Regulation of PRiMA-linked G(4) AChE by a cAMP-dependent signaling pathway in cultured rat pheochromocyoma PC12 cells.

The catalytic subunit of acetylcholinesterase (AChE(T)) interacts with proline-rich membrane anchor (PRiMA) to form PRiMA-linked G(4) AChE on membrane surface for its cholinergic function. Cultured PC12 cells expressed the transcripts encoding AChE(T) and PRiMA I, but the expression of PRiMA II transcript was below detection. Upon the treatment of dibutyryl-cAMP (Bt(2)-cAMP) and forskolin in cultured cells to stimulate the cAMP-dependent signaling pathway, the mRNA expressions of both AChE(T) and PRiMA I, as well as the enzymatic activity were up-regulated. More importantly, sucrose density gradient analysis revealed that both G(1) and G(4) AChE isoforms were increased in the Bt(2)-cAMP-treated cultures. These results suggest that the regulation of PRiMA-linked G(4) AChE in terms of gene transcription and molecular assembly in the cultured PC12 cells could be mediated by a cAMP-dependent signaling mechanism.