Molecular characterization and expression of equine testicular cytochrome P450 aromatase

被引：12

作者：

Seralini, GE ^{[1
]}

Tomilin, A ^{[1
]}

Auvray, P ^{[1
]}

Nativelle-Serpentini, C ^{[1
]}

Sourdaine, P ^{[1
]}

Moslemi, S ^{[1
]}

机构：

[1] Univ Caen, Biochem & Mol Biol Lab, IBBA, EA 2608, F-14032 Caen, France

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 2003年 / 1625卷 / 03期

关键词：

aromatase; cytochrome P450; horse; testis; cDNA cloning; steroid;

D O I：

10.1016/S0167-4781(02)00621-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2003 Elsevier Science B.V. All rights reserved.

引用

页码：229 / 238

页数：10

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