Abstract
ATP receptors, activation of which leads to an increase in membrane conductance for monovalent cations and to the appearance of an inward ionic current at negative membrane potential values, have been found on the outer surface of the somatic membrane of sensory ganglionic neurons of rats and cats. The ATP-activated ionic channel is almost equally permeable for ions of the alkali metals and possesses marked permeability even for Tris and tetraethylammonium ions. Simultaneously with this, the channel demonstrates marked anomalous rectification. For the receptor to be activated, one ATP molecule must interact with it. Activation of the receptors is not connected with the use of energy of high-energy bonds. Affinity of the receptors for agonists is increased with a fall of membrane potential. Adenine nucleotides containing at least two phosphoric acid residues are agonists. The most active agonist is ATP. Adenosine monophosphate, adenosine, and puromycin competitively block these receptors. Pyrimidine nucleotides, and also purine nucleotides — guanosine triphosphate and inosine triphosphate — do not interact with ATP receptors. ATP-activated currents develop quickly and are then slowly desensitized. The desensitization time constant decreases with an increase in ATP concentration, to reach about 2 sec at a saturating concentration.
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A. A. Bogomolets Institute of Physiology, Academy of Sciences of the Ukrainian SSR, Kiev. Translated from Neirofiziologiya, Vol. 16, No. 3, pp. 327–336, May–June, 1984.
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Kryshtal', O.A., Marchenko, S.M. ATP-activated ionic conductance in the somatic membrane of mammalian sensory ganglionic neurons. Neurophysiology 16, 255–263 (1984). https://doi.org/10.1007/BF01065377
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DOI: https://doi.org/10.1007/BF01065377