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Cyclic adenosine monophosphate (cAMP) controls differentiation in several   types of cells during brain development. However, the molecular mechanism of   cAMP-controlled differentiation is not fully understood. We investigated the   role of protein kinase A (PKA) and exchange protein directly activated by   cAMP (Epac) on cAMP-induced glial fibrillary acidic protein (GFAP), an   astrocyte marker, in cultured glial cells. B92 glial cells were treated with   cAMP-elevating drugs, an activator of adenylate cyclase, phosphodiesterase   inhibitor and a ß adrenal receptor agonist. These cAMP-elevating agents   induced dramatic morphological changes and expression of GFAP. A cAMP analog,   8-Br-cAMP, which activates Epac as well as PKA, induced GFAP expression and   morphological changes, while another cAMP analog, 8-CPT-cAMP, which activates   Epac with greater efficacy when compared to PKA, induced GFAP expression but   very weak morphological changes. Most importantly, the treatment with a PKA   inhibitor partially reduced cAMP-induced GFAP expression. Taken together,   these results indicate that cAMP-elevating drugs lead to the induction of   GFAP via PKA and/or Epac activation in B92 glial cells

Protein kinase A and Epac activation by cAMP regulates the expression of glial fibrillary acidic protein in glial cells