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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Detalles Bibliográficos
Autores: 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
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2015
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/185963
Acceso en línea:http://hdl.handle.net/11336/185963
Access Level:acceso abierto
Palabra clave:S-NITROSYLATION
NFKB
NIS
https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
Descripción
Sumario: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.