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1: Biochim Biophys Acta. 2003 Feb 20;1625(3):229-38.Click here to read Links

Molecular characterization and expression of equine testicular cytochrome P450 aromatase.

Seralini GE, Tomilin A, Auvray P, Nativelle-Serpentini C, Sourdaine P, Moslemi S.

Laboratory of Biochemistry and Molecular Biology, EA 2608, IBBA, University of Caen, Esplanade de la Paix, 14032 Caen Cedex, France. bioch.bio.mol@ibba.unicaen.fr

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.

PMID: 12591609 [PubMed - indexed for MEDLINE]