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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/79876

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network_name_str CONICET Digital (CONICET)
spelling 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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