Abstract
Atrial natriuretic peptide (ANP) is a cardiac hormone that inhibits aldosterone secretion induced by all physiologic agonists. The purpose of this study is to explore ANP-induced changes in the phosphorylation of myristoylated alanine-rich C-kinase substrate (MARCKS) and the steroidogenic acute regulatory protein (StAR), in AngII or K+-stimulated glomerulosa cells. The data show that ANP completely inhibits the phosphorylation of MARCKS and partially inhibits that of StAR in cells stimulated with K+. ANP also partially inhibits MARCKS phosphorylation but does not affect StAR phosphorylation in cells stimulated with AngII. These effects appear to be cGMP-independent and at least partially dependent on inhibition of protein kinase C (PKC). To our knowledge, this is the first report of ANP modulating either MARCKS or StAR phosphorylation in [32P]-labeled cells. The data also support the hypothesis that ANP inhibits aldosterone secretion acting as a step involved in cholesterol transport to the mitochondria.
Original language | English (US) |
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Pages (from-to) | 71-79 |
Number of pages | 9 |
Journal | Molecular and Cellular Endocrinology |
Volume | 177 |
Issue number | 1-2 |
DOIs | |
State | Published - May 25 2001 |
Keywords
- Adrenal glomerulosa
- Aldosterone
- Angiotensin II
- Myristoylated alanine-rich C-kinase substrate
- Potassium
- Steroidogenic acute regulatory protein
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Endocrinology