Related Experiment Video
Updated: Aug 25, 2026

Developing a Rat Model for Bipolar Disorder
Published on: May 2, 2025
Antipsychotics regulate cyclic AMP-dependent protein kinase and phosphorylated cyclic AMP response element-binding
Angela V Turalba1, Kimberly A Leite-Morris, Gary B Kaplan
1Department of Psychiatry, Brown Medical School, Providence, RI 02912, USA.
Abstract:
Adenosine 3',5'-monophosphate (cAMP) and cAMP-dependent protein kinase (PKA) signaling have been implicated in antipsychotic drug action. This study examines the effects of acute antipsychotic treatment using typical (haloperidol) and atypical (olanzapine) agents on cAMP signaling in dorsal striatum, nucleus accumbens and medial prefrontal cortex in mice. PKA catalytic subunit (PKA-c) and phosphorylated cAMP response element-binding protein (pCREB) levels were measured to evaluate antipsychotic drug effects. Nuclear PKA-c levels increased in the dorsal striatum after haloperidol and olanzapine treatment. In medial prefrontal cortex, olanzapine produced dose-dependent decreases in PKA-c and pCREB levels. The differential effects of typical versus atypical antipsychotic agents on PKA and pCREB in striatal and cortical regions illustrate the diverging actions of these agents on cAMP pathways.
Related Concept Videos
cAMP-dependent Protein Kinase Pathways
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
GPCRs Regulate Adenylyl Cylase Activity
Two...
PI3K/mTOR/AKT Signaling Pathway
