Source:http://linkedlifedata.com/resource/pubmed/id/15459117
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2004-12-16
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pubmed:abstractText |
Progesterone is produced from cholesterol in cumulus cells during meiotic resumption of porcine oocytes. In follicular cells, it has been shown that exogenous lipoprotein-bound cholesterol ester can be used for steroid hormone production. However, in serum-free medium, progesterone is also secreted by FSH- and LH-stimulated cumulus-oocyte complexes, suggesting that progesterone could be produced from de novo synthesized cholesterol in cumulus cells. In the present study, we investigated the expression of Delta14-reductase and Delta7-reductase, which are the members of the superfamily that converts acetyl-CoA to cholesterol in cumulus cells. The expression of both genes was analyzed by RT-PCR. Both Delta14-reductase mRNA and Delta7-reductase mRNA in cumulus cells, cultured until 4 h, were under the level of detection limit. In response to gonadotropins, both mRNA levels were dramatically up-regulated, reaching a maximum at 20 h. To clarify the role of induced enzymes in cumulus cells, cumulus-oocyte complexes were cultured with either Delta14-reductase inhibitor, AY9944-A-7, or Delta7-reductase inhibitor, BM15.766. The results indicated that these inhibitors significantly suppressed the progesterone production in cumulus cells and meiotic progression of oocytes. The inhibitory effects reached a maximum at 1 microM AY9944-A-7 or 20 microM BM15.766. The addition of 20 ng/ml progesterone overcame the inhibitory effects of both drugs on meiotic resumption of oocytes. These results imply that gonadotropin-induced expression and function of Delta14-reductase and Delta7-reductase in cumulus cells contribute to oocyte meiotic resumption via a progesterone-dependent pathway.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/BM 15766,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Follicle Stimulating Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Luteinizing Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases Acting on CH-CH...,
http://linkedlifedata.com/resource/pubmed/chemical/Piperazines,
http://linkedlifedata.com/resource/pubmed/chemical/Progesterone,
http://linkedlifedata.com/resource/pubmed/chemical/delta(14)-sterol reductase,
http://linkedlifedata.com/resource/pubmed/chemical/lathosterol delta-5-dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/trans-1,4-Bis(2-chlorobenzaminomethy...
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0013-7227
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
146
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
186-94
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15459117-Amino Acid Sequence,
pubmed-meshheading:15459117-Animals,
pubmed-meshheading:15459117-Apoptosis,
pubmed-meshheading:15459117-Culture Media,
pubmed-meshheading:15459117-Enzyme Inhibitors,
pubmed-meshheading:15459117-Female,
pubmed-meshheading:15459117-Follicle Stimulating Hormone,
pubmed-meshheading:15459117-Gene Expression,
pubmed-meshheading:15459117-Luteinizing Hormone,
pubmed-meshheading:15459117-Meiosis,
pubmed-meshheading:15459117-Molecular Sequence Data,
pubmed-meshheading:15459117-Oocytes,
pubmed-meshheading:15459117-Ovarian Follicle,
pubmed-meshheading:15459117-Oxidoreductases,
pubmed-meshheading:15459117-Oxidoreductases Acting on CH-CH Group Donors,
pubmed-meshheading:15459117-Piperazines,
pubmed-meshheading:15459117-Progesterone,
pubmed-meshheading:15459117-Swine,
pubmed-meshheading:15459117-Time Factors,
pubmed-meshheading:15459117-trans-1,4-Bis(2-chlorobenzaminomethyl)cyclohexane...
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pubmed:year |
2005
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pubmed:articleTitle |
Gonadotropin-induced delta14-reductase and delta7-reductase gene expression in cumulus cells during meiotic resumption of porcine oocytes.
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pubmed:affiliation |
Department of Applied Animal Science, Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima, Hiroshima 739-8528, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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