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This in vitro study of the wall lizard Hemidactylus flaviviridis demonstrates the role of the opioid peptide dynorphin A((1-17)) [dyn A((1-17))] in the regulation of the phagocytic activity of splenic phagocytes. Dyn A((1-17)) in a concentration-dependent manner inhibited the phagocytic activity, and the maximum inhibition was recorded at a concentration of 10(-9) mol l(-1). To explore the receptor-mediated effect of dyn A((1-17)), cells were treated simultaneously with the non-selective opioid receptor blocker naltrexone and dyn A((1-17)). Naltrexone completely blocked the inhibitory effect of dyn A((1-17)) on phagocytosis. Moreover, the involvement of selective opioid receptors was investigated using selective opioid receptor antagonists. CTAP and naltrindole, selective μ- and δ-opioid receptor blockers, respectively, failed to block the inhibitory effect of dyn A((1-17)) on phagocytosis. However, the selective κ-opioid receptor blocker NorBNI completely antagonized the inhibitory effect of dyn A((1-17)). Regarding the κ-opioid receptor-coupled downstream signaling cascade, the adenylate cyclase (AC) inhibitor SQ 22536 and protein kinase A (PKA) inhibitor H-89 decreased the inhibitory effect of dyn A((1-17)) on phagocytosis. Furthermore, treatment with dyn A((1-17)) caused an increase in intracellular cAMP content in splenic phagocytes. Thus, it can be concluded that, in H. flaviviridis, dyn A((1-17)) negatively regulates the phagocytic activity of splenic phagocytes by acting through κ-opioid receptors that are coupled with the AC-cAMP-PKA signal transduction mechanism.

journal of experimental biology

Dynorphin regulates the phagocytic activity of splenic phagocytes in wall lizards: involvement of a κ-opioid receptor-coupled adenylate-cyclase–cAMP–PKA pathway