Synaptopodin is regulated by aromatase activity
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Synaptopodin is regulated by aromatase activity. / Fester, Lars; Zhou, Lepu; Ossig, Christiana; Labitzke, Jan; Bläute, Corinna; Bader, Manuela; Vollmer, Günter; Jarry, Hubertus; Rune, Gabriele M.
in: J NEUROCHEM, Jahrgang 140, Nr. 1, 01.2017, S. 126-139.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Synaptopodin is regulated by aromatase activity
AU - Fester, Lars
AU - Zhou, Lepu
AU - Ossig, Christiana
AU - Labitzke, Jan
AU - Bläute, Corinna
AU - Bader, Manuela
AU - Vollmer, Günter
AU - Jarry, Hubertus
AU - Rune, Gabriele M
N1 - © 2016 International Society for Neurochemistry.
PY - 2017/1
Y1 - 2017/1
N2 - Locally synthesized estradiol plays an important role in synaptic plasticity in the hippocampus. We have previously shown that in hippocampal neurons, activity of the enzyme aromatase, which converts testosterone into estradiol, is reduced via Ca(2+) -dependent phosphorylation. Synaptopodin is a highly estrogen responsive protein, and it has been shown that it is an important regulator of synaptic plasticity, mediated by its close association with internal calcium stores. In this study, we show that the expression of synaptopodin is stronger in the hippocampus of female animals than in that of male animals. Phosphorylation of aromatase, using letrozole, however, down-regulates synaptopodin immunohistochemistry in the hippocampus of both male and females. Similarly, in aromatase knock-out mice synaptopodin expression in the hippocampus is reduced sex independently. Using primary-dissociated hippocampal neurons, we found that evoked release of Ca(2+) from internal stores down-regulates aromatase activity, which is paralleled by reduced expression of synaptopodin. Opposite effects were achieved after inhibition of the release. Calcium-dependent regulation of synaptopodin expression was abolished when the control of aromatase activity by the Ca(2+) transients was disrupted. Our data suggest that the regulation of aromatase activity by Ca(2+) transients in neurons contributes to synaptic plasticity in the hippocampus of male and female animals as an on-site regulatory mechanism.
AB - Locally synthesized estradiol plays an important role in synaptic plasticity in the hippocampus. We have previously shown that in hippocampal neurons, activity of the enzyme aromatase, which converts testosterone into estradiol, is reduced via Ca(2+) -dependent phosphorylation. Synaptopodin is a highly estrogen responsive protein, and it has been shown that it is an important regulator of synaptic plasticity, mediated by its close association with internal calcium stores. In this study, we show that the expression of synaptopodin is stronger in the hippocampus of female animals than in that of male animals. Phosphorylation of aromatase, using letrozole, however, down-regulates synaptopodin immunohistochemistry in the hippocampus of both male and females. Similarly, in aromatase knock-out mice synaptopodin expression in the hippocampus is reduced sex independently. Using primary-dissociated hippocampal neurons, we found that evoked release of Ca(2+) from internal stores down-regulates aromatase activity, which is paralleled by reduced expression of synaptopodin. Opposite effects were achieved after inhibition of the release. Calcium-dependent regulation of synaptopodin expression was abolished when the control of aromatase activity by the Ca(2+) transients was disrupted. Our data suggest that the regulation of aromatase activity by Ca(2+) transients in neurons contributes to synaptic plasticity in the hippocampus of male and female animals as an on-site regulatory mechanism.
U2 - 10.1111/jnc.13889
DO - 10.1111/jnc.13889
M3 - SCORING: Journal article
C2 - 27861893
VL - 140
SP - 126
EP - 139
JO - J NEUROCHEM
JF - J NEUROCHEM
SN - 0022-3042
IS - 1
ER -