|Titre||Molecular characterization and expression of equine testicular cytochrome P450 aromatase*1|
|Type de publication||Journal Article|
|Year of Publication||2003|
|Auteurs||Seralini, G-E, Tomilin, A, Auvray, P, Nativelle-Serpentini, C, Sourdaine, P, Moslemi, S|
|Journal||Biochimica et Biophysica Acta (BBA) – Gene Structure and Expression|
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.