Subcellular localization of 3β hydroxysteroid dehydrogenase isomerase in testis of Bufo arenarum H.

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3β-hydroxysteroid dehydrogenase 5-ene isomerase (3βHSD/I) catalyzes an essential step in the biosynthesis of steroid hormones and is usually considered to be mainly microsomal, although there is a dual distribution of the enzyme in toad interrenals. The present study demonstrates that in the testicu...

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Autores principales: Pozzi, A.G., Lantos, C.P., Ceballos, N.R.
Formato: JOUR
Materias:
3(or 17)beta hydroxysteroid dehydrogenase
androstenedione
isomerase
prasterone
pregnenolone
animal tissue
article
enzyme localization
enzyme substrate
hormone synthesis
microsome
mitochondrion
nonhuman
priority journal
steroidogenesis
testis
toad
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00166480_v106_n3_p400_Pozzi
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling todo:paper_00166480_v106_n3_p400_Pozzi2023-10-03T14:14:00Z Subcellular localization of 3β hydroxysteroid dehydrogenase isomerase in testis of Bufo arenarum H. Pozzi, A.G. Lantos, C.P. Ceballos, N.R. 3(or 17)beta hydroxysteroid dehydrogenase androstenedione isomerase prasterone pregnenolone animal tissue article enzyme localization enzyme substrate hormone synthesis microsome mitochondrion nonhuman priority journal steroidogenesis testis toad 3β-hydroxysteroid dehydrogenase 5-ene isomerase (3βHSD/I) catalyzes an essential step in the biosynthesis of steroid hormones and is usually considered to be mainly microsomal, although there is a dual distribution of the enzyme in toad interrenals. The present study demonstrates that in the testicular tissue, as in interrenals of Bufo arenarum H., 3βHSD/I is both mitochondrial and microsomal. The conversion of dehydroepiandrosterone to androstenedione takes place only in microsomes while pregnenolone is converted to progesterone in both microsomes and mitochondria. Kinetic constants of 3βHSD/I were determined by the oxidation of pregnenolone and dehydroepiandrosterone. The preferred substrate of the microsomal 3βHSD/I enzyme was dehydroepiandrosterone (K(m) = 0.17 μM and 0.53 μM for dehydroepiandrosterone and pregnenolone, respectively) not only during the breeding season but also in the nonbreeding period (K(m) = 0.49 μM and 2.9 μM for dehydroepiandrosterone and pregnenolone, respectively). JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00166480_v106_n3_p400_Pozzi
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic 3(or 17)beta hydroxysteroid dehydrogenase
androstenedione
isomerase
prasterone
pregnenolone
animal tissue
article
enzyme localization
enzyme substrate
hormone synthesis
microsome
mitochondrion
nonhuman
priority journal
steroidogenesis
testis
toad
spellingShingle 3(or 17)beta hydroxysteroid dehydrogenase
androstenedione
isomerase
prasterone
pregnenolone
animal tissue
article
enzyme localization
enzyme substrate
hormone synthesis
microsome
mitochondrion
nonhuman
priority journal
steroidogenesis
testis
toad
Pozzi, A.G.
Lantos, C.P.
Ceballos, N.R.
Subcellular localization of 3β hydroxysteroid dehydrogenase isomerase in testis of Bufo arenarum H.
topic_facet 3(or 17)beta hydroxysteroid dehydrogenase
androstenedione
isomerase
prasterone
pregnenolone
animal tissue
article
enzyme localization
enzyme substrate
hormone synthesis
microsome
mitochondrion
nonhuman
priority journal
steroidogenesis
testis
toad
description 3β-hydroxysteroid dehydrogenase 5-ene isomerase (3βHSD/I) catalyzes an essential step in the biosynthesis of steroid hormones and is usually considered to be mainly microsomal, although there is a dual distribution of the enzyme in toad interrenals. The present study demonstrates that in the testicular tissue, as in interrenals of Bufo arenarum H., 3βHSD/I is both mitochondrial and microsomal. The conversion of dehydroepiandrosterone to androstenedione takes place only in microsomes while pregnenolone is converted to progesterone in both microsomes and mitochondria. Kinetic constants of 3βHSD/I were determined by the oxidation of pregnenolone and dehydroepiandrosterone. The preferred substrate of the microsomal 3βHSD/I enzyme was dehydroepiandrosterone (K(m) = 0.17 μM and 0.53 μM for dehydroepiandrosterone and pregnenolone, respectively) not only during the breeding season but also in the nonbreeding period (K(m) = 0.49 μM and 2.9 μM for dehydroepiandrosterone and pregnenolone, respectively).
format JOUR
author Pozzi, A.G.
Lantos, C.P.
Ceballos, N.R.
author_facet Pozzi, A.G.
Lantos, C.P.
Ceballos, N.R.
author_sort Pozzi, A.G.
title Subcellular localization of 3β hydroxysteroid dehydrogenase isomerase in testis of Bufo arenarum H.
title_short Subcellular localization of 3β hydroxysteroid dehydrogenase isomerase in testis of Bufo arenarum H.
title_full Subcellular localization of 3β hydroxysteroid dehydrogenase isomerase in testis of Bufo arenarum H.
title_fullStr Subcellular localization of 3β hydroxysteroid dehydrogenase isomerase in testis of Bufo arenarum H.
title_full_unstemmed Subcellular localization of 3β hydroxysteroid dehydrogenase isomerase in testis of Bufo arenarum H.
title_sort subcellular localization of 3β hydroxysteroid dehydrogenase isomerase in testis of bufo arenarum h.
url http://hdl.handle.net/20.500.12110/paper_00166480_v106_n3_p400_Pozzi
work_keys_str_mv AT pozziag subcellularlocalizationof3bhydroxysteroiddehydrogenaseisomeraseintestisofbufoarenarumh
AT lantoscp subcellularlocalizationof3bhydroxysteroiddehydrogenaseisomeraseintestisofbufoarenarumh
AT ceballosnr subcellularlocalizationof3bhydroxysteroiddehydrogenaseisomeraseintestisofbufoarenarumh
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