Signal transduction mechanisms involved in carbachol-induced aldosterone secretion from bovine adrenal glomerulosa cells

Wendy B. Bollag, Paula Q. Barrett, Carlos M. Isales, Mordechai Liscovitch, Howard Rasmussen

Research output: Contribution to journalArticle

13 Scopus citations


In cultured bovine adrenal glomerulosa cells, diacylglycerol content remains elevated for up to 75 min following the removal of angiotensin II. This maintained increase could provide a mechanism by which angiotensin II pretreatment may prime cells to secrete aldosterone in response to the calcium channel agonist Bay K 8644. In the present study we find that carbachol failed both to produce this persistent diacylglycerol elevation and to exert a priming effect. In addition, because carbachol was also a less potent activator of phospholipase D than angiotensin II, our results implicate phospholipase D in the maintained increase in diacylglycerol content observed following stimulation with and removal of angiotensin II. Carbachol also elicited changes in the radiolabeled levels of both myristate- and arachidonate-containing diacylglycerol. However, the rapid decline in diacylglycerol content following carbachol removal resembled the rapid fall in arachidonate-diacylglycerol; we therefore proposed that the diacylglycerol species generated with carbachol stimulation contains predominantly arachidonic acid. In summary, our results suggest that prolonged elevations in diacylglycerol content following removal of hormones such as angiotensin II, as well as the identity of the diacylglycerol species itself, may be important in the regulation of cellular responses.

Original languageEnglish (US)
Pages (from-to)93-101
Number of pages9
JournalMolecular and Cellular Endocrinology
Issue number1-2
Publication statusPublished - Jul 1992
Externally publishedYes



  • Aldosterone secretion
  • Angiotensin II
  • Carbachol
  • Diacylglycerol
  • Glomerulosa cell

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Endocrinology

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