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Cloning, characterization and functional expression of Taenia solium 17 beta-hydroxysteroid dehydrogenase.
Aceves-Ramos, A; de la Torre, P; Hinojosa, L; Ponce, A; García-Villegas, R; Laclette, J P; Bobes, R J; Romano, M C.
Afiliación
  • Aceves-Ramos A; Dpto. de Fisiología, Biofísica y Neurociencias, CINVESTAV del I.P.N., Apdo. Postal 14-740, 07000 México, D.F., Mexico.
  • de la Torre P; Dpto. de Inmunología, Instituto de Investigaciones Biomédicas, UNAM, México, D.F., Mexico.
  • Hinojosa L; Dpto. de Fisiología, Biofísica y Neurociencias, CINVESTAV del I.P.N., Apdo. Postal 14-740, 07000 México, D.F., Mexico.
  • Ponce A; Dpto. de Fisiología, Biofísica y Neurociencias, CINVESTAV del I.P.N., Apdo. Postal 14-740, 07000 México, D.F., Mexico.
  • García-Villegas R; Dpto. de Fisiología, Biofísica y Neurociencias, CINVESTAV del I.P.N., Apdo. Postal 14-740, 07000 México, D.F., Mexico.
  • Laclette JP; Dpto. de Inmunología, Instituto de Investigaciones Biomédicas, UNAM, México, D.F., Mexico.
  • Bobes RJ; Dpto. de Inmunología, Instituto de Investigaciones Biomédicas, UNAM, México, D.F., Mexico.
  • Romano MC; Dpto. de Fisiología, Biofísica y Neurociencias, CINVESTAV del I.P.N., Apdo. Postal 14-740, 07000 México, D.F., Mexico. Electronic address: mromano@fisio.cinvestav.mx.
Gen Comp Endocrinol ; 203: 186-92, 2014 Jul 01.
Article en En | MEDLINE | ID: mdl-24698785
The 17ß-hydroxysteroid dehydrogenases (17ß-HSD) are key enzymes involved in the formation (reduction) and inactivation (oxidation) of sex steroids. Several types have been found in vertebrates including fish, as well as in invertebrates like Caenorhabditis elegans, Ciona intestinalis and Haliotis diversicolor supertexta. To date limited information is available about this enzyme in parasites. We showed previously that Taenia solium cysticerci are able to synthesize sex steroid hormones in vitro when precursors are provided in the culture medium. Here, we identified a T. solium 17ß-HSD through in silico blast searches in the T. solium genome database. This coding sequence was amplified by RT-PCR and cloned into the pcDNA 3.1(+) expression vector. The full length cDNA contains 957bp, corresponding to an open reading frame coding for 319 aa. The highest identity (84%) at the protein level was found with the Echinococcus multilocularis 17ß-HSD although significant similarities were also found with other invertebrate and vertebrate 17ß-HSD sequences. The T. solium Tsol-17ßHSD belongs to the short-chain dehydrogenase/reductase (SDR) protein superfamily. HEK293T cells transiently transfected with Tsol17ß-HSD induced expression of Tsol17ß-HSD that transformed 3H-androstenedione into testosterone. In contrast, 3H-estrone was not significantly transformed into estradiol. In conclusion, T. solium cysticerci express a 17ß-HSD that catalyzes the androgen reduction. The enzyme belongs to the short chain dehydrogenases/reductase family and shares motifs and activity with the type 3 enzyme of some other species.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Hormonas Esteroides Gonadales / Taenia solium / 17-Hidroxiesteroide Deshidrogenasas Límite: Animals / Humans Idioma: En Revista: Gen Comp Endocrinol Año: 2014 Tipo del documento: Article País de afiliación: México Pais de publicación: Estados Unidos
Texto completo
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Imprimir
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Hormonas Esteroides Gonadales / Taenia solium / 17-Hidroxiesteroide Deshidrogenasas Límite: Animals / Humans Idioma: En Revista: Gen Comp Endocrinol Año: 2014 Tipo del documento: Article País de afiliación: México Pais de publicación: Estados Unidos