α-RgIA: A novel conotoxin that specifically and potently blocks the α9α10 nAChR
- Autores
- Ellison, Michael; Haberlandt, Christian; Gomez Casati, Maria Eugenia; Watkins, Maren; Elgoyhen, Ana Belen; McIntosh, J. Michael; Olivera, Baldomero M.
- Año de publicación
- 2006
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The α9 and α10 nicotinic acetylcholine receptor (nAChR) subunits assemble to form the α9α10 nAChR subtype. This receptor is believed to mediate cholinergic synaptic transmission between efferent olivocochlear fibers and the hair cells of the cochlea. In addition α9 and/or α10 expression has been described in dorsal root ganglion neurons, lymphocytes, skin keratinocytes, and the pars tuberalis of the pituitary. Specific antagonists that selectively block the α9α10 channel could be valuable tools for elucidating its role in these diverse tissues. This study describes a novel α-conotoxin from the Western Atlantic species Conus regius, α-conotoxin RgIA (α-RgIA), that is a subtype specific blocker of the α9α10 nAChR. α-RgIA belongs to the α4/3 subfamily of the α-conotoxin family; sequence and subtype specificity comparisons between α-RgIA and previously characterized α4/3 toxins indicate that the amino acids in the C-terminal half of α-RgIA are responsible for its preferential inhibition of the α9α10 nAChR subtype
Fil: Ellison, Michael. University of Utah; Estados Unidos
Fil: Haberlandt, Christian. University of Utah; Estados Unidos
Fil: Gomez Casati, Maria Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Watkins, Maren. University of Utah; Estados Unidos
Fil: Elgoyhen, Ana Belen. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: McIntosh, J. Michael. University of Utah; Estados Unidos
Fil: Olivera, Baldomero M.. University of Utah; Estados Unidos - Materia
- Nicotinic Acetylcholine Receptors
- Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/79876
Ver los metadatos del registro completo
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α-RgIA: A novel conotoxin that specifically and potently blocks the α9α10 nAChREllison, MichaelHaberlandt, ChristianGomez Casati, Maria EugeniaWatkins, MarenElgoyhen, Ana BelenMcIntosh, J. MichaelOlivera, Baldomero M.Nicotinic Acetylcholine Receptorshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The α9 and α10 nicotinic acetylcholine receptor (nAChR) subunits assemble to form the α9α10 nAChR subtype. This receptor is believed to mediate cholinergic synaptic transmission between efferent olivocochlear fibers and the hair cells of the cochlea. In addition α9 and/or α10 expression has been described in dorsal root ganglion neurons, lymphocytes, skin keratinocytes, and the pars tuberalis of the pituitary. Specific antagonists that selectively block the α9α10 channel could be valuable tools for elucidating its role in these diverse tissues. This study describes a novel α-conotoxin from the Western Atlantic species Conus regius, α-conotoxin RgIA (α-RgIA), that is a subtype specific blocker of the α9α10 nAChR. α-RgIA belongs to the α4/3 subfamily of the α-conotoxin family; sequence and subtype specificity comparisons between α-RgIA and previously characterized α4/3 toxins indicate that the amino acids in the C-terminal half of α-RgIA are responsible for its preferential inhibition of the α9α10 nAChR subtypeFil: Ellison, Michael. University of Utah; Estados UnidosFil: Haberlandt, Christian. University of Utah; Estados UnidosFil: Gomez Casati, Maria Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Watkins, Maren. University of Utah; Estados UnidosFil: Elgoyhen, Ana Belen. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: McIntosh, J. Michael. University of Utah; Estados UnidosFil: Olivera, Baldomero M.. University of Utah; Estados UnidosAmerican Chemical Society2006-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/79876Ellison, Michael; Haberlandt, Christian; Gomez Casati, Maria Eugenia; Watkins, Maren; Elgoyhen, Ana Belen; et al.; α-RgIA: A novel conotoxin that specifically and potently blocks the α9α10 nAChR; American Chemical Society; Biochemistry; 45; 5; 2-2006; 1511-15170006-2960CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/bi0520129info:eu-repo/semantics/altIdentifier/doi/10.1021/bi0520129info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:20:01Zoai:ri.conicet.gov.ar:11336/79876instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:20:02.113CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
α-RgIA: A novel conotoxin that specifically and potently blocks the α9α10 nAChR |
title |
α-RgIA: A novel conotoxin that specifically and potently blocks the α9α10 nAChR |
spellingShingle |
α-RgIA: A novel conotoxin that specifically and potently blocks the α9α10 nAChR Ellison, Michael Nicotinic Acetylcholine Receptors |
title_short |
α-RgIA: A novel conotoxin that specifically and potently blocks the α9α10 nAChR |
title_full |
α-RgIA: A novel conotoxin that specifically and potently blocks the α9α10 nAChR |
title_fullStr |
α-RgIA: A novel conotoxin that specifically and potently blocks the α9α10 nAChR |
title_full_unstemmed |
α-RgIA: A novel conotoxin that specifically and potently blocks the α9α10 nAChR |
title_sort |
α-RgIA: A novel conotoxin that specifically and potently blocks the α9α10 nAChR |
dc.creator.none.fl_str_mv |
Ellison, Michael Haberlandt, Christian Gomez Casati, Maria Eugenia Watkins, Maren Elgoyhen, Ana Belen McIntosh, J. Michael Olivera, Baldomero M. |
author |
Ellison, Michael |
author_facet |
Ellison, Michael Haberlandt, Christian Gomez Casati, Maria Eugenia Watkins, Maren Elgoyhen, Ana Belen McIntosh, J. Michael Olivera, Baldomero M. |
author_role |
author |
author2 |
Haberlandt, Christian Gomez Casati, Maria Eugenia Watkins, Maren Elgoyhen, Ana Belen McIntosh, J. Michael Olivera, Baldomero M. |
author2_role |
author author author author author author |
dc.subject.none.fl_str_mv |
Nicotinic Acetylcholine Receptors |
topic |
Nicotinic Acetylcholine Receptors |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
The α9 and α10 nicotinic acetylcholine receptor (nAChR) subunits assemble to form the α9α10 nAChR subtype. This receptor is believed to mediate cholinergic synaptic transmission between efferent olivocochlear fibers and the hair cells of the cochlea. In addition α9 and/or α10 expression has been described in dorsal root ganglion neurons, lymphocytes, skin keratinocytes, and the pars tuberalis of the pituitary. Specific antagonists that selectively block the α9α10 channel could be valuable tools for elucidating its role in these diverse tissues. This study describes a novel α-conotoxin from the Western Atlantic species Conus regius, α-conotoxin RgIA (α-RgIA), that is a subtype specific blocker of the α9α10 nAChR. α-RgIA belongs to the α4/3 subfamily of the α-conotoxin family; sequence and subtype specificity comparisons between α-RgIA and previously characterized α4/3 toxins indicate that the amino acids in the C-terminal half of α-RgIA are responsible for its preferential inhibition of the α9α10 nAChR subtype Fil: Ellison, Michael. University of Utah; Estados Unidos Fil: Haberlandt, Christian. University of Utah; Estados Unidos Fil: Gomez Casati, Maria Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina Fil: Watkins, Maren. University of Utah; Estados Unidos Fil: Elgoyhen, Ana Belen. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina Fil: McIntosh, J. Michael. University of Utah; Estados Unidos Fil: Olivera, Baldomero M.. University of Utah; Estados Unidos |
description |
The α9 and α10 nicotinic acetylcholine receptor (nAChR) subunits assemble to form the α9α10 nAChR subtype. This receptor is believed to mediate cholinergic synaptic transmission between efferent olivocochlear fibers and the hair cells of the cochlea. In addition α9 and/or α10 expression has been described in dorsal root ganglion neurons, lymphocytes, skin keratinocytes, and the pars tuberalis of the pituitary. Specific antagonists that selectively block the α9α10 channel could be valuable tools for elucidating its role in these diverse tissues. This study describes a novel α-conotoxin from the Western Atlantic species Conus regius, α-conotoxin RgIA (α-RgIA), that is a subtype specific blocker of the α9α10 nAChR. α-RgIA belongs to the α4/3 subfamily of the α-conotoxin family; sequence and subtype specificity comparisons between α-RgIA and previously characterized α4/3 toxins indicate that the amino acids in the C-terminal half of α-RgIA are responsible for its preferential inhibition of the α9α10 nAChR subtype |
publishDate |
2006 |
dc.date.none.fl_str_mv |
2006-02 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/79876 Ellison, Michael; Haberlandt, Christian; Gomez Casati, Maria Eugenia; Watkins, Maren; Elgoyhen, Ana Belen; et al.; α-RgIA: A novel conotoxin that specifically and potently blocks the α9α10 nAChR; American Chemical Society; Biochemistry; 45; 5; 2-2006; 1511-1517 0006-2960 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/79876 |
identifier_str_mv |
Ellison, Michael; Haberlandt, Christian; Gomez Casati, Maria Eugenia; Watkins, Maren; Elgoyhen, Ana Belen; et al.; α-RgIA: A novel conotoxin that specifically and potently blocks the α9α10 nAChR; American Chemical Society; Biochemistry; 45; 5; 2-2006; 1511-1517 0006-2960 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/bi0520129 info:eu-repo/semantics/altIdentifier/doi/10.1021/bi0520129 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
American Chemical Society |
publisher.none.fl_str_mv |
American Chemical Society |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1844614176536788992 |
score |
13.070432 |