The 3-hydroxy-3-methylglutaryl coenzyme-A reductases from fungi: A proposal as a therapeutic target and as a study model

Revista Iberoamericana de Micologia

Volumn 31, Issue 1, 2014, Pages 81-85

  Andrade Pavón, Dulce ^a   Sánchez Sandoval, Eugenia ^a   Rosales Acosta, Blanca ^a   Ibarra, José Antonio ^a   Tamariz, Joaquín ^a   Hernández Rodríguez, César ^a   Villa Tanaca, Lourdes ^a  

^a INSTITUTO POLITÉCNICO NACIONAL   (Mexico)

Author keywords

3 Hydroxy 3 methylglutaryl coenzyme; A reductase(EC 1.1.1.34); Ergosterol synthesis

Indexed keywords

(EC 1.1.1.34); 3-HIDROXI-3-METILGLUTARIL COENZIMA A REDUCTASA; 3-HYDROXY-3-METHYLGLUTARYL COENZYME A REDUCTASE; ERGOSTEROL SYNTHESIS; SÍNTESIS DE COLESTEROL;

ANIMALS; ANTIFUNGAL AGENTS; CANDIDA; CHOLESTEROL; CRYSTALLOGRAPHY, X-RAY; DRUG EVALUATION, PRECLINICAL; ERGOSTEROL; FUNGAL PROTEINS; FUNGI; GENES, FUNGAL; HUMANS; HYDROXYMETHYLGLUTARYL COA REDUCTASES; HYDROXYMETHYLGLUTARYL-COA REDUCTASE INHIBITORS; MOLECULAR TARGETED THERAPY; MYCOSES; NADP; RODENTIA; SCHIZOSACCHAROMYCES; SPECIES SPECIFICITY; USTILAGO;

EID: 84893718650     PISSN: 11301406     EISSN: 21739188     Source Type: Journal    
DOI: 10.1016/j.riam.2013.10.004     Document Type: Short Survey

References (25)

1. Arguelles N., Sanchez-Sandoval E., Mendieta A., Villa-Tanaca L., Garduno-Siciliano L., Jimenez F., et al. Design, synthesis, and docking of highly hypolipidemic agents: Schizosaccharomyces pombe as a new model for evaluating alpha-asarone-based HMG-CoA reductase inhibitors. Bioorg Med Chem 2010, 18:4238-4248.
2. Basson M.L., Thorsness M.K., Rine J. Saccharomyces cerevisiae contains two functional genes encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase. Proc Natl Acad Sci USA 1986, 83:5563-5567.
3. Burg J.S., Espenshade P.J. Regulation of HMG-CoA reductase in mammals and yeast. Prog Lipid Res 2011, 50:403-410.
4. Cabral M.E., Figueroa L.I.C., Fariña J.I. Synergistic antifungal activity of statin-azole associations as witnessed by Saccharomyces cerevisiae- and Candida utilis-bioassays an ergosterol quantification. Rev Iberoam Micol 2013, 30:31-38.
5. Chin N.X., Weitzman I., Della-Latta P. In vitro activity of fluvastatin, a cholesterol lowering agent, and synergy with fluconazole and itraconazole against Candida species and Cryptococcus neoformans. Antimicrob Agents Chemother 1997, 41:850-852.
6. Croxen R., Croosey M.W., Keon J.P.R., Hargreaves J.A. Isolation of an Ustilago maydis gene encoding 3-hydroxy-3-methylglutaryl-coenzyme A reductase and expression of a C-terminal-truncated form in Escherichia coli. Microbiology 1994, 140:2363-2370.
7. Daum G., Lees N.D., Bard M., Dickson R. Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae. Yeast 1998, 14:1471-1510.
8. Endo A., Kuroda M., Tsujita Y. ML-236A ML-236B, and ML-236C, new inhibitors of cholesterogenesis produced by Penicillium citrinium. J Antibiot (Tokyo) 1976, 29:1346-1348.
9. Friesen J.A., Rodwell V.W. The 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-Co-A) reductases. Genome Biol 2004, 5. 248.1-248 7.
10. Grabinska K., Palamarczyk G. Dolichol biosynthesis in the yeast Saccharomyces cerevisiae: an insight into the regulatory role of farnesyl diphosphate synthase. FEMS Yeast Res 2002, 2:259-265.
11. Haines B.E., Wiest O., Stauffacher C.V. The increasingly complex mechanism of HMG-CoA reductase. Acc Chem Res 2013, 46:2416-2426.
12. Istvan E.S., Palnitkar M., Buchanan S.K., Deisenhofer J. Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis. EMBO J 2000, 19:819-830.
13. Iwaki T., Iefuji H., Hiraga Y., Hosomi A., Morita T., Giga-Hama Y., et al. Multiple functions of ergosterol in the fission yeast Schizosaccharomyces pombe. Microbiology 2008, 154:830-841.
14. Jin H., McCaffery J.M., Grote E. Ergosterol promotes pheromone signaling and plasma membrane fusion in mating yeast. J Cell Biol 2008, 180:813-826.
15. Koning A.J., Roberts C.J., Wright R.L. Different subcellular localization of Saccharomyces cerevisiae HMG-CoA reductase isoenzymes at elevated levels corresponds to distinct endoplasmic reticulum membrane proliferations. Mol Biol Cell 1996, 7:769-789.
16. Lees N.D., Skaggs B., Kirsch D.R., Bard M. Cloning of the late genes in the ergosterol biosynthetic pathway of Saccharomyces cerevisiae - a review. Lipids 1995, 30:221-226.
17. Leszczynska A., Burzynska B., Plochocka D., Kaminska J., Zimnicka M., Kania M., et al. Investigating the effects of statins on cellular lipid metabolism using a yeast expression system. PLoS One 2009, 4:e8499.
18. Lorenz R.T., Parks L.W. Effects of lovastatin (mevinolin) on sterol levels and on activity of azoles in Saccharomyces cerevisiae. Antimicrob Agents Chemother 1990, 34:1660-1665.
19. Lukács G., Papp T., Somogyvári F., Csernetics A., Nyilasi I., Vágvölgyi C. Cloning of the Rhizomucor miehei 3-hydroxy-3-methylglutaryl-coenzyme A reductase gene and its heterelogous expression in Mucor circinelloides. Antonie Van Leeuwenhoek 2009, 95:55-64.
20. Lum P.Y., Edwards S., Wright R. Molecular, functional and evolutionary characterization of the gene encoding HMG-CoA reductase in the fission yeast, Schizosaccharomyces pombe. Yeast 1996, 12:1107-1124.
21. Macreadie I.G., Johnson G., Schlosser T., Macreadie P.I. Growth inhibition of Candida species and Aspergillus fumigatus by statins. FEMS Microbiol Lett 2006, 262:9-13.
22. Medina-Franco J.L., López-Vallejo F., Rodríguez-Morales S., Castillo R., Chamorro G., Tamariz J. Molecular docking of the highly hypolipidemic agent alpha-asarone with the catalytic portion of HMG-CoA reductase. Bioorg Med Chem Lett 2005, 15:989-994.
23. Tobert J.A. Lovastatin and beyond: the history of the HMG-CoA reductase inhibitors. Nat Rev Drug Discov 2003, 2:517-526.
24. Wachtler V., Rajagopalan S., Balasubramanian M.K. Sterol-rich plasma membrane domains in the fission yeast Schizosaccharomyces pombe. J Cell Sci 2003, 116:867-874.
25. Westermeyer C., Macreadie I.G. Simvastatin reduces ergosterol levels, inhibits growth and causes loss of mtDNA in Candida glabrata. FEMS Yeast Res 2007, 7:436-441.