Reference : Species and tissue-independent rapid regulation of aromatase activity by phosphorylations.
Scientific congresses and symposiums : Paper published in a journal
Life sciences : Anatomy (cytology, histology, embryology...) & physiology
http://hdl.handle.net/2268/35049
Species and tissue-independent rapid regulation of aromatase activity by phosphorylations.
English
Charlier, Thierry mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Biologie de la différenciation sexuelle du cerveau >]
Harada, Nobuhiro [ > > ]
Ball, Gregory F. [ > > ]
Balthazart, Jacques mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Biologie de la différenciation sexuelle du cerveau >]
2009
Acta Neurologica Belgica
Acta Medica Belgica
32
No
National
0300-9009
Bruxelles
Belgique
8th Bi-Annual meeting of the Belgian Society for Neurosciences
Liège
Belgium
[en] Aromatase activity (AA) is rapidly inhibited in male quail brains, following expression of sexual behavior, activation of glutamatergic receptors or exposure to phosphorylating conditions. Questions remain as to whether direct aromatase phosphorylation is the common key regulatory mechanism and whether these inhibitions are specific to quail hypothalamus. We now showed that AA is rapidly downregulated in quail ovary homogenates incubated in phosphorylating conditions, similarly to what is observed in hypothalamic homogenates. To understand the processes underlying this control, we expressed human aromatase in the human cell line HEK293 and 1) researched whether human aromatase can also be rapidly modulated by phosphorylations and 2) investigated more precisely the processes involved in this rapid control of activity. AA in HEK293 was rapidly inhibited following depolarization of intact cells with 100 mM KCl or in cell lysates exposed to phosphorylating conditions. Thus inhibition of AA in phosphorylating conditions is not unique to the quail hypothalamus neural environment but seems to be a general process. We are now defining the contribution of single residues of the aromatase protein to this enzymatic control.
http://hdl.handle.net/2268/35049

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Restricted access
BSN Thierry1 - JB.docAuthor postprint24.5 kBRequest copy

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.