| pubmed-article:8325965 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8325965 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8325965 | lifeskim:mentions | umls-concept:C0010762 | lld:lifeskim |
| pubmed-article:8325965 | lifeskim:mentions | umls-concept:C0038302 | lld:lifeskim |
| pubmed-article:8325965 | lifeskim:mentions | umls-concept:C0072084 | lld:lifeskim |
| pubmed-article:8325965 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:8325965 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8325965 | pubmed:dateCreated | 1993-8-6 | lld:pubmed |
| pubmed-article:8325965 | pubmed:abstractText | Progesterone and pregnenolone are metabolized to 17 alpha-hydroxysteroids by a cytochrome P450-dependent 17 alpha-hydroxylase (P450c17). The same enzyme can also catalyze the removal of the side-chain of these 17 alpha-hydroxylated steroids to yield androstenedione and dehydroepiandrosterone, respectively. We investigated the metabolism of progesterone by monkey kidney tumor (COS 1) cells transfected with a plasmid vector containing the cDNA encoding the complete amino acid sequence for human cytochrome P450c17. Transfected COS 1 cells converted progesterone to 17 alpha-hydroxyprogesterone as well as 16 alpha-hydroxyprogesterone, but no detectable androstenedione was produced. However, pregnenolone was converted to 17 alpha-hydroxypregnenolone and, ultimately, dehydroepiandrosterone. No 16 alpha-hydroxypregnenolone was produced. The kinetics of progesterone metabolism by the enzyme expressed in COS 1 cells indicated that both 17 alpha- and 16 alpha-hydroxylated products were products were produced from a common active site. Microsomes prepared from fetal adrenal and adult testis converted progesterone to 17 alpha-hydroxyprogesterone as well as 16 alpha-hydroxyprogesterone. No detectable androstenedione was produced by these preparations. Antibodies raised against porcine cytochrome P450c17 inhibited the 17 alpha- and 16 alpha-hydroxylation of progesterone to the same extent when using fetal adrenal microsomes, whereas no inhibition of 21-hydroxylation of progesterone was observed. Similar results were obtained with the imidazole antimycotic agent ketoconazole, which is a preferential cytochrome P450c17 inhibitor. From these results we conclude that human cytochrome P450c17 exhibits marked progesterone 16 alpha-hydroxylase activity in addition to its 17 alpha-hydroxylase function when expressed not only in a heterologous cell expression system but also, importantly, in human steroidogenic cells. Furthermore, the human enzyme has extremely low C-17,20-lyase activity toward progesterone, 17 alpha-hydroxyprogesterone, and 16 alpha-hydroxyprogesterone and fails to convert these to corresponding C19 steroids. | lld:pubmed |
| pubmed-article:8325965 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8325965 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:8325965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8325965 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8325965 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:8325965 | pubmed:issn | 0021-972X | lld:pubmed |
| pubmed-article:8325965 | pubmed:author | pubmed-author:EstabrookR... | lld:pubmed |
| pubmed-article:8325965 | pubmed:author | pubmed-author:WatermanM RMR | lld:pubmed |
| pubmed-article:8325965 | pubmed:author | pubmed-author:MasonJ IJI | lld:pubmed |
| pubmed-article:8325965 | pubmed:author | pubmed-author:SwartA CAC | lld:pubmed |
| pubmed-article:8325965 | pubmed:author | pubmed-author:StockR GRG | lld:pubmed |
| pubmed-article:8325965 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8325965 | pubmed:volume | 77 | lld:pubmed |
| pubmed-article:8325965 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8325965 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8325965 | pubmed:pagination | 98-102 | lld:pubmed |
| pubmed-article:8325965 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8325965 | pubmed:meshHeading | pubmed-meshheading:8325965-... | lld:pubmed |
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| pubmed-article:8325965 | pubmed:meshHeading | pubmed-meshheading:8325965-... | lld:pubmed |
| pubmed-article:8325965 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8325965 | pubmed:articleTitle | Progesterone 16 alpha-hydroxylase activity is catalyzed by human cytochrome P450 17 alpha-hydroxylase. | lld:pubmed |
| pubmed-article:8325965 | pubmed:affiliation | Cecil H. and Ida Green Center for Reproductive Biology Sciences, Departments of Biochemistry and Obstetrics and Gynecology, University of Texas Southwestern Medical Center, Dallas 75235. | lld:pubmed |
| pubmed-article:8325965 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8325965 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8325965 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8325965 | lld:pubmed |
