prigge. "3-Hydroxy-3-methylglutaryl coenzyme A reductase activity in the human gastrointestinal tract." Journal of Lipid Research 26, no. 1 (1985): 47–53. http://dx.doi.org/10.1016/s0022-2275(20)34403-5.

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39

Meigs, T. E., and R. D. Simoni. "Regulated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in permeabilized cells." Journal of Biological Chemistry 267, no. 19 (1992): 13547–52. http://dx.doi.org/10.1016/s0021-9258(18)42246-6.

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40

MOORE, UNA M., ALAN H. JOHNSON, BRIDGET M. DICKSON, GERALD H. TOMKIN, and PATRICK B. COLLINS. "Insulinopaenia increases 3-hydroxy-3-methylglutaryl-coenzyme A reductase levels in intestinal cells." Biochemical Society Transactions 18, no. 2 (1990): 321–22. http://dx.doi.org/10.1042/bst0180321.

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41

Jarmużek, Dorota, Tomasz Pedzinski, Marcin Hoffmann, Tomasz Siodła, and Donata Pluskota-Karwatka. "Phototransformations of pitavastatin - The inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase." Journal of Photochemistry and Photobiology A: Chemistry 389 (February 2020): 112243. http://dx.doi.org/10.1016/j.jphotochem.2019.112243.

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42

Adam, Oliver, Hans-Ruprecht Neuberger, Michael Böhm, and Ulrich Laufs. "Prevention of Atrial Fibrillation With 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Inhibitors." Circulation 118, no. 12 (2008): 1285–93. http://dx.doi.org/10.1161/circulationaha.107.760892.

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43

Ji, Wan, Kriton K. Hatzios, and Carole L. Cramer. "Expression of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in maize tissues." Physiologia Plantarum 84, no. 2 (1992): 185–92. http://dx.doi.org/10.1034/j.1399-3054.1992.840201.x.

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44

Lüdke, Svena M., Ulrich Flenker, Wilhelm Schänzer, and Dietmar Schomburg. "Stable carbon isotope discrimination by human 3-hydroxy-3-methylglutaryl-coenzyme A reductase." Journal of Lipid Research 49, no. 12 (2008): 2620–26. http://dx.doi.org/10.1194/jlr.m800313-jlr200.

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45

Corsini, Alberto, Franco Bernini, Pierangelo Quarato, et al. "Non-Lipid-Related Effects of 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Inhibitors." Cardiology 87, no. 6 (1996): 458–68. http://dx.doi.org/10.1159/000177139.

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46

Yu, Suzanne G., Naji M. Abuirmeileh, Asaf A. Qureshi, and Charles E. Elson. "Dietary .beta.-ionone suppresses hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase activity." Journal of Agricultural and Food Chemistry 42, no. 7 (1994): 1493–96. http://dx.doi.org/10.1021/jf00043a019.

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47

Istvan, Eva S. "Structural mechanism for statin inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase." American Heart Journal 144, no. 6 (2002): S27—S32. http://dx.doi.org/10.1067/mhj.2002.130300.

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48

LEHOUX, JEAN-GUY, NICOLAS KANDALAFT, SERGE BELISLE, and DIEGO BELLABARBA. "Characterization of 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase in Human Adrenal Cortex*." Endocrinology 117, no. 4 (1985): 1462–68. http://dx.doi.org/10.1210/endo-117-4-1462.

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49

Hoeg, Jeffrey M. "3-Hydroxy-3-Methylglutaryl—Coenzyme A Reductase Inhibitors in the Treatment of Hypercholesterolemia." JAMA: The Journal of the American Medical Association 258, no. 24 (1987): 3532. http://dx.doi.org/10.1001/jama.1987.03400240064025.

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50

Bochar, Daniel A., Cynthia V. Stauffacher, and Victor W. Rodwell. "Sequence Comparisons Reveal Two Classes of 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase." Molecular Genetics and Metabolism 66, no. 2 (1999): 122–27. http://dx.doi.org/10.1006/mgme.1998.2786.

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