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

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 isoforms in Ado-induced steroidogenesis. The 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 was indeed activated by Ado. Moreover, downregulation of duanyu1531μ 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 duanyu1531μ phosphorylation. Together, these findings suggest that signaling mediates Ado-stimulated adrenal steroidogenesis.

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