Mechanisms by which the orexigen NPY regulates anorexigenic -MSH and TRH

Autores
Cyr, Nicole E; Toorie, Anika M.; Steger, Jennifer S.; Sochat, Matthew M; Hyner, Samantha; Perello, Mario; Stuart, Ronald; Nillni, Eduardo A.
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Protein posttranslational processing is a cellular mechanism fundamental to the generation of bioactive peptides, including the anorectic α-melanocyte-stimulating hormone (α-MSH) and thyrotropin-releasing hormone (TRH) peptides produced in the hypothalamic arcuate (ARC) and paraventricular (PVN) nuclei, respectively. Neuropeptide Y (NPY) promotes positive energy balance in part by suppressing α-MSH and TRH. The mechanism by which NPY regulates α-MSH output, however, is not well understood. Our results reveal that NPY inhibited the posttranslational processing of α-MSH's inactive precursor proopiomelanocortin (POMC) by decreasing the prohormone convertase-2 (PC2). We also found that early growth response protein-1 (Egr-1) and NPY-Y1 receptors mediated the NPY-induced decrease in PC2. NPY given intra-PVN also decreased PC2 in PVN samples, suggesting a reduction in PC2-mediated pro-TRH processing. In addition, NPY attenuated the α-MSH-induced increase in TRH production by two mechanisms. First, NPY decreased α-MSH-induced CREB phosphorylation, which normally enhances TRH transcription. Second, NPY decreased the amount of α-MSH in the PVN. Collectively, these results underscore the significance of the interaction between NPY and α-MSH in the central regulation of energy balance and indicate that posttranslational processing is a mechanism that plays a specific role in this interaction.
Fil: Cyr, Nicole E. University Brown; Estados Unidos
Fil: Toorie, Anika M.. University Brown; Estados Unidos
Fil: Steger, Jennifer S.. University Brown; Estados Unidos
Fil: Sochat, Matthew M. University Brown; Estados Unidos
Fil: Hyner, Samantha. University Brown; Estados Unidos
Fil: Perello, Mario. University Brown; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina
Fil: Stuart, Ronald. University Brown; Estados Unidos
Fil: Nillni, Eduardo A.. University Brown; Estados Unidos
Materia
Hipotalamo
Apetito
Gasto Energetico
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:11336/23970
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/23970
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Mechanisms by which the orexigen NPY regulates anorexigenic -MSH and TRHCyr, Nicole EToorie, Anika M.Steger, Jennifer S.Sochat, Matthew MHyner, SamanthaPerello, MarioStuart, RonaldNillni, Eduardo A.HipotalamoApetitoGasto Energeticohttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Protein posttranslational processing is a cellular mechanism fundamental to the generation of bioactive peptides, including the anorectic α-melanocyte-stimulating hormone (α-MSH) and thyrotropin-releasing hormone (TRH) peptides produced in the hypothalamic arcuate (ARC) and paraventricular (PVN) nuclei, respectively. Neuropeptide Y (NPY) promotes positive energy balance in part by suppressing α-MSH and TRH. The mechanism by which NPY regulates α-MSH output, however, is not well understood. Our results reveal that NPY inhibited the posttranslational processing of α-MSH's inactive precursor proopiomelanocortin (POMC) by decreasing the prohormone convertase-2 (PC2). We also found that early growth response protein-1 (Egr-1) and NPY-Y1 receptors mediated the NPY-induced decrease in PC2. NPY given intra-PVN also decreased PC2 in PVN samples, suggesting a reduction in PC2-mediated pro-TRH processing. In addition, NPY attenuated the α-MSH-induced increase in TRH production by two mechanisms. First, NPY decreased α-MSH-induced CREB phosphorylation, which normally enhances TRH transcription. Second, NPY decreased the amount of α-MSH in the PVN. Collectively, these results underscore the significance of the interaction between NPY and α-MSH in the central regulation of energy balance and indicate that posttranslational processing is a mechanism that plays a specific role in this interaction.Fil: Cyr, Nicole E. University Brown; Estados UnidosFil: Toorie, Anika M.. University Brown; Estados UnidosFil: Steger, Jennifer S.. University Brown; Estados UnidosFil: Sochat, Matthew M. University Brown; Estados UnidosFil: Hyner, Samantha. University Brown; Estados UnidosFil: Perello, Mario. University Brown; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; ArgentinaFil: Stuart, Ronald. University Brown; Estados UnidosFil: Nillni, Eduardo A.. University Brown; Estados UnidosAmerican Physiological Society2013-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/23970Cyr, Nicole E; Toorie, Anika M.; Steger, Jennifer S.; Sochat, Matthew M; Hyner, Samantha; et al.; Mechanisms by which the orexigen NPY regulates anorexigenic -MSH and TRH; American Physiological Society; American Journal Of Physiology-endocrinology And Metabolism; 304; 6; 3-2013; E640-E6500193-1849CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1152/ajpendo.00448.2012info:eu-repo/semantics/altIdentifier/url/http://ajpendo.physiology.org/content/304/6/E640info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:02:27Zoai:ri.conicet.gov.ar:11336/23970instacron: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:34982025-09-03 10:02:27.785CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Mechanisms by which the orexigen NPY regulates anorexigenic -MSH and TRH
title Mechanisms by which the orexigen NPY regulates anorexigenic -MSH and TRH
spellingShingle Mechanisms by which the orexigen NPY regulates anorexigenic -MSH and TRH
Cyr, Nicole E
Hipotalamo
Apetito
Gasto Energetico
title_short Mechanisms by which the orexigen NPY regulates anorexigenic -MSH and TRH
title_full Mechanisms by which the orexigen NPY regulates anorexigenic -MSH and TRH
title_fullStr Mechanisms by which the orexigen NPY regulates anorexigenic -MSH and TRH
title_full_unstemmed Mechanisms by which the orexigen NPY regulates anorexigenic -MSH and TRH
title_sort Mechanisms by which the orexigen NPY regulates anorexigenic -MSH and TRH
dc.creator.none.fl_str_mv Cyr, Nicole E
Toorie, Anika M.
Steger, Jennifer S.
Sochat, Matthew M
Hyner, Samantha
Perello, Mario
Stuart, Ronald
Nillni, Eduardo A.
author Cyr, Nicole E
author_facet Cyr, Nicole E
Toorie, Anika M.
Steger, Jennifer S.
Sochat, Matthew M
Hyner, Samantha
Perello, Mario
Stuart, Ronald
Nillni, Eduardo A.
author_role author
author2 Toorie, Anika M.
Steger, Jennifer S.
Sochat, Matthew M
Hyner, Samantha
Perello, Mario
Stuart, Ronald
Nillni, Eduardo A.
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Hipotalamo
Apetito
Gasto Energetico
topic Hipotalamo
Apetito
Gasto Energetico
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Protein posttranslational processing is a cellular mechanism fundamental to the generation of bioactive peptides, including the anorectic α-melanocyte-stimulating hormone (α-MSH) and thyrotropin-releasing hormone (TRH) peptides produced in the hypothalamic arcuate (ARC) and paraventricular (PVN) nuclei, respectively. Neuropeptide Y (NPY) promotes positive energy balance in part by suppressing α-MSH and TRH. The mechanism by which NPY regulates α-MSH output, however, is not well understood. Our results reveal that NPY inhibited the posttranslational processing of α-MSH's inactive precursor proopiomelanocortin (POMC) by decreasing the prohormone convertase-2 (PC2). We also found that early growth response protein-1 (Egr-1) and NPY-Y1 receptors mediated the NPY-induced decrease in PC2. NPY given intra-PVN also decreased PC2 in PVN samples, suggesting a reduction in PC2-mediated pro-TRH processing. In addition, NPY attenuated the α-MSH-induced increase in TRH production by two mechanisms. First, NPY decreased α-MSH-induced CREB phosphorylation, which normally enhances TRH transcription. Second, NPY decreased the amount of α-MSH in the PVN. Collectively, these results underscore the significance of the interaction between NPY and α-MSH in the central regulation of energy balance and indicate that posttranslational processing is a mechanism that plays a specific role in this interaction.
Fil: Cyr, Nicole E. University Brown; Estados Unidos
Fil: Toorie, Anika M.. University Brown; Estados Unidos
Fil: Steger, Jennifer S.. University Brown; Estados Unidos
Fil: Sochat, Matthew M. University Brown; Estados Unidos
Fil: Hyner, Samantha. University Brown; Estados Unidos
Fil: Perello, Mario. University Brown; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina
Fil: Stuart, Ronald. University Brown; Estados Unidos
Fil: Nillni, Eduardo A.. University Brown; Estados Unidos
description Protein posttranslational processing is a cellular mechanism fundamental to the generation of bioactive peptides, including the anorectic α-melanocyte-stimulating hormone (α-MSH) and thyrotropin-releasing hormone (TRH) peptides produced in the hypothalamic arcuate (ARC) and paraventricular (PVN) nuclei, respectively. Neuropeptide Y (NPY) promotes positive energy balance in part by suppressing α-MSH and TRH. The mechanism by which NPY regulates α-MSH output, however, is not well understood. Our results reveal that NPY inhibited the posttranslational processing of α-MSH's inactive precursor proopiomelanocortin (POMC) by decreasing the prohormone convertase-2 (PC2). We also found that early growth response protein-1 (Egr-1) and NPY-Y1 receptors mediated the NPY-induced decrease in PC2. NPY given intra-PVN also decreased PC2 in PVN samples, suggesting a reduction in PC2-mediated pro-TRH processing. In addition, NPY attenuated the α-MSH-induced increase in TRH production by two mechanisms. First, NPY decreased α-MSH-induced CREB phosphorylation, which normally enhances TRH transcription. Second, NPY decreased the amount of α-MSH in the PVN. Collectively, these results underscore the significance of the interaction between NPY and α-MSH in the central regulation of energy balance and indicate that posttranslational processing is a mechanism that plays a specific role in this interaction.
publishDate 2013
dc.date.none.fl_str_mv 2013-03
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/11336/23970
Cyr, Nicole E; Toorie, Anika M.; Steger, Jennifer S.; Sochat, Matthew M; Hyner, Samantha; et al.; Mechanisms by which the orexigen NPY regulates anorexigenic -MSH and TRH; American Physiological Society; American Journal Of Physiology-endocrinology And Metabolism; 304; 6; 3-2013; E640-E650
0193-1849
CONICET Digital
CONICET
url http://hdl.handle.net/11336/23970
identifier_str_mv Cyr, Nicole E; Toorie, Anika M.; Steger, Jennifer S.; Sochat, Matthew M; Hyner, Samantha; et al.; Mechanisms by which the orexigen NPY regulates anorexigenic -MSH and TRH; American Physiological Society; American Journal Of Physiology-endocrinology And Metabolism; 304; 6; 3-2013; E640-E650
0193-1849
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1152/ajpendo.00448.2012
info:eu-repo/semantics/altIdentifier/url/http://ajpendo.physiology.org/content/304/6/E640
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 American Physiological Society
publisher.none.fl_str_mv American Physiological 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
_version_ 1842269756176990208
score 13.13397

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