Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT)

Autores
Prados, Maria Belen; Caramelo, Julio Javier; Miranda, Silvia Esther
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
UDP-Glucose:glycoprotein glucosyltransferase (UGGT) is a central component of the endoplasmic reticulum (ER) glycoprotein-folding quality control system, which prevents the exit of partially folded species. UGGT activity can be regulated by the accumulation of misfolded proteins in the ER, a stimulus that triggers a complex signaling pathway known as unfolded protein response (UPR) which is closely associated with inflammation and disease. In this work, we investigated the effect of progesterone (P4) on the expression and activity of UGGT in a mouse hybridoma. We detected the expression of two UGGT isoforms, UGGT1 and UGGT2, and demonstrated that both isoforms are active in these cells. Interestingly, the expression of each isoform is regulated by high physiological P4 concentrations. This work provides the first evidence of a hormonal regulation of UGGT isoform expression and activity, which might influence the glycoprotein quality control mechanism. These findings could contribute to the study of pathologies triggered by the accumulation of misfolded proteins.
Fil: Prados, Maria Belen. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Cardiológicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Cardiológicas; Argentina
Fil: Caramelo, Julio Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Miranda, Silvia Esther. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Cardiológicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Cardiológicas; Argentina
Materia
Progesterone
Endoplasmic Reticulum Quality Control
Udp-Glc: Glycoprotein Glucosyltransferase
Upr
Folding
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/16769
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/16769
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT)Prados, Maria BelenCaramelo, Julio JavierMiranda, Silvia EstherProgesteroneEndoplasmic Reticulum Quality ControlUdp-Glc: Glycoprotein GlucosyltransferaseUprFoldinghttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1UDP-Glucose:glycoprotein glucosyltransferase (UGGT) is a central component of the endoplasmic reticulum (ER) glycoprotein-folding quality control system, which prevents the exit of partially folded species. UGGT activity can be regulated by the accumulation of misfolded proteins in the ER, a stimulus that triggers a complex signaling pathway known as unfolded protein response (UPR) which is closely associated with inflammation and disease. In this work, we investigated the effect of progesterone (P4) on the expression and activity of UGGT in a mouse hybridoma. We detected the expression of two UGGT isoforms, UGGT1 and UGGT2, and demonstrated that both isoforms are active in these cells. Interestingly, the expression of each isoform is regulated by high physiological P4 concentrations. This work provides the first evidence of a hormonal regulation of UGGT isoform expression and activity, which might influence the glycoprotein quality control mechanism. These findings could contribute to the study of pathologies triggered by the accumulation of misfolded proteins.Fil: Prados, Maria Belen. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Cardiológicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Cardiológicas; ArgentinaFil: Caramelo, Julio Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaFil: Miranda, Silvia Esther. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Cardiológicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Cardiológicas; ArgentinaElsevier Science2013-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/16769Prados, Maria Belen; Caramelo, Julio Javier; Miranda, Silvia Esther; Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT); Elsevier Science; Biochimica Et Biophysica Acta-molecular Cell Research; 1833; 12; 12-2013; 3368-33740167-4889enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0167488913003443info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamcr.2013.09.022info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:01:46Zoai:ri.conicet.gov.ar:11336/16769instacron: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 10:01:46.557CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT)
title Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT)
spellingShingle Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT)
Prados, Maria Belen
Progesterone
Endoplasmic Reticulum Quality Control
Udp-Glc: Glycoprotein Glucosyltransferase
Upr
Folding
title_short Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT)
title_full Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT)
title_fullStr Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT)
title_full_unstemmed Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT)
title_sort Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT)
dc.creator.none.fl_str_mv Prados, Maria Belen
Caramelo, Julio Javier
Miranda, Silvia Esther
author Prados, Maria Belen
author_facet Prados, Maria Belen
Caramelo, Julio Javier
Miranda, Silvia Esther
author_role author
author2 Caramelo, Julio Javier
Miranda, Silvia Esther
author2_role author
author
dc.subject.none.fl_str_mv Progesterone
Endoplasmic Reticulum Quality Control
Udp-Glc: Glycoprotein Glucosyltransferase
Upr
Folding
topic Progesterone
Endoplasmic Reticulum Quality Control
Udp-Glc: Glycoprotein Glucosyltransferase
Upr
Folding
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv UDP-Glucose:glycoprotein glucosyltransferase (UGGT) is a central component of the endoplasmic reticulum (ER) glycoprotein-folding quality control system, which prevents the exit of partially folded species. UGGT activity can be regulated by the accumulation of misfolded proteins in the ER, a stimulus that triggers a complex signaling pathway known as unfolded protein response (UPR) which is closely associated with inflammation and disease. In this work, we investigated the effect of progesterone (P4) on the expression and activity of UGGT in a mouse hybridoma. We detected the expression of two UGGT isoforms, UGGT1 and UGGT2, and demonstrated that both isoforms are active in these cells. Interestingly, the expression of each isoform is regulated by high physiological P4 concentrations. This work provides the first evidence of a hormonal regulation of UGGT isoform expression and activity, which might influence the glycoprotein quality control mechanism. These findings could contribute to the study of pathologies triggered by the accumulation of misfolded proteins.
Fil: Prados, Maria Belen. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Cardiológicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Cardiológicas; Argentina
Fil: Caramelo, Julio Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Miranda, Silvia Esther. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Cardiológicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Cardiológicas; Argentina
description UDP-Glucose:glycoprotein glucosyltransferase (UGGT) is a central component of the endoplasmic reticulum (ER) glycoprotein-folding quality control system, which prevents the exit of partially folded species. UGGT activity can be regulated by the accumulation of misfolded proteins in the ER, a stimulus that triggers a complex signaling pathway known as unfolded protein response (UPR) which is closely associated with inflammation and disease. In this work, we investigated the effect of progesterone (P4) on the expression and activity of UGGT in a mouse hybridoma. We detected the expression of two UGGT isoforms, UGGT1 and UGGT2, and demonstrated that both isoforms are active in these cells. Interestingly, the expression of each isoform is regulated by high physiological P4 concentrations. This work provides the first evidence of a hormonal regulation of UGGT isoform expression and activity, which might influence the glycoprotein quality control mechanism. These findings could contribute to the study of pathologies triggered by the accumulation of misfolded proteins.
publishDate 2013
dc.date.none.fl_str_mv 2013-12
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/11336/16769
Prados, Maria Belen; Caramelo, Julio Javier; Miranda, Silvia Esther; Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT); Elsevier Science; Biochimica Et Biophysica Acta-molecular Cell Research; 1833; 12; 12-2013; 3368-3374
0167-4889
url http://hdl.handle.net/11336/16769
identifier_str_mv Prados, Maria Belen; Caramelo, Julio Javier; Miranda, Silvia Esther; Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT); Elsevier Science; Biochimica Et Biophysica Acta-molecular Cell Research; 1833; 12; 12-2013; 3368-3374
0167-4889
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0167488913003443
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamcr.2013.09.022
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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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score 13.13397

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