Is C-26 hydroxylation an evolutionarily conserved steroid inactivation mechanism?
作者： Steve Meaney
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摘要: Sterols are essential components of virtually all higher eukaryotic organisms, though the exact identity dominating sterol varies between species, from C-27 cholesterol in vertebrates to C-28 and C-29 sterols plants invertebrates. In addition their role as structural cell membranes these also converted into a variety biologically active hormones. This conversion generally involves modifications basic structure by dealkylation, hydroxylation and/or isomerization. Recent studies have demonstrated that irreversible inactivation both plant insect hormones is achieved specific C-26 hydroxylation. The concept deactivation 26-hydroxylation appears be an example evolutionarily conserved mechanism has persisted despite widely varying requirements for species where it been detected.—Meaney, S. Is steroid mechanism?
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researchgate.net 参考文章(39)
J. Gustafsson, S. Sjöstedt, On the Stereospecificity of Microsomal "26''-Hydroxylation in Bile Acid Biosynthesis* Journal of Biological Chemistry. ,vol. 253, pp. 199- 201 ,(1978) , 10.1016/S0021-9258(17)38288-1
Lawrence I Gilbert, Halloween genes encode P450 enzymes that mediate steroid hormone biosynthesis in Drosophila melanogaster. Molecular and Cellular Endocrinology. ,vol. 215, pp. 1- 10 ,(2004) , 10.1016/J.MCE.2003.11.003
Steven D. Clouse, Recent Advances in Brassinosteroid Research: From Molecular Mechanisms to Practical Applications. Journal of Plant Growth Regulation. ,vol. 22, pp. 273- 275 ,(2003) , 10.1007/S00344-003-0067-Y
Hideharu Seto, Shozo Fujioka, Hiroyuki Koshino, Shigeo Yoshida, Masayoshi Tsubuki, Toshio Honda, Synthesis and biological evaluation of extra-hydroxylated brassinolide analogs Tetrahedron. ,vol. 55, pp. 8341- 8352 ,(1999) , 10.1016/S0040-4020(99)00427-5
Ryusuke Niwa, Takahiro Matsuda, Takuji Yoshiyama, Toshiki Namiki, Kazuei Mita, Yoshinori Fujimoto, Hiroshi Kataoka, CYP306A1, a cytochrome P450 enzyme, is essential for ecdysteroid biosynthesis in the prothoracic glands of Bombyx and Drosophila. Journal of Biological Chemistry. ,vol. 279, pp. 35942- 35949 ,(2004) , 10.1074/JBC.M404514200
J. T. Warren, A. Petryk, G. Marques, M. Jarcho, J.-P. Parvy, C. Dauphin-Villemant, M. B. O'Connor, L. I. Gilbert, Molecular and biochemical characterization of two P450 enzymes in the ecdysteroidogenic pathway of Drosophila melanogaster Proceedings of the National Academy of Sciences of the United States of America. ,vol. 99, pp. 11043- 11048 ,(2002) , 10.1073/PNAS.162375799
M.R. Walters, I. Nemere, Receptors for steroid hormones: membrane-associated and nuclear forms. Cellular and Molecular Life Sciences. ,vol. 61, pp. 2309- 2321 ,(2004) , 10.1007/S00018-004-4065-4
Ulf Diczfalusy, Erik Lund, Dieter Lötjohann, Ingemar Björkhem, Novel pathways for elimination of cholesterol by extrahepatic formation of side-chain oxidized oxysterols Scandinavian Journal of Clinical and Laboratory Investigation. ,vol. 56, pp. 9- 17 ,(1996) , 10.1080/00365519609168296
Mizuho Une, Hyun-Guell Kim, Michiko Yoshii, Taiju Kuramoto, Takahiko Hoshita, Comparative studies on ω-hydroxylation of 5β-cholestane-3α, 7α,12α-triol in the mitochondrial and microsomal fraction of the liver from several vertebrates Steroids. ,vol. 62, pp. 458- 461 ,(1997) , 10.1016/S0039-128X(97)00012-3
Imelda R. Soriano, Ian T. Riley, Mark J. Potter, William S. Bowers, Phytoecdysteroids: a novel defense against plant-parasitic nematodes. Journal of Chemical Ecology. ,vol. 30, pp. 1885- 1899 ,(2004) , 10.1023/B:JOEC.0000045584.56515.11