Steroid promiscuity: Diversity of enzyme action

Journal of Steroid Biochemistry and Molecular Biology

Volumn 151, Issue , 2015, Pages 1-2

  Lathe, Richard ^a   Kotelevtsev, Yuri ^b   Mason, J Ian ^c  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b SKOLKOVO INSTITUTE OF SCIENCE AND TECHNOLOGY   (Russian Federation)

^c UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

Promiscuity; Steroid

Indexed keywords

ADRENALIN; CYTOCHROME P450; ESTROGEN RECEPTOR; HYDROXYSTEROID DEHYDROGENASE; PROGESTERONE; STEROID; CHOLESTEROL ACYLTRANSFERASE; LIGAND;

BINDING AFFINITY; BINDING SITE; BIOLOGICAL ACTIVITY; BLOOD FLOW; EDITORIAL; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; LIGAND BINDING; METABOLIC BALANCE; SIGNAL TRANSDUCTION;

CYTOCHROME P-450 ENZYME SYSTEM; HYDROXYSTEROID DEHYDROGENASES; LIGANDS; STEROIDS; STEROL O-ACYLTRANSFERASE;

EID: 84938837708     PISSN: 09600760     EISSN: 18791220     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2015.01.008     Document Type: Editorial

References (23)

1. [1] Mark, L.C., Brand, L., What price pharmacological promiscuity?. J. Oral Ther. Pharmacol., 2, 1965, 125.
2. [2] Lieberman, P.M., O'Hare, P., Hayward, G.S., Hayward, S.D., Promiscuous trans activation of gene expression by an Epstein–Barr virus-encoded early nuclear protein. J. Virol. 60 (1986), 140–148.
3. [3] Kenakin, T., Are receptors promiscuous? Intrinsic efficacy as a transduction phenomenon. Life Sci. 43 (1988), 1095–1101.
4. [4] Cheng, H.C., Matsuura, I., Wang, J.H., In vitro substrate specificity of protein tyrosine kinases. Mol. Cell. Biochem. 127–128 (1993), 103–112.
5. [5] Pilgrim, C., The unexpected promiscuity of steroid hormones. Eur. J. Histochem. 43 (1999), 261–264.
6. [6] Diczfalusy, U., Bjorkhem, I., Still another activity by the highly promiscuous enzyme CYP3A4: 25-hydroxylation of cholesterol. J. Lipid Res. 52 (2011), 1447–1449.
7. [7] Hulce, J.J., Cognetta, A.B., Niphakis, M.J., Tully, S.E., Cravatt, B.F., Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells. Nat. Methods 10 (2013), 259–264.
8. [8] Lathe, R., Kotelevtsev, Y., Steroid signaling: ligand-binding promiscuity molecular symmetry, and the need for gating. Steroids 82 (2014), 14–22.
9. [9] Kell, D.B., Dobson, P.D., Bilsland, E., Oliver, S.G., The promiscuous binding of pharmaceutical drugs and their transporter-mediated uptake into cells: what we (need to) know and how we can do so. Drug Discov. Today 18 (2013), 218–239.
10. [10] O'Brien, P.J., Herschlag, D., Catalytic promiscuity and the evolution of new enzymatic activities. Chem. Biol. 6 (1999), R91–R105.
11. [11] Tawfik, D.S., Messy biology and the origins of evolutionary innovations. Nat. Chem. Biol. 6 (2010), 692–696.
12. [12] Weng, J.K., Noel, J.P., The remarkable pliability and promiscuity of specialized metabolism. Cold Spring Harb. Symp. Quant. Biol. 77 (2012), 309–320.
13. [13] Kuiper, G.G., Carlsson, B., Grandien, K., Enmark, E., Haggblad, J., Nilsson, S., et al. Comparison of the ligand binding specificity and transcript tissue distribution of estrogen receptors alpha and beta. Endocrinology 138 (1997), 863–870.
14. [14] Pace, P., Taylor, J., Suntharalingam, S., Coombes, R.C., Ali, S., Human estrogen receptor beta binds DNA in a manner similar to and dimerizes with estrogen receptor alpha. J. Biol. Chem. 272 (1997), 25832–25838.
15. [15] O'Brian, C.A., Liskamp, R.M., Solomon, D.H., Weinstein, I.B., Inhibition of protein kinase C by tamoxifen. Cancer Res. 45 (1985), 2462–2465.
16. 2+-dependent binding of tamoxifen to calmodulin isolated from bovine brain. Cancer Res. 50 (1990), 2753–2758.
17. [17] de Medina, P., Payre, B.L., Bernad, J., Bosser, I., Pipy, B., Silvente-Poirot, S., et al. Tamoxifen is a potent inhibitor of cholesterol esterification and prevents the formation of foam cells. J. Pharmacol. Exp. Ther. 308 (2004), 1165–1173.
18. [18] Kedjouar, B., de, M.P., Oulad-Abdelghani, M., Payre, B., Silvente-Poirot, S., Favre, G., et al. Molecular characterization of the microsomal tamoxifen binding site. J. Biol. Chem. 279 (2004), 34048–34061.
19. [19] Filardo, E., Quinn, J., Pang, Y., Graeber, C., Shaw, S., Dong, J., et al. Activation of the novel estrogen receptor G protein-coupled receptor 30 (GPR30) at the plasma membrane. Endocrinology 148 (2007), 3236–3245.
20. [20] Toran-Allerand, C.D., Guan, X., MacLusky, N.J., Horvath, T.L., Diano, S., Singh, M., et al. ER-X: a novel plasma membrane-associated, putative estrogen receptor that is regulated during development and after ischemic brain injury. J. Neurosci. 22 (2002), 8391–8401.
21. [21] Jordan, V.C., Tamoxifen: a most unlikely pioneering medicine. Nat. Rev. Drug Discov. 2 (2003), 205–213.
22. [22] Payre, B., de, M.P., Boubekeur, N., Mhamdi, L., Bertrand-Michel, J., Terce, F., et al. Microsomal antiestrogen-binding site ligands induce growth control and differentiation of human breast cancer cells through the modulation of cholesterol metabolism. Mol. Cancer Ther. 7 (2008), 3707–3718.
23. [23] de Medina, P., Payre, B., Boubekeur, N., Bertrand-Michel, J., Terce, F., Silvente-Poirot, S., et al. Ligands of the antiestrogen-binding site induce active cell death and autophagy in human breast cancer cells through the modulation of cholesterol metabolism. Cell Death Differ. 16 (2009), 1372–1384.