The α9α10 nicotinic acetylcholine receptor is permeable to and is modulated by divalent cations
The native cholinergic receptor that mediates synaptic transmission between olivocochlear fibers and outer hair cells of the cochlea is permeable to Ca2+ and is thought to be composed of both the α9 and the α10 cholinergic nicotinic subunits. The aim of the present work was to study the permeability...
Guardado en:
| Autores principales: | , |
|---|---|
| Publicado: |
2002
|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03785955_v167_n1-2_p122_Weisstaub http://hdl.handle.net/20.500.12110/paper_03785955_v167_n1-2_p122_Weisstaub |
| Aporte de: |
| id |
paper:paper_03785955_v167_n1-2_p122_Weisstaub |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_03785955_v167_n1-2_p122_Weisstaub2023-06-08T15:40:23Z The α9α10 nicotinic acetylcholine receptor is permeable to and is modulated by divalent cations Weisstaub, Noelia V. Katz, Eleonora Ca2+ permeability Ligand-gated channel Neurotransmitter receptor channel Nicotinic receptor Olivocochlear efferent synapse Outer hair cell Voltage-dependent blockage acetylcholine barium ion calcium ion complementary RNA divalent cation magnesium ion monovalent cation nicotinic receptor receptor subunit recombinant receptor calcium Chrna9 protein, rat divalent cation magnesium protein subunit recombinant protein article concentration response controlled study depolarization electric potential electrode evoked response hyperpolarization IC 50 ion current ion permeability modulation nonhuman oocyte priority journal rat receptor affinity receptor blocking regulatory mechanism voltage clamp Xenopus laevis animal chemistry drug effect electrophysiology female genetics hair cell in vitro study metabolism permeability synaptic transmission Animals Calcium Cations, Divalent Electrophysiology Female Hair Cells, Outer Magnesium Oocytes Permeability Protein Subunits Rats Receptors, Nicotinic Recombinant Proteins Synaptic Transmission Xenopus laevis The native cholinergic receptor that mediates synaptic transmission between olivocochlear fibers and outer hair cells of the cochlea is permeable to Ca2+ and is thought to be composed of both the α9 and the α10 cholinergic nicotinic subunits. The aim of the present work was to study the permeability of the recombinant α9α10 nicotinic acetylcholine receptor to Ca2+, Ba2+ and Mg2+ and its modulation by these divalent cations. Experiments were performed, by the two-electrode voltage-clamp technique, in Xenopus laevis oocytes injected with α9 and α10 cRNA. The relative divalent to monovalent cation permeability was high (∼10) for Ca2+, Ba2+ and Mg2+. Currents evoked by acetylcholine (ACh) were potentiated by either Ca2+ or Ba2+ up to 500 μM but were blocked by higher concentrations of these cations. Potentiation by Ca2+ was voltage-independent, whereas blockage was stronger at hyperpolarized than at depolarized potentials. Mg2+ did not potentiate but it blocked ACh-evoked currents (IC50=0.38 mM). In the absence of Ca2+, the EC50 for ACh was higher (48 μM) than that obtained with 1.8 mM Ca2+ (14.3 μM), suggesting that potentiation by Ca2+ involves changes in the apparent affinity of the α9α10 receptor for ACh. © 2002 Elsevier Science B.V. All rights reserved. Fil:Weisstaub, N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Katz, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2002 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03785955_v167_n1-2_p122_Weisstaub http://hdl.handle.net/20.500.12110/paper_03785955_v167_n1-2_p122_Weisstaub |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Ca2+ permeability Ligand-gated channel Neurotransmitter receptor channel Nicotinic receptor Olivocochlear efferent synapse Outer hair cell Voltage-dependent blockage acetylcholine barium ion calcium ion complementary RNA divalent cation magnesium ion monovalent cation nicotinic receptor receptor subunit recombinant receptor calcium Chrna9 protein, rat divalent cation magnesium protein subunit recombinant protein article concentration response controlled study depolarization electric potential electrode evoked response hyperpolarization IC 50 ion current ion permeability modulation nonhuman oocyte priority journal rat receptor affinity receptor blocking regulatory mechanism voltage clamp Xenopus laevis animal chemistry drug effect electrophysiology female genetics hair cell in vitro study metabolism permeability synaptic transmission Animals Calcium Cations, Divalent Electrophysiology Female Hair Cells, Outer Magnesium Oocytes Permeability Protein Subunits Rats Receptors, Nicotinic Recombinant Proteins Synaptic Transmission Xenopus laevis |
| spellingShingle |
Ca2+ permeability Ligand-gated channel Neurotransmitter receptor channel Nicotinic receptor Olivocochlear efferent synapse Outer hair cell Voltage-dependent blockage acetylcholine barium ion calcium ion complementary RNA divalent cation magnesium ion monovalent cation nicotinic receptor receptor subunit recombinant receptor calcium Chrna9 protein, rat divalent cation magnesium protein subunit recombinant protein article concentration response controlled study depolarization electric potential electrode evoked response hyperpolarization IC 50 ion current ion permeability modulation nonhuman oocyte priority journal rat receptor affinity receptor blocking regulatory mechanism voltage clamp Xenopus laevis animal chemistry drug effect electrophysiology female genetics hair cell in vitro study metabolism permeability synaptic transmission Animals Calcium Cations, Divalent Electrophysiology Female Hair Cells, Outer Magnesium Oocytes Permeability Protein Subunits Rats Receptors, Nicotinic Recombinant Proteins Synaptic Transmission Xenopus laevis Weisstaub, Noelia V. Katz, Eleonora The α9α10 nicotinic acetylcholine receptor is permeable to and is modulated by divalent cations |
| topic_facet |
Ca2+ permeability Ligand-gated channel Neurotransmitter receptor channel Nicotinic receptor Olivocochlear efferent synapse Outer hair cell Voltage-dependent blockage acetylcholine barium ion calcium ion complementary RNA divalent cation magnesium ion monovalent cation nicotinic receptor receptor subunit recombinant receptor calcium Chrna9 protein, rat divalent cation magnesium protein subunit recombinant protein article concentration response controlled study depolarization electric potential electrode evoked response hyperpolarization IC 50 ion current ion permeability modulation nonhuman oocyte priority journal rat receptor affinity receptor blocking regulatory mechanism voltage clamp Xenopus laevis animal chemistry drug effect electrophysiology female genetics hair cell in vitro study metabolism permeability synaptic transmission Animals Calcium Cations, Divalent Electrophysiology Female Hair Cells, Outer Magnesium Oocytes Permeability Protein Subunits Rats Receptors, Nicotinic Recombinant Proteins Synaptic Transmission Xenopus laevis |
| description |
The native cholinergic receptor that mediates synaptic transmission between olivocochlear fibers and outer hair cells of the cochlea is permeable to Ca2+ and is thought to be composed of both the α9 and the α10 cholinergic nicotinic subunits. The aim of the present work was to study the permeability of the recombinant α9α10 nicotinic acetylcholine receptor to Ca2+, Ba2+ and Mg2+ and its modulation by these divalent cations. Experiments were performed, by the two-electrode voltage-clamp technique, in Xenopus laevis oocytes injected with α9 and α10 cRNA. The relative divalent to monovalent cation permeability was high (∼10) for Ca2+, Ba2+ and Mg2+. Currents evoked by acetylcholine (ACh) were potentiated by either Ca2+ or Ba2+ up to 500 μM but were blocked by higher concentrations of these cations. Potentiation by Ca2+ was voltage-independent, whereas blockage was stronger at hyperpolarized than at depolarized potentials. Mg2+ did not potentiate but it blocked ACh-evoked currents (IC50=0.38 mM). In the absence of Ca2+, the EC50 for ACh was higher (48 μM) than that obtained with 1.8 mM Ca2+ (14.3 μM), suggesting that potentiation by Ca2+ involves changes in the apparent affinity of the α9α10 receptor for ACh. © 2002 Elsevier Science B.V. All rights reserved. |
| author |
Weisstaub, Noelia V. Katz, Eleonora |
| author_facet |
Weisstaub, Noelia V. Katz, Eleonora |
| author_sort |
Weisstaub, Noelia V. |
| title |
The α9α10 nicotinic acetylcholine receptor is permeable to and is modulated by divalent cations |
| title_short |
The α9α10 nicotinic acetylcholine receptor is permeable to and is modulated by divalent cations |
| title_full |
The α9α10 nicotinic acetylcholine receptor is permeable to and is modulated by divalent cations |
| title_fullStr |
The α9α10 nicotinic acetylcholine receptor is permeable to and is modulated by divalent cations |
| title_full_unstemmed |
The α9α10 nicotinic acetylcholine receptor is permeable to and is modulated by divalent cations |
| title_sort |
α9α10 nicotinic acetylcholine receptor is permeable to and is modulated by divalent cations |
| publishDate |
2002 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03785955_v167_n1-2_p122_Weisstaub http://hdl.handle.net/20.500.12110/paper_03785955_v167_n1-2_p122_Weisstaub |
| work_keys_str_mv |
AT weisstaubnoeliav thea9a10nicotinicacetylcholinereceptorispermeabletoandismodulatedbydivalentcations AT katzeleonora thea9a10nicotinicacetylcholinereceptorispermeabletoandismodulatedbydivalentcations AT weisstaubnoeliav a9a10nicotinicacetylcholinereceptorispermeabletoandismodulatedbydivalentcations AT katzeleonora a9a10nicotinicacetylcholinereceptorispermeabletoandismodulatedbydivalentcations |
| _version_ |
1768546071769776128 |