A multifaceted examination of the action of PDE4 inhibitor rolipram on MMP2/9 reveals therapeutic implications.

ABSTRACT: A PDE4 (phosphodiesterase 4) inhibitor, Rolipram, was previously found to down-regulate (in a manner dependent on cAMP (cyclic adenosine monophosphate)-PKA (protein kinase A)) MMP2 (matrix metalloproteinase 2) and MMP9 protein expression levels, important markers of epithelial-to-mesenchymal transition in human breast cancer cell lines. However, zymographic studies revealed that rolipram could also alter the enzymatic activities of these MMPs, even in the presence of the PKA inhibitor H89. This calls for more detailed investigations of the inhibitory mechanism of rolipram on MMP2 and MMP9. The prediction of ligand-based targets through online reverse screening indicated that proteases are likely targets of rolipram. Computational molecular docking also demonstrated significant binding affi

SUBMITTER: Bagchi A 

PROVIDER: S-EPMC11958756 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature