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Molecular characterization and expression of equine testicular cytochrome P450 aromatase*1

TitreMolecular characterization and expression of equine testicular cytochrome P450 aromatase*1
Type de publicationJournal Article
Year of Publication2003
AuteursSeralini, G-E, Tomilin, A, Auvray, P, Nativelle-Serpentini, C, Sourdaine, P, Moslemi, S
JournalBiochimica et Biophysica Acta (BBA) – Gene Structure and Expression
Volume1625
Pagination229–238
Résumé

We characterized testicular equine aromatase and its expression. A 2707 bp cDNA was isolated, it encoded a polypeptide of 503 residues with a deduced molecular mass of 57.8 kDa. The sequence features were those of a cytochrome P450 aromatase, with a 78% polypeptide identity with the human counterpart. The gene has a minimal length of 74 kb comprising at least 9 exons and expresses a 2.8 kb mRNA in the testis. Transient cDNA transfections in E293 cells and in vitro translations in a reticulocyte lysate system allowed aromatase protein and activity detections. The activity increased with androstenedione as substrate in a dose-dependent manner. The isolation of testicular aromatase by a new immunoaffinity method demonstrated that the protein could exist either glycosylated or not with a 2 kDa difference. All these results taken together allow new structural studies to progress in the understanding of this cytochrome P450.