Phorbol ester increases mitochondrial cholesterol content in NCI H295R cells

Wendy B. Bollag, Patricia Kent, Stephanie White, Mariya V. Wilson, Carlos M. Isales, Roberto A. Calle

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

The first step in steroidogenesis is cholesterol mobilization from cytosolic lipid droplets to the initiating rate-limiting enzyme complex located on the inner mitochondrial membrane. Angiotensin II (AngII), the primary agonist of aldosterone secretion from adrenal glomerulosa cells, is known to induce cholesterol mobilization to mitochondria. However, the role of the protein kinase C (PKC) pathway in mediating cholesterol mobilization is unknown. To determine PKC's involvement, human adrenocortical carcinoma cells were incubated with or without PKC-activating phorbol 12-myristate 13-acetate (PMA) and mitochondrial cholesterol content assayed. Like AngII, PMA significantly elevated mitochondrial cholesterol content as well as aldosterone secretion. Thus, PKC may play a role in cholesterol mobilization to mitochondria and hence steroid production. Atrial natriuretic peptide (ANP) inhibited both AngII- and PMA-stimulated mitochondrial cholesterol content. These findings suggest that the ability of ANP to inhibit steroidogenesis induced by multiple agents may be related to its capacity to reduce cholesterol mobilization.

Original languageEnglish (US)
Pages (from-to)53-57
Number of pages5
JournalMolecular and Cellular Endocrinology
Volume296
Issue number1-2
DOIs
StatePublished - Dec 16 2008

Keywords

  • 12-O-tetradecanoylphorbol 13-acetate
  • Aldosterone secretion
  • Human adrenocortical carcinoma cells
  • NCI H295R cells
  • Phorbol 12-myristate 13-acetate
  • Steroidogenesis

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Endocrinology

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