5α-Reductase, an enzyme regulating glucocorticoid action in the testis of Rhinella arenarum (Amphibia: Anura)
The reduction of A-ring of glucocorticoids to produce 5α-dihydro-derivatives by 5α-reductases has been considered as a pathway of irreversible inactivation. However, 5α-reduced metabolites of corticosterone and testosterone have significant biological activity. In this paper, we investigated whether...
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Academic Press Inc.
2012
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| 005 | 20230518203938.0 | ||
| 008 | 190411s2012 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-84859914893 | |
| 024 | 7 | |2 cas |a corticosterone, 50-22-6; dexamethasone, 50-02-2; steroid 5alpha reductase; testosterone, 58-22-0 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a GCENA | ||
| 100 | 1 | |a Tesone, A.J. | |
| 245 | 1 | 0 | |a 5α-Reductase, an enzyme regulating glucocorticoid action in the testis of Rhinella arenarum (Amphibia: Anura) |
| 260 | |b Academic Press Inc. |c 2012 | ||
| 270 | 1 | 0 | |m Ceballos, N.R.; Laboratorio de Endocrinología Comparada, Dept. de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, Univ. de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas, Buenos Aires, Argentina; email: nceballo@bg.fcen.uba.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a The reduction of A-ring of glucocorticoids to produce 5α-dihydro-derivatives by 5α-reductases has been considered as a pathway of irreversible inactivation. However, 5α-reduced metabolites of corticosterone and testosterone have significant biological activity. In this paper, we investigated whether toad testicular 5α-reductase (5α-Red) is able to transform corticosterone into 5α-dihydrocorticosterone. Furthermore, we studied the role of 5α-reduced metabolite of corticosterone as a glucocorticoid receptor (GR) agonist. The activity of 5α-Red was assayed in subcellular fractions with [3H]corticosterone or [3H]testosterone as substrate. The enzyme localizes in microsomes and its optimal pH is between 7 and 8. The activity is not inhibited by finasteride. These results support the conclusion that toad 5α-Red resembles mammalian type 1 isoenzyme. Kinetic studies indicate that neither Km nor Vmax for both corticosterone and testosterone were significantly different among reproductive periods. The Km value for testosterone was significantly higher than that for corticosterone, indicating that the C-21 steroid is the preferred substrate for the enzyme. Studies of the binding capacity of 5α-dihydrocorticosterone (5α-DHB) to the testicular GR show that 5α-DHB is able to displace the binding of [3H]dexamethasone to testicular cytosol with a similar potency than corticosterone. The inhibition constant (Ki) values for corticosterone and 5α-DHB were similar, 31.33±2.9nM and 35.24±2.3nM, respectively. In vitro experiments suggest that 5α-DHB is an agonist of toad testicular GR, decreasing the activity of the key enzyme for androgen synthesis, the cytochrome P450 17-hydroxylase, C17,20-lyase. © 2012 Elsevier Inc. |l eng | |
| 536 | |a Detalles de la financiación: Universidad de Buenos Aires, UBACyT X042 | ||
| 536 | |a Detalles de la financiación: National Council for Scientific Research, PIP 2433 | ||
| 536 | |a Detalles de la financiación: This work was supported by grants from The University of Buenos Aires (UBACyT X042) and The National Research Council of Argentina (PIP 2433). The experiments comply with de “Principles of animal care”, publication No. 86-23, and revised 1985 of the National Institute of Health and also with the argentine laws. | ||
| 593 | |a Laboratorio de Endocrinología Comparada, Dept. de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, Univ. de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas, Buenos Aires, Argentina | ||
| 593 | |a Laboratorio de Neuroendocrinología Comparada, Inst. de Investigaciones Biotecnológicas-Inst. Tecnológico Chascomus (IIB-INTECH), Consejo Nacional de Investigaciones Cientificas y Tecnicas, Univ. Nacional de General San Martin, Chascomús, Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a 5Α-REDUCTASE |
| 690 | 1 | 0 | |a ANDROGENS |
| 690 | 1 | 0 | |a GLUCOCORTICOID-RECEPTOR |
| 690 | 1 | 0 | |a TOAD TESTES |
| 690 | 1 | 0 | |a 5ALPHA DIHYDROCORTICOSTERONE |
| 690 | 1 | 0 | |a CORTICOSTERONE |
| 690 | 1 | 0 | |a DEXAMETHASONE |
| 690 | 1 | 0 | |a GLUCOCORTICOID |
| 690 | 1 | 0 | |a GLUCOCORTICOID RECEPTOR |
| 690 | 1 | 0 | |a STEROID 5ALPHA REDUCTASE |
| 690 | 1 | 0 | |a TESTOSTERONE |
| 690 | 1 | 0 | |a UNCLASSIFIED DRUG |
| 690 | 1 | 0 | |a ANIMAL TISSUE |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a BINDING AFFINITY |
| 690 | 1 | 0 | |a BIOTRANSFORMATION |
| 690 | 1 | 0 | |a CONTROLLED STUDY |
| 690 | 1 | 0 | |a CYTOSOL |
| 690 | 1 | 0 | |a ENZYME ACTIVITY |
| 690 | 1 | 0 | |a ENZYME KINETICS |
| 690 | 1 | 0 | |a ENZYME LOCALIZATION |
| 690 | 1 | 0 | |a ENZYME SUBSTRATE |
| 690 | 1 | 0 | |a FROGS AND TOADS |
| 690 | 1 | 0 | |a HORMONE ACTION |
| 690 | 1 | 0 | |a HORMONE RECEPTOR INTERACTION |
| 690 | 1 | 0 | |a IN VITRO STUDY |
| 690 | 1 | 0 | |a MALE |
| 690 | 1 | 0 | |a MICROSOME |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a REPRODUCTION |
| 690 | 1 | 0 | |a RHINELLA ARENARUM |
| 690 | 1 | 0 | |a TESTIS |
| 650 | 1 | 7 | |2 spines |a PH |
| 700 | 1 | |a Regueira, E. | |
| 700 | 1 | |a Fabián Canosa, L. | |
| 700 | 1 | |a Ceballos, N.R. | |
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