Dexamethasone-induced selenoprotein S degradation is required for adipogenesis
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 ti...
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| Format: | Article |
| Language: | English |
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Elsevier
2013-08-01
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| Series: | Journal of Lipid Research |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520375246 |
| _version_ | 1819077198828535808 |
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| author | Choon Young Kim Kee-Hong Kim |
| author_facet | Choon Young Kim Kee-Hong Kim |
| author_sort | Choon Young Kim |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-21T18:53:24Z |
| format | Article |
| id | doaj.art-c465dab478d7403ea14546d09fc15e78 |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-21T18:53:24Z |
| publishDate | 2013-08-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-c465dab478d7403ea14546d09fc15e782022-12-21T18:53:41ZengElsevierJournal of Lipid Research0022-22752013-08-0154820692082Dexamethasone-induced selenoprotein S degradation is required for adipogenesisChoon Young Kim0Kee-Hong Kim1Department of Food Science, Purdue University, West Lafayette, IN 47907To whom correspondence should be addressed; Department of Food Science, Purdue University, West Lafayette, IN 47907Although 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.http://www.sciencedirect.com/science/article/pii/S00222275203752463T3-L1adipocytesglucocorticoidendoplasmic reticulum stressubiquitin-proteasome systemendoplasmic reticulum-associated protein degradation |
| spellingShingle | Choon Young Kim Kee-Hong Kim Dexamethasone-induced selenoprotein S degradation is required for adipogenesis Journal of Lipid Research 3T3-L1 adipocytes glucocorticoid endoplasmic reticulum stress ubiquitin-proteasome system endoplasmic reticulum-associated protein degradation |
| title | Dexamethasone-induced selenoprotein S degradation is required for adipogenesis |
| title_full | Dexamethasone-induced selenoprotein S degradation is required for adipogenesis |
| title_fullStr | Dexamethasone-induced selenoprotein S degradation is required for adipogenesis |
| title_full_unstemmed | Dexamethasone-induced selenoprotein S degradation is required for adipogenesis |
| title_short | Dexamethasone-induced selenoprotein S degradation is required for adipogenesis |
| title_sort | dexamethasone induced selenoprotein s degradation is required for adipogenesis |
| topic | 3T3-L1 adipocytes glucocorticoid endoplasmic reticulum stress ubiquitin-proteasome system endoplasmic reticulum-associated protein degradation |
| url | http://www.sciencedirect.com/science/article/pii/S0022227520375246 |
| work_keys_str_mv | AT choonyoungkim dexamethasoneinducedselenoproteinsdegradationisrequiredforadipogenesis AT keehongkim dexamethasoneinducedselenoproteinsdegradationisrequiredforadipogenesis |