picrotoxinin and avermectin

picrotoxinin has been researched along with avermectin* in 2 studies

Other Studies

2 other study(ies) available for picrotoxinin and avermectin

Article	Year
Activation of Cl- channels by avermectin in rat cultured hippocampal neurons. Naunyn-Schmiedeberg's archives of pharmacology, 1993, Volume: 348, Issue:6 The actions of the insecticide avermectin (AVM) were studied in rat cultured hippocampal neurons with patch-clamp techniques. Application of micromolar concentrations of AVM to voltage-clamped cells gave rise to whole-cell currents, which showed a slow time-course of activation in the order of 10 s, and wash-out periods of typically 20 min. Dose-response curves revealed a half-maximally activating AVM concentration (EC50) of 2.0 +/- 0.6 microM and a Hill coefficient of 1.5 +/- 0.9. The current activated by AVM was carried predominantly by Cl- ions, as demonstrated by ion-substitution experiments. The Cl- channel blocker picrotoxinin (100 microM) substantially but transiently reduced the AVM response. Outside-out patch recording showed that AVM opened Cl- channels with a conductance of 40 +/- 12 pS. The open-time distribution was characterized by two time constants of 11 ms and 259 ms. It is suggested that AVM directly activates Cl- channels in mammalian central neurons, which resemble the channels activated by the physiological transmitters GABA and glycine. Topics: Animals; Animals, Newborn; Anthelmintics; Cells, Cultured; Chloride Channels; Electrophysiology; Hippocampus; Ivermectin; Membrane Potentials; Neurons; Picrotoxin; Rats; Rats, Wistar; Receptors, GABA-A; Sesterterpenes	1993
Evidence for association of a high affinity avermectin binding site with the benzodiazepine receptor. European journal of pharmacology, 1984, Jun-01, Volume: 101, Issue:3-4 Avermectin B1a concentrations corresponding to the KD value of a specific high affinity binding site for [3H]avermectin B1a are sufficient to stimulate the specific high affinity binding of [3H]flunitrazepam to its receptors. This stimulation of [3H]flunitrazepam binding by low concentrations of avermectin B1a was enhanced by chloride ions and picrotoxinin and reduced by the GABA agonists THIP and PSA. The similar modulation by chloride ions, GABA agonists and picrotoxinin and the resistance against washing of membranes of avermectin B1a bound to its specific high affinity binding site or to the site modulating [3H]flunitrazepam binding indicate a close association of the specific high affinity binding site for [3H]avermectin B1a with the GABA-benzodiazepine receptor complex. Topics: Animals; Binding Sites; Binding, Competitive; Cell Membrane; Cerebellar Cortex; Chlorides; Flunitrazepam; In Vitro Techniques; Ivermectin; Lactones; Picrotoxin; Rats; Receptors, Cell Surface; Receptors, GABA-A; Sesterterpenes; Temperature	1984

Article

Year

Activation of Cl- channels by avermectin in rat cultured hippocampal neurons.

Naunyn-Schmiedeberg's archives of pharmacology, 1993, Volume: 348, Issue:6

The actions of the insecticide avermectin (AVM) were studied in rat cultured hippocampal neurons with patch-clamp techniques. Application of micromolar concentrations of AVM to voltage-clamped cells gave rise to whole-cell currents, which showed a slow time-course of activation in the order of 10 s, and wash-out periods of typically 20 min. Dose-response curves revealed a half-maximally activating AVM concentration (EC50) of 2.0 +/- 0.6 microM and a Hill coefficient of 1.5 +/- 0.9. The current activated by AVM was carried predominantly by Cl- ions, as demonstrated by ion-substitution experiments. The Cl- channel blocker picrotoxinin (100 microM) substantially but transiently reduced the AVM response. Outside-out patch recording showed that AVM opened Cl- channels with a conductance of 40 +/- 12 pS. The open-time distribution was characterized by two time constants of 11 ms and 259 ms. It is suggested that AVM directly activates Cl- channels in mammalian central neurons, which resemble the channels activated by the physiological transmitters GABA and glycine.

Topics: Animals; Animals, Newborn; Anthelmintics; Cells, Cultured; Chloride Channels; Electrophysiology; Hippocampus; Ivermectin; Membrane Potentials; Neurons; Picrotoxin; Rats; Rats, Wistar; Receptors, GABA-A; Sesterterpenes

1993

Evidence for association of a high affinity avermectin binding site with the benzodiazepine receptor.

European journal of pharmacology, 1984, Jun-01, Volume: 101, Issue:3-4

Avermectin B1a concentrations corresponding to the KD value of a specific high affinity binding site for [3H]avermectin B1a are sufficient to stimulate the specific high affinity binding of [3H]flunitrazepam to its receptors. This stimulation of [3H]flunitrazepam binding by low concentrations of avermectin B1a was enhanced by chloride ions and picrotoxinin and reduced by the GABA agonists THIP and PSA. The similar modulation by chloride ions, GABA agonists and picrotoxinin and the resistance against washing of membranes of avermectin B1a bound to its specific high affinity binding site or to the site modulating [3H]flunitrazepam binding indicate a close association of the specific high affinity binding site for [3H]avermectin B1a with the GABA-benzodiazepine receptor complex.

Topics: Animals; Binding Sites; Binding, Competitive; Cell Membrane; Cerebellar Cortex; Chlorides; Flunitrazepam; In Vitro Techniques; Ivermectin; Lactones; Picrotoxin; Rats; Receptors, Cell Surface; Receptors, GABA-A; Sesterterpenes; Temperature

1984