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Protein kinase Cmu mediates adenosine-stimulated steroidogenesis in primary rat adrenal cells.

Authors: Chen, YC  Chen, Y  Huang, SH  Wang, SM 
Citation: Chen YC, etal., FEBS Lett. 2010 Nov 5;584(21):4442-8. Epub 2010 Oct 13.
Pubmed: (View Article at PubMed) PMID:20937274
DOI: Full-text: DOI:10.1016/j.febslet.2010.10.001

Adenosine (Ado), an endogenous nucleoside, can stimulate corticosterone synthesis in adrenal cells via the A(2A)/A(2B) adenosine receptors (ARs). This study evaluated the contribution of protein kinase C (PKC) isoforms in Ado-induced steroidogenesis. The PKC inhibitor calphostin c blocked Ado-induced steroidogenesis, the mitogen-activated protein kinase (MEK)-extracellular signal-related regulated kinase (ERK)-cyclic AMP responsive element-binding protein cascade, and the mRNA expression of steroidogenic acute regulatory protein and CYP11B1. Further analyses revealed that PKCmu was indeed activated by Ado. Moreover, downregulation of PKCmu by small interfering RNA (siRNA) inhibited Ado-stimulated steroidogenesis and ERK phosphorylation. Finally, inhibition of either A(2A)AR or A(2B)AR led to the suppression of PKCmu phosphorylation. Together, these findings suggest that A(2)AR-PKCmu-MEK signaling mediates Ado-stimulated adrenal steroidogenesis.


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RGD Object Information
RGD ID: 4145529
Created: 2010-11-09
Species: All species
Last Modified: 2010-11-09
Status: ACTIVE


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