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KMID : 0894520060100020127
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Development & Reproduction
2006 Volume.10 No. 2 p.127 ~ p.133
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Characterization of Ovarian Cytochrome P450C17 (17α-hydroxylase/17,20-lyase) in Rana dybowski
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Kang Hae-Mook
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Abstract
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17α-hydroxylase/17,20-lyase(P450C17) is the key enzyme mediating the conversion of progesterone to 17α -hydroxyprogesterone, ultimately to androstenedione during steroidogenesis. R. dybowskii’s ovarian P450C17 cDNA was cloned to understand the regulatory mechanism of ovarian steroidogenic pathway at the molecular level in amphibian. A 2.5kb cDNA clone encoding a single open-reading frame with a 519 deduced amino acid was isolated with the screening of ovarian cDNA library. This sequence contained the three highly conserved domains as seen in P450C17 of other species. The comparison of amino acid sequence of Rana P450C17 with other animal’s P450C17 showed relatively high identity with 76% in Xenopus, 63% in chicken, 60% in rainbow trout, and 45% in human. Phylogenic analysis also indicated that Rana P450C17 gene was evolutionary well conserved among vertebrate. Northern analysis indicated that the two different sizes of P450C17 transcripts with approximately 2.5 and 3.6kb were detected in ovary tissue, but not in other tissues. The expression vector of Rana P450C17 clearly showed the 17α-hydroxylase activity converting the exogenous progesterone into 17α-hydroxyprogesterone in the nonsteroidogenic COS-1 cells. Therefore, Rana P450C17 cDNA is very useful to investigate the molecular mechanism of the ovarian steroidogenesis in amphibian.
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KEYWORD
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P450SUB>C17, Steroidogenesis, Ovary, Amphibian
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