Contrasting effects of sn-1,2-dioctanoyl glycerol as compared to other protein kinase C activators in adrenal glomerulosa cells
Author
dc.contributor.author
Lobo, Maria V.
Author
dc.contributor.author
Marusic, Elisa
Admission date
dc.date.accessioned
2019-01-29T15:47:30Z
Available date
dc.date.available
2019-01-29T15:47:30Z
Publication date
dc.date.issued
1991
Cita de ítem
dc.identifier.citation
Journal of Steroid Biochemistry and Molecular Biology, Volumen 39, Issue 3, 2018, Pages 323-327
Identifier
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09600760
Identifier
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10.1016/0960-0760(91)90042-4
Identifier
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https://repositorio.uchile.cl/handle/2250/162379
Abstract
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Angiotensin II acts on adrenal glomerulosa cells to induce the phospholipase C-mediated generation of inositol trisphosphate and sn-1,2-diacyglycerol as the major products of inositol phospholipid breakdown. This last product is known to activate protein kinase C, but its role in the action of angiotensin II on steroidogenesis has not been defined. We report herein that, in bovine adrenal glomerulosa cells, protein kinase C activators, such as phorbol 12,13-dibutyrate, 12-O-tetradecanoylphorbol-13-acetate, mezerein and sn 1,2 oleoyl acetoylglycerol, each failed to increase steroidogenesis. These results contrast with our recent report on the enhancement of aldosterone output by sn-1,2-dioctanoylglycerol (DiC8) [J. Steroid Biochem. 35 (1990) 19-33]. In addition, the difference between DiC8 and the other protein kinase activators was also observed in the pattern of 86Rb efflux from preloaded glomerulosa cells; only DiC8 mimicked the effect of angiotensin II on ion fluxes. Furthermore, st