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

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 stimulu...

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Autores principales: Prados, M.B., Caramelo, J.J., Miranda, S.E.
Formato: Artículo publishedVersion
Publicado: 2013
Materias:
DJN
P4
UPR
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_01674889_v1833_n12_p3368_Prados
http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_01674889_v1833_n12_p3368_Prados_oai
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id I28-R145-paper_01674889_v1833_n12_p3368_Prados_oai
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spelling I28-R145-paper_01674889_v1833_n12_p3368_Prados_oai2020-10-19 Prados, M.B. Caramelo, J.J. Miranda, S.E. 2013 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. © 2013 Elsevier B.V. application/pdf http://hdl.handle.net/20.500.12110/paper_01674889_v1833_n12_p3368_Prados info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar Biochim. Biophys. Acta Mol. Cell Res. 2013;1833(12):3368-3374 DJN Endoplasmic reticulum quality control Folding P4 Progesterone UDP-Glc: glycoprotein glucosyltransferase UGGT UPR glucosyltransferase glycoprotein progesterone UDP glucose glycoprotein glucosyltransferase unclassified drug animal experiment animal model article cell proliferation cellular distribution controlled study endoplasmic reticulum enzyme activity gene expression gene silencing hormonal regulation hybridoma hybridoma cell culture intracellular signaling mouse nonhuman priority journal protein analysis protein expression protein folding protein function protein synthesis quality control unfolded protein response Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT) info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_01674889_v1833_n12_p3368_Prados_oai
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-145
collection Repositorio Digital de la Universidad de Buenos Aires (UBA)
topic DJN
Endoplasmic reticulum quality control
Folding
P4
Progesterone
UDP-Glc: glycoprotein glucosyltransferase
UGGT
UPR
glucosyltransferase
glycoprotein
progesterone
UDP glucose glycoprotein glucosyltransferase
unclassified drug
animal experiment
animal model
article
cell proliferation
cellular distribution
controlled study
endoplasmic reticulum
enzyme activity
gene expression
gene silencing
hormonal regulation
hybridoma
hybridoma cell culture
intracellular signaling
mouse
nonhuman
priority journal
protein analysis
protein expression
protein folding
protein function
protein synthesis
quality control
unfolded protein response
spellingShingle DJN
Endoplasmic reticulum quality control
Folding
P4
Progesterone
UDP-Glc: glycoprotein glucosyltransferase
UGGT
UPR
glucosyltransferase
glycoprotein
progesterone
UDP glucose glycoprotein glucosyltransferase
unclassified drug
animal experiment
animal model
article
cell proliferation
cellular distribution
controlled study
endoplasmic reticulum
enzyme activity
gene expression
gene silencing
hormonal regulation
hybridoma
hybridoma cell culture
intracellular signaling
mouse
nonhuman
priority journal
protein analysis
protein expression
protein folding
protein function
protein synthesis
quality control
unfolded protein response
Prados, M.B.
Caramelo, J.J.
Miranda, S.E.
Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT)
topic_facet DJN
Endoplasmic reticulum quality control
Folding
P4
Progesterone
UDP-Glc: glycoprotein glucosyltransferase
UGGT
UPR
glucosyltransferase
glycoprotein
progesterone
UDP glucose glycoprotein glucosyltransferase
unclassified drug
animal experiment
animal model
article
cell proliferation
cellular distribution
controlled study
endoplasmic reticulum
enzyme activity
gene expression
gene silencing
hormonal regulation
hybridoma
hybridoma cell culture
intracellular signaling
mouse
nonhuman
priority journal
protein analysis
protein expression
protein folding
protein function
protein synthesis
quality control
unfolded protein response
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. © 2013 Elsevier B.V.
format Artículo
Artículo
publishedVersion
author Prados, M.B.
Caramelo, J.J.
Miranda, S.E.
author_facet Prados, M.B.
Caramelo, J.J.
Miranda, S.E.
author_sort Prados, M.B.
title Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT)
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)
publishDate 2013
url http://hdl.handle.net/20.500.12110/paper_01674889_v1833_n12_p3368_Prados
http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_01674889_v1833_n12_p3368_Prados_oai
work_keys_str_mv AT pradosmb progesteroneregulatestheexpressionandactivityoftwomouseisoformsoftheglycoproteinfoldingsensorudpglcglycoproteinglucosyltransferaseuggt
AT caramelojj progesteroneregulatestheexpressionandactivityoftwomouseisoformsoftheglycoproteinfoldingsensorudpglcglycoproteinglucosyltransferaseuggt
AT mirandase progesteroneregulatestheexpressionandactivityoftwomouseisoformsoftheglycoproteinfoldingsensorudpglcglycoproteinglucosyltransferaseuggt
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