Benzodiazepines modulate the A2 adenosine binding sites on 108CC15 neuroblastoma X glioma hybrid cells.

Abstract

We have demonstrated high affinity diazepam binding sites of the Ro5-4864 benzodiazepine receptor subtype on 108CC15 neuroblastoma X glioma hybrid cells. These cells were previously shown to have purinoceptors of the A2 adenosine subtype and we have now found that [3H]-adenosine can be displaced from this binding site by the benzodiazepines and related compounds that can also bind to the Ro5-4864 site. Diazepam was found to have no intrinsic activity at the A2-receptor as measured by the stimulation of adenosine 3':5'-cyclic monophosphate (cyclic AMP) production in this cell line. At concentrations sufficient to compete for the A2-receptor, diazepam was shown to facilitate, by approximately 2 fold, the stimulation of cyclic AMP by adenosine. These effects are not due to inhibition of adenosine uptake or phosphodiesterase activity, but are probably a consequence of modulation of the coupling of the A2-receptor to cyclic AMP production in this hybrid cell line.

• Authors: C R Snell, P H Snell
• Journal: British journal of pharmacology (Br J Pharmacol) Vol. 83 Issue 3 Pg. 791-8 (Nov 1984) ISSN: 0007-1188 [Print] England
• PMID: 6150742 (Publication Type: Journal Article)

Chemical References

• Anti-Anxiety Agents
• Phosphodiesterase Inhibitors
• Pyrrolidinones
• Receptors, Cell Surface
• Receptors, GABA-A
• Receptors, Purinergic
• Benzodiazepines
• ID 690
• Clonazepam
• Cyclic AMP
• Rolipram
• Diazepam

Topics

• Animals
• Anti-Anxiety Agents (pharmacology)
• Benzodiazepines
• Binding, Competitive (drug effects)
• Cells, Cultured
• Clonazepam (analogs & derivatives, pharmacology)
• Cyclic AMP (biosynthesis)
• Diazepam (metabolism)
• Glioma (metabolism)
• Hybrid Cells
• Kinetics
• Neuroblastoma (metabolism)
• Phosphodiesterase Inhibitors (pharmacology)
• Pyrrolidinones (pharmacology)
• Receptors, Cell Surface (metabolism)
• Receptors, GABA-A (metabolism)
• Receptors, Purinergic
• Rolipram