S-nitrosylation of NF-κB p65 inhibits TSH-induced Na+/I- symporter expression

Nitric oxide (NO) is a ubiquitous signaling molecule involved in a wide variety of cellular physiological processes. In thyroid cells, NO-synthase III-endogenously produced NO reduces TSH-stimulatedthyroid-specificgene expression, suggesting a potential autocrine role of NO in modulating thyroid fun...

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Authors: Nicola, Juan Pablo, Peyret, Victoria, Nazar, Magalí, Romero, Jorge Miguel, Lucero, Ariel Maximiliano, Del Mar Montesinos, María, Bocco, José Luis, Pellizas, Claudia Gabriela, Masini, Ana María
Format: article
Status:Published version
Publication Date:2015
Country:Argentina
Institution:Consejo Nacional de Investigaciones Científicas y Técnicas
Repository:CONICET Digital (CONICET)
Language:English
OAI Identifier:oai:ri.conicet.gov.ar:11336/185963
Online Access:http://hdl.handle.net/11336/185963
Access Level:Open access
Keyword:S-NITROSYLATION
NFKB
NIS
https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
id AR_a57900b4fef4e7df445c3eab4cd72a2c
oai_identifier_str oai:ri.conicet.gov.ar:11336/185963
network_acronym_str AR
network_name_str Argentina
repository_id_str
dc.title.none.fl_str_mv S-nitrosylation of NF-κB p65 inhibits TSH-induced Na+/I- symporter expression
title S-nitrosylation of NF-κB p65 inhibits TSH-induced Na+/I- symporter expression
spellingShingle S-nitrosylation of NF-κB p65 inhibits TSH-induced Na+/I- symporter expression
Nicola, Juan Pablo
S-NITROSYLATION
NFKB
NIS
https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
title_short S-nitrosylation of NF-κB p65 inhibits TSH-induced Na+/I- symporter expression
title_full S-nitrosylation of NF-κB p65 inhibits TSH-induced Na+/I- symporter expression
title_fullStr S-nitrosylation of NF-κB p65 inhibits TSH-induced Na+/I- symporter expression
title_full_unstemmed S-nitrosylation of NF-κB p65 inhibits TSH-induced Na+/I- symporter expression
title_sort S-nitrosylation of NF-κB p65 inhibits TSH-induced Na+/I- symporter expression
dc.creator.none.fl_str_mv Nicola, Juan Pablo
Peyret, Victoria
Nazar, Magalí
Romero, Jorge Miguel
Lucero, Ariel Maximiliano
Del Mar Montesinos, María
Bocco, José Luis
Pellizas, Claudia Gabriela
Masini, Ana María
author Nicola, Juan Pablo
author_facet Nicola, Juan Pablo
Peyret, Victoria
Nazar, Magalí
Romero, Jorge Miguel
Lucero, Ariel Maximiliano
Del Mar Montesinos, María
Bocco, José Luis
Pellizas, Claudia Gabriela
Masini, Ana María
author_role author
author2 Peyret, Victoria
Nazar, Magalí
Romero, Jorge Miguel
Lucero, Ariel Maximiliano
Del Mar Montesinos, María
Bocco, José Luis
Pellizas, Claudia Gabriela
Masini, Ana María
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv S-NITROSYLATION
NFKB
NIS
https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
topic S-NITROSYLATION
NFKB
NIS
https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
description Nitric oxide (NO) is a ubiquitous signaling molecule involved in a wide variety of cellular physiological processes. In thyroid cells, NO-synthase III-endogenously produced NO reduces TSH-stimulatedthyroid-specificgene expression, suggesting a potential autocrine role of NO in modulating thyroid function. Further studies indicate that NO induces thyroid dedifferentiation, because NO donors repress TSH-stimulated iodide (I-) uptake. Here, we investigated the molecular mechanism underlying the NO-inhibited Na+/I- symporter (NIS)-mediated I- uptake in thyroid cells. We showed that NO donors reduce I- uptake in a concentration-dependent manner, which correlates with decreased NIS protein expression. NO-reduced I- uptake results from transcriptional repression of NIS gene ratherthan posttranslational modifications reducing functional NIS expression at the plasma membrane. We observed that NO donors repress TSH-induced NIS gene expression by reducing the transcriptional activity of the nuclear factor-κB subunit p65. NO-promoted p65 S-nitrosylation reduces p65-mediated transactivation of the NIS promoter in response to TSH stimulation. Overall, our data are consistent with the notion that NO plays a role as an inhibitory signal to counterbalance TSH-stimulated nuclear factor-κB activation, thus modulating thyroid hormone biosynthesis.
publishDate 2015
dc.date.none.fl_str_mv 2015-12
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/11336/185963
Nicola, Juan Pablo; Peyret, Victoria; Nazar, Magalí; Romero, Jorge Miguel; Lucero, Ariel Maximiliano; et al.; S-nitrosylation of NF-κB p65 inhibits TSH-induced Na+/I- symporter expression; Endocrine Society; Endocrinology; 156; 12; 12-2015; 4741-4754
0013-7227
1945-7170
CONICET Digital
CONICET
url http://hdl.handle.net/11336/185963
identifier_str_mv Nicola, Juan Pablo; Peyret, Victoria; Nazar, Magalí; Romero, Jorge Miguel; Lucero, Ariel Maximiliano; et al.; S-nitrosylation of NF-κB p65 inhibits TSH-induced Na+/I- symporter expression; Endocrine Society; Endocrinology; 156; 12; 12-2015; 4741-4754
0013-7227
1945-7170
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/ 10.1210/en.2015-1192
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/endo/article/156/12/4741/2423183
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
dc.publisher.none.fl_str_mv Endocrine Society
publisher.none.fl_str_mv Endocrine Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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
_version_ 1799195111383367680
spelling S-nitrosylation of NF-κB p65 inhibits TSH-induced Na+/I- symporter expressionNicola, Juan PabloPeyret, VictoriaNazar, MagalíRomero, Jorge MiguelLucero, Ariel MaximilianoDel Mar Montesinos, MaríaBocco, José LuisPellizas, Claudia GabrielaMasini, Ana MaríaS-NITROSYLATIONNFKBNIShttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Nitric oxide (NO) is a ubiquitous signaling molecule involved in a wide variety of cellular physiological processes. In thyroid cells, NO-synthase III-endogenously produced NO reduces TSH-stimulatedthyroid-specificgene expression, suggesting a potential autocrine role of NO in modulating thyroid function. Further studies indicate that NO induces thyroid dedifferentiation, because NO donors repress TSH-stimulated iodide (I-) uptake. Here, we investigated the molecular mechanism underlying the NO-inhibited Na+/I- symporter (NIS)-mediated I- uptake in thyroid cells. We showed that NO donors reduce I- uptake in a concentration-dependent manner, which correlates with decreased NIS protein expression. NO-reduced I- uptake results from transcriptional repression of NIS gene ratherthan posttranslational modifications reducing functional NIS expression at the plasma membrane. We observed that NO donors repress TSH-induced NIS gene expression by reducing the transcriptional activity of the nuclear factor-κB subunit p65. NO-promoted p65 S-nitrosylation reduces p65-mediated transactivation of the NIS promoter in response to TSH stimulation. Overall, our data are consistent with the notion that NO plays a role as an inhibitory signal to counterbalance TSH-stimulated nuclear factor-κB activation, thus modulating thyroid hormone biosynthesis.Fil: Nicola, Juan Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Peyret, Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Bioquímica Clínica; ArgentinaFil: Nazar, Magalí. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Romero, Jorge Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Lucero, Ariel Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Del Mar Montesinos, María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Bocco, José Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Pellizas, Claudia Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Masini, Ana María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaEndocrine Society2015-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/185963Nicola, Juan Pablo; Peyret, Victoria; Nazar, Magalí; Romero, Jorge Miguel; Lucero, Ariel Maximiliano; et al.; S-nitrosylation of NF-κB p65 inhibits TSH-induced Na+/I- symporter expression; Endocrine Society; Endocrinology; 156; 12; 12-2015; 4741-47540013-72271945-7170CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/ 10.1210/en.2015-1192info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/endo/article/156/12/4741/2423183info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2024-05-08T13:43:44Zoai:ri.conicet.gov.ar:11336/185963instacron: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:34982024-05-08 13:43:44.372CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
score 15.811543

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