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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2004-12-16
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
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...
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
146
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
186-94
pubmed:dateRevised
2006-11-15
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...
pubmed:year
2005
pubmed:articleTitle
Gonadotropin-induced delta14-reductase and delta7-reductase gene expression in cumulus cells during meiotic resumption of porcine oocytes.
pubmed:affiliation
Department of Applied Animal Science, Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima, Hiroshima 739-8528, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't