Local modulation of steroid action: rapid control of enzymatic activity
Estrogens can induce rapid, short-lived physiological and behavioral responses, in addition to their slow, but long-term, effects at the transcriptional level. To be functionally relevant, these effects should be associated with rapid modulations of estrogens concentrations. 17beta-estradiol is synt...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2015-03-01
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| Series: | Frontiers in Neuroscience |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fnins.2015.00083/full |
| _version_ | 1811331116602228736 |
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| author | Thierry D Charlier Charlotte A Cornil Christine ePatte-Mensah Laurence eMeyer A Guy Mensah-Nyagan Jacques eBalthazart |
| author_facet | Thierry D Charlier Charlotte A Cornil Christine ePatte-Mensah Laurence eMeyer A Guy Mensah-Nyagan Jacques eBalthazart |
| author_sort | Thierry D Charlier |
| collection | DOAJ |
| description | Estrogens can induce rapid, short-lived physiological and behavioral responses, in addition to their slow, but long-term, effects at the transcriptional level. To be functionally relevant, these effects should be associated with rapid modulations of estrogens concentrations. 17beta-estradiol is synthesized by the enzyme aromatase, using testosterone as a substrate, but can also be degraded into catechol-estrogens via hydroxylation by the same enzyme, leading to an increase or decrease in estrogens concentration, respectively. The first evidence that aromatase activity (AA) can be rapidly modulated came from experiments performed in Japanese quail hypothalamus homogenates. This rapid modulation is triggered by calcium-dependent phosphorylations and was confirmed in other tissues and species. The mechanisms controlling the phosphorylation status, the targeted amino acid residues and the reversibility seem to vary depending of the tissues and is discussed in this review. We currently do not know whether the phosphorylation of the same amino acid affects both aromatase and/or hydroxylase activities or whether these residues are different. These processes provide a new general mechanism by which local estrogen concentration can be rapidly altered in the brain and other tissues. |
| first_indexed | 2024-04-13T16:14:17Z |
| format | Article |
| id | doaj.art-c5a8c11b183944d79667ccad27e55f43 |
| institution | Directory Open Access Journal |
| issn | 1662-453X |
| language | English |
| last_indexed | 2024-04-13T16:14:17Z |
| publishDate | 2015-03-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Neuroscience |
| spelling | doaj.art-c5a8c11b183944d79667ccad27e55f432022-12-22T02:40:06ZengFrontiers Media S.A.Frontiers in Neuroscience1662-453X2015-03-01910.3389/fnins.2015.00083126900Local modulation of steroid action: rapid control of enzymatic activityThierry D Charlier0Charlotte A Cornil1Christine ePatte-Mensah2Laurence eMeyer3A Guy Mensah-Nyagan4Jacques eBalthazart5University of Rennes1University of LiegeUniversity of StrasbourgUniversity of StrasbourgUniversity of StrasbourgUniversity of LiegeEstrogens can induce rapid, short-lived physiological and behavioral responses, in addition to their slow, but long-term, effects at the transcriptional level. To be functionally relevant, these effects should be associated with rapid modulations of estrogens concentrations. 17beta-estradiol is synthesized by the enzyme aromatase, using testosterone as a substrate, but can also be degraded into catechol-estrogens via hydroxylation by the same enzyme, leading to an increase or decrease in estrogens concentration, respectively. The first evidence that aromatase activity (AA) can be rapidly modulated came from experiments performed in Japanese quail hypothalamus homogenates. This rapid modulation is triggered by calcium-dependent phosphorylations and was confirmed in other tissues and species. The mechanisms controlling the phosphorylation status, the targeted amino acid residues and the reversibility seem to vary depending of the tissues and is discussed in this review. We currently do not know whether the phosphorylation of the same amino acid affects both aromatase and/or hydroxylase activities or whether these residues are different. These processes provide a new general mechanism by which local estrogen concentration can be rapidly altered in the brain and other tissues.http://journal.frontiersin.org/Journal/10.3389/fnins.2015.00083/fullAromataseHypothalamusPhosphorylationNeurosteroidogenesiscatechol-estrogens17B-estradiol |
| spellingShingle | Thierry D Charlier Charlotte A Cornil Christine ePatte-Mensah Laurence eMeyer A Guy Mensah-Nyagan Jacques eBalthazart Local modulation of steroid action: rapid control of enzymatic activity Frontiers in Neuroscience Aromatase Hypothalamus Phosphorylation Neurosteroidogenesis catechol-estrogens 17B-estradiol |
| title | Local modulation of steroid action: rapid control of enzymatic activity |
| title_full | Local modulation of steroid action: rapid control of enzymatic activity |
| title_fullStr | Local modulation of steroid action: rapid control of enzymatic activity |
| title_full_unstemmed | Local modulation of steroid action: rapid control of enzymatic activity |
| title_short | Local modulation of steroid action: rapid control of enzymatic activity |
| title_sort | local modulation of steroid action rapid control of enzymatic activity |
| topic | Aromatase Hypothalamus Phosphorylation Neurosteroidogenesis catechol-estrogens 17B-estradiol |
| url | http://journal.frontiersin.org/Journal/10.3389/fnins.2015.00083/full |
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