The intracellular mechanisms of action of α-MSH in rat adrenocortical cells were examined. When rat adrenal capsule (largely glomerulosa) cells were stimulated with a range of concentrations of α-MSH there was significant stimulation of aldosterone secretion at 10-10 mol/l, although cyclic AMP was not increased until high concentrations of α-MSH were used (10-6 mol/l and above). However, cells incubated with ACTH showed an increase in aldosterone secretion at 10-11 mol/l and levels of cyclic AMP were elevated at 10-9 mol ACTH/1.
When rat adrenal whole capsules were incubated with α-MSH, membrane-bound protein kinase C (PKC) activity was increased and cytosolic enzyme activity decreased, showing PKC activation. Stimulation with angiotensin II also induced translocation of PKC activity, but ACTH did not.
When [3H]inositol-loaded glomerulosa cells were stimulated with α-MSH there was significant generation of [3H]inositol trisphosphate (IP3) at concentrations of α-MSH which stimulated secretion of aldosterone. Significantly increased levels of [3H]IP3 were also measured when loaded cells were exposed to angiotensin II. ACTH did not cause any significant stimulation of [3H]IP3 production at any concentration used. These results indicate that activation of PKC and phospholipase C is important in modulating the steroidogenic effect of α-MSH.
Journal of Molecular Endocrinology is committed to supporting researchers in demonstrating the impact of their articles published in the journal.
The two types of article metrics we measure are (i) more traditional full-text views and pdf downloads, and (ii) Altmetric data, which shows the wider impact of articles in a range of non-traditional sources, such as social media.
More information is on the Reasons to publish page.
|Sept 2018 onwards||Past Year||Past 30 Days|
|Full Text Views||0||0||0|