Key result
Extracellular ATP activates channels permeable to di- and monovalent inorganic cations in rat peritoneal macrophages, likely involving a GTP-binding protein in receptor-to-channel coupling.
Extracellular ATP activates cation-permeable channels in rat peritoneal macrophages, a process that may involve a GTP-binding protein.
No immediate clinical implications; leaves open ATP channel roles in human macrophage function and inflammation.
The patch-clamp technique was used to study mechanisms of ATP-induced Ca2+ influx in rat peritoneal macrophages. The experiments on whole-cell and patch membranes have shown that extracellular ATP activates channels permeable to di- and monovalent inorganic cations. Ratios of unitary channel conductances in 105 mM Ca2+, Sr2+, Mn2+, Ba2+ and normal sodium solutions were 1.0, 0.95, 0.75, 0.55 and 0.85, respectively. The channels could open in the presence of non-hydrolyzable GTP analogues in artificial intracellular solution. The data are consistent with the hypothesis that a GTP-binding protein is involved in receptor-to-channel coupling.
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Naumov et al. (1992) studied this question. Extracellular ATP was evaluated on ATP-induced Ca2+ influx mechanisms and channel conductances. Extracellular ATP activates channels permeable to di- and monovalent inorganic cations in rat peritoneal macrophages, likely involving a GTP-binding protein in receptor-to-channel coupling.
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