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Dexamethasone-induced selenoprotein S degradation is required for adipogenesis

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Title: Dexamethasone-induced selenoprotein S degradation is required for adipogenesis
Authors: Choon Young Kim, Kee-Hong Kim
Source: Journal of Lipid Research, Vol 54, Iss 8, Pp 2069-2082 (2013)
Publisher Information: Elsevier, 2013.
Publication Year: 2013
Collection: LCC:Biochemistry
Subject Terms: 3T3-L1, adipocytes, glucocorticoid, endoplasmic reticulum stress, ubiquitin-proteasome system, endoplasmic reticulum-associated protein degradation, Biochemistry, QD415-436
More Details: Although adipogenesis is associated with induction of endoplasmic reticulum (ER) stress, the role of selenoprotein S (SEPS1), an ER resident selenoprotein known to regulate ER stress and ER-associated protein degradation, is unknown. We found an inverse relationship between SEPS1 level in adipose tissue and adiposity in mice. While SEPS1 expression was increased during adipogenesis, a markedly reduced SEPS1 protein level was found in the early phase of adipogenesis due to dexamethasone (DEX)-induced proteosomal degradation of SEPS1. Overexpression of SEPS1 in the early phase of cell differentiation resulted in impairment of adipogenesis with reduced levels of CCAAT/enhancer binding protein α and other adipocyte marker genes during the course of adipogenesis. Conversely, knockdown of SEPS1 resulted in the promotion of adipogenesis. Additionally, altered SEPS1 expression was associated with changes in expression of ER stress marker genes in the early phase of adipogenesis, and ubiquitin-proteasome system (UPS)-related ubiquitination and proteasome function. Our study reveals that SEPS1 is a novel anti-adipogenic selenoprotein that modulates ER stress- and UPS-dependent adipogenesis. Our results also identifies a novel function of DEX in the regulation of adipogenesis through induction of SEPS1 degradation. Taken together, DEX-dependent degradation of SEPS1 in the early phase of adipogenesis is necessary for initiating ER stress- and UPS-dependent maturation of adipocytes.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 0022-2275
Relation: http://www.sciencedirect.com/science/article/pii/S0022227520375246; https://doaj.org/toc/0022-2275
DOI: 10.1194/jlr.M034603
Access URL: https://doaj.org/article/c465dab478d7403ea14546d09fc15e78
Accession Number: edsdoj.465dab478d7403ea14546d09fc15e78
Database: Directory of Open Access Journals
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  Data: Dexamethasone-induced selenoprotein S degradation is required for adipogenesis
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  Data: Journal of Lipid Research, Vol 54, Iss 8, Pp 2069-2082 (2013)
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  Data: Elsevier, 2013.
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  Data: Although adipogenesis is associated with induction of endoplasmic reticulum (ER) stress, the role of selenoprotein S (SEPS1), an ER resident selenoprotein known to regulate ER stress and ER-associated protein degradation, is unknown. We found an inverse relationship between SEPS1 level in adipose tissue and adiposity in mice. While SEPS1 expression was increased during adipogenesis, a markedly reduced SEPS1 protein level was found in the early phase of adipogenesis due to dexamethasone (DEX)-induced proteosomal degradation of SEPS1. Overexpression of SEPS1 in the early phase of cell differentiation resulted in impairment of adipogenesis with reduced levels of CCAAT/enhancer binding protein α and other adipocyte marker genes during the course of adipogenesis. Conversely, knockdown of SEPS1 resulted in the promotion of adipogenesis. Additionally, altered SEPS1 expression was associated with changes in expression of ER stress marker genes in the early phase of adipogenesis, and ubiquitin-proteasome system (UPS)-related ubiquitination and proteasome function. Our study reveals that SEPS1 is a novel anti-adipogenic selenoprotein that modulates ER stress- and UPS-dependent adipogenesis. Our results also identifies a novel function of DEX in the regulation of adipogenesis through induction of SEPS1 degradation. Taken together, DEX-dependent degradation of SEPS1 in the early phase of adipogenesis is necessary for initiating ER stress- and UPS-dependent maturation of adipocytes.
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