Human chorionic gonadotropin and free beta subunits stimulate phospholipid methylation in intact rat Leydig cells
Author
dc.contributor.author
Ronco Macchiavello, Ana María
Author
dc.contributor.author
Llanos Silva, Miguel
Author
dc.contributor.author
Valladares Boasi, Luis
Admission date
dc.date.accessioned
2019-01-29T14:51:20Z
Available date
dc.date.available
2019-01-29T14:51:20Z
Publication date
dc.date.issued
1993
Cita de ítem
dc.identifier.citation
Steroids, 1993, vol. 58, July
Identifier
dc.identifier.issn
0039128X
Identifier
dc.identifier.other
10.1016/0039-128X(93)90090-A
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/160993
Abstract
dc.description.abstract
The effect of human chorionic gonadotropin (hCG) on intact Leydig cell phospholipid methylation was
studied. Hormonal stimulation of rat Leydig cells increased the incorporation of[methyl-3H]methionine
into phospholipids threefold. This effect was observed after 10 minutes of incubation time and was
time and dose dependent with a maximal stimulation at 67 ng/ml of hCG. In the presence of hCG, 3Hlabeled
methyl groups were preferentially incorporated into phosphatidyl-N-monomethylethanolamine.
This effect of hCG was not reproduced by dibutyryl cyclic adenosine monophosphate (cAMP), cholera
toxin, or forskolin. Purified hCG[3 subunit but not hCGc~ subunit had stimulatory activity on Leydig
cell phospholipid methylation. We conclude that luteinizing hormone (LH)/hCG stimulates specifically
Leydig cell phospholipid methylation, because LH-releasing hormone or [ArgS]-vasopressin did not
modify these reactions. We postulate that these reactions are occurring at a cellular level that involves
hormone-receptor interaction. It is also suggested that this biological response involves hCG[3 subunit
receptor interaction and does not require cAMP synthesis.