Effects of different steroid-biosynthesis inhibitors on the testicular steroidogenesis of the toad Bufo arenarum

Testis fragments from Bufo arenarum were incubated with [7(n)-3H]pregnenolone (P5), [1,2-3H]de-hydroepiandrosterone (DHEA) and [1,2,6,7-3H]testosterone (T), and different steroid-biosynthesis inhibitors. The inhibitors used were: cyanoketone (CNK), spironolactone (SPNL) and finasteride (FIN). CNK si...

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Autor principal: Canosa, L.F
Otros Autores: Ceballos, N.R
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Springer Verlag 2001
Acceso en línea:Registro en Scopus
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030 |a JCPBD 
100 1 |a Canosa, L.F. 
245 1 0 |a Effects of different steroid-biosynthesis inhibitors on the testicular steroidogenesis of the toad Bufo arenarum 
260 |b Springer Verlag  |c 2001 
270 1 0 |m Ceballos, N.R.; Departamento de Ciencias Biologicas, Facultad de Ciencias Exactas, Ciudad Universitaria, 1428 Buenos Aires, Argentina; email: nceballo@bg.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
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504 |a Canosa, L.F., Pozzi, A.G., Ceballos, N.R., Pregnenolone and progesterone metabolism by testes of Bufo arenarum (1998) J Comp Physiol B, 168, pp. 491-496 
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504 |a Hall, P.F., Testicular steroid synthesis: Organization and regulation (1994), 1, pp. 1335-1443. , Knobil E, Neill J (eds) The physiology of reproduction. Raven, New York; Hall, P.F., Sozer, C.C., Eik-Nes, K.B., Formation of dehydro-epiandrosterone during in vivo and in vitro biosynthesis of testosterone by testicular tissue (1964) Endocrinology, 74, pp. 35-43 
504 |a Hirsch, K.S., Jones, C.D., Audia, J.E., Andersson, S., McQuaid, L., Stamm, N.B., Neubauer, B.L., Russell, D.W., LY191704: A selective, nonsteroidal inhibitor of human steroid 5-reductase type I (1993) Proc Natl Acad Sci USA, 90, pp. 5277-5281 
504 |a Hoschoian, J.C., Brownie, A.C., Pathway of androgen synthesis in monkey testis (1967) Steroids, 10, pp. 49-69 
504 |a De Launoit, Y., Simard, J., Durocher, F., Labrie, F., Androgenic 17β-hydroxysteroid dehydrogenase activity of rat type I 3β3-hydroxysteroid dehydrogenase/ΔD5-ΔD4 isomerase (1992) Endocrinology, 130, pp. 553-557 
504 |a Lisboa, B.P., Thin-layer chromatography of steroid, sterols and related compounds (1969), 15, pp. 3-157. , Clayton RB (ed) Methods in enzymology. Academic Press, New York; Menard, R.H., Martin, H.F., Stripp, B., Gillette, J.R., Bartter, F.C., Spironolactone and cytochrome P-450: Impairment of steroid hydroxylation in the adrenal cortex (1974) Life Sci, 15, pp. 1639-1648 
504 |a O'Donnell, L., Stanton, P.G., Wreford, N.G., Robertson, D.M., McLachlan, R.I., Inhibition of 5 alpha-reductase activity impairs the testosterone-dependent restoration of spermiogenesis in adult rats (1996) Endocrinology, 137, pp. 2703-2710 
504 |a Payne, A.H., Hormonal regulation of cytochrome P450 enzymes, cholesterol side-chain cleavage and 17α-hydroxylase/C17-20 lyase in Leydig cells (1990) Biol Reprod, 42, pp. 399-404 
504 |a Penning, T.M., Molecular endocrinology of hydroxysteroid dehydrogenases (1997) Endocr Rev, 18, pp. 281-305 
504 |a Pozzi, A.G., Lantos, C.P., Ceballos, N.R., Mitochondrial localization of 3 beta-hydroxysteroid dehydrogenase 5-ene isomerase in interrenals of the toad Bufo arenarum H (1996) Gen Comp Endocrinol, 103, pp. 176-181 
504 |a Pozzi, A.G., Lantos, C.P., Ceballos, N.R., Subcellular localization of 3 beta hydroxysteroid dehydrogenase isomerase in testis of Bufo arenarum H (1997) Gen Comp Endocrinol, 106, pp. 400-406 
504 |a Preslock, J.P., Steroidogenesis in the mammalian testis (1980) Endocr Rev, 1, pp. 132-139 
504 |a Preslock, J.P., Steinberger, E., Pathway of testosterone biosynthesis in the testis of the marmoset Saguinus oedipus (1976) Steroids, 28, pp. 775-784 
504 |a Preslock, J.P., Steinberger, E., Androgen biosynthesis by marmoset testes in vitro (1977) Gen Comp Endocrinol, 31, pp. 101-105 
504 |a Preslock, J.P., Steinberger, E., Product-inhibition of testicular steroidogenic enzymes in the marmoset Saguinus oedipus (1979) J Steroid Biochem, 11, pp. 1151-1157 
504 |a Schoonen, W.G., Lambert, J.G., Steroid metabolism in the testes of the African catfish, Clarias gariepinus (Burchell), during spawning season, under natural conditions and kept in ponds (1986) Gen Comp Endocrinol, 61, pp. 40-52 
504 |a Schoonen, W.G., Lambert, J.G., Resink, J.W., Viveen, W.J., Van Oordt, P.G., A quantitative study of steroid bioconversions in the testis of the African catfish, Clarias gariepinus (Burchell), under natural spawning and natural and cultivated non-spawning conditions (1987) J Endocrinol, 112, pp. 323-332 
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504 |a Slaunwhite, W.R., Sammuels, L.T., Progesterone as a precursor of testicular androgens (1956) J Biol Chem, 220, pp. 341-352 
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504 |a Takahashi, M., Luu-The, V., Labrie, F., Inhibitory effect of synthetic progestins, 4-MA and cyanoketone on human placental 3 beta-hydroxysteroid dehydrogenase/5-4-ene- isomerase activity (1990) J Steroid Biochem Mol Biol, 37, pp. 231-236 
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520 3 |a Testis fragments from Bufo arenarum were incubated with [7(n)-3H]pregnenolone (P5), [1,2-3H]de-hydroepiandrosterone (DHEA) and [1,2,6,7-3H]testosterone (T), and different steroid-biosynthesis inhibitors. The inhibitors used were: cyanoketone (CNK), spironolactone (SPNL) and finasteride (FIN). CNK significantly increased the recovery of 3β-hydroxy-5-ene steroids while SPNL reduced the metabolism of P5 and the production of C19-steroids. The metabolism of C19-substrates was only modified by CNK, which reduced the transformation of DHEA without modifying the metabolism of T. To determine the degree of inhibition exerted by the inhibitors used, the activities of the enzymes were estimated as the percentage of their contribution to the total steroid metabolism. CNK strongly inhibited the activity of hydroxysteroid dehydrogenase/isomerase if its contribution was estimated using both P5 and DHEA. If the analysis was made considering both activities associated to cytochrome P450 17α-hydroxylase, C17-20 lyase (P450c17), it became evident that SPNL inhibited both of them. The percent contribution of 17β-hydroxysteroid dehydrogenase (17βHSD) activity diminished in the presence of CNK only if it was estimated considering P5 and DHEA metabolism. SPNL produced a significant inhibition of 17βHSD when its contribution was estimated considering P5 metabolism. However, SPNL was insufficient if DHEA or T were considered. The effect of SPNL on the contribution of 17βHSD could be due to the reduction of C19-substrates. The activity of 5α-reductase was inhibited by CNK only if results from P5 and DHEA were considered.  |l eng 
536 |a Detalles de la financiación: Universidad de Buenos Aires 
536 |a Detalles de la financiación: National Council for Scientific Research 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: Acknowledgments This work was supported by grants from the National Research Council of Argentina (CONICET) to its Prog-rama de Regulación Hormonal y Metabólica (PRHOM), and the University of Buenos Aires. The authors wish to thank Dr. Carlos P. Lantos for the critical revision of the manuscript and Mr. Rubén Di Paola for technical assistance. The experiments comply with de ``Principles of animal care'', publication No. 86-23, revised 1985 of the National Institute of Health and also with the argentine laws. 
593 |a Programa de Regulación Hormonal y Metabólica (PRHOM-CONICET), Departamento de Ciencias Biológicas, Universidad de Buenos Aires, Buenos Aires, Argentina 
593 |a Laboratorio de Endocrinología Comparada, Departamento de Ciencias Biológicas, Pabellón 2. Ciudad Universitaria, 1428 Buenos Aires, Argentina 
690 1 0 |a AMPHIBIA 
690 1 0 |a ANURA 
690 1 0 |a ENZYME-INHIBITION 
690 1 0 |a STEROID-HORMONES 
690 1 0 |a TESTES 
700 1 |a Ceballos, N.R. 
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