pubmed-article:1831673 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1831673 | lifeskim:mentions | umls-concept:C1135183 | lld:lifeskim |
pubmed-article:1831673 | lifeskim:mentions | umls-concept:C0205252 | lld:lifeskim |
pubmed-article:1831673 | lifeskim:mentions | umls-concept:C0023602 | lld:lifeskim |
pubmed-article:1831673 | lifeskim:mentions | umls-concept:C0036536 | lld:lifeskim |
pubmed-article:1831673 | lifeskim:mentions | umls-concept:C0036537 | lld:lifeskim |
pubmed-article:1831673 | lifeskim:mentions | umls-concept:C0039601 | lld:lifeskim |
pubmed-article:1831673 | lifeskim:mentions | umls-concept:C0011185 | lld:lifeskim |
pubmed-article:1831673 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:1831673 | lifeskim:mentions | umls-concept:C0100748 | lld:lifeskim |
pubmed-article:1831673 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
pubmed-article:1831673 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:1831673 | pubmed:dateCreated | 1991-9-27 | lld:pubmed |
pubmed-article:1831673 | pubmed:abstractText | In the present study, we evaluated the effect of the homodimer activin A on immature porcine Leydig cell functions in primary culture. Activin A (0.5-100 ng/ml) reduced hCG-stimulated dehydroepiandrosterone (DHEA) accumulation in a dose- and time-dependent manner, with a maximal inhibitory effect (58% decrease) at 20 ng/ml (8 x 10(-10) M). Activin A was found not to control steroidogenesis, either through a modulation of the gonadotropin LH/hCG binding or low-density lipoprotein cholesterol binding and internalization. However, activin A significantly decreased pregnenolone (p less than 0.002) and DHEA (p less than 0.001) formation (evaluated in the presence of 10(-5) M of WIN 24540, an inhibitor of 3 beta-hydroxysteroid dehydrogenase/isomerase [3 beta-HSDI]activity) in Leydig cells maximally stimulated with hCG (3 ng/ml, 3 h) or incubated in the presence of 22R-hydroxycholesterol (5 micrograms/ml, 2 h). These findings indicate that activin A probably exerts a partial inhibitory effect on cholesterol side-chain cleavage cytochrome P450 (P450scc) activity. On the other hand, activin A significantly (p less than 0.001) enhanced the conversion of exogenous pregnenolone and DHEA (500 ng/ml) but not of progesterone and androstenedione (500 ng/ml) into testosterone, suggesting that activin A potentially enhances 3 beta-HSDI activity in Leydig cells. Activin A action on 3 beta-HSDI activity was found to be closely related to that of transforming growth factor-beta 1 (TGF beta 1), since both activin A (20 ng/ml) and TGF beta 1 (2 ng/ml) induced a comparable and non-additive increase in 3 beta-HSDI activity.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
pubmed-article:1831673 | pubmed:language | eng | lld:pubmed |
pubmed-article:1831673 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1831673 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1831673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1831673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1831673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1831673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1831673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1831673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1831673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1831673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1831673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1831673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1831673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1831673 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1831673 | pubmed:month | Jul | lld:pubmed |
pubmed-article:1831673 | pubmed:issn | 0006-3363 | lld:pubmed |
pubmed-article:1831673 | pubmed:author | pubmed-author:MoreraA MAM | lld:pubmed |
pubmed-article:1831673 | pubmed:author | pubmed-author:de PerettiEE | lld:pubmed |
pubmed-article:1831673 | pubmed:author | pubmed-author:BenahmedMM | lld:pubmed |
pubmed-article:1831673 | pubmed:author | pubmed-author:ChauvinM AMA | lld:pubmed |
pubmed-article:1831673 | pubmed:author | pubmed-author:MauduitCC | lld:pubmed |
pubmed-article:1831673 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1831673 | pubmed:volume | 45 | lld:pubmed |
pubmed-article:1831673 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1831673 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1831673 | pubmed:pagination | 101-9 | lld:pubmed |
pubmed-article:1831673 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:1831673 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1831673 | pubmed:articleTitle | Effect of activin A on dehydroepiandrosterone and testosterone secretion by primary immature porcine Leydig cells. | lld:pubmed |
pubmed-article:1831673 | pubmed:affiliation | INSERM CJF n. 90-08, Hôpital Sainte Eugénie, Centre Hospitalier Lyon-Sud, Pierre-Bénite, France. | lld:pubmed |
pubmed-article:1831673 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1831673 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |