Thioredoxin-interacting protein gene expression via MondoA is rapidly and transiently suppressed during inflammatory responses.
Whereas accumulating evidence indicates that a number of inflammatory genes are induced by activation of nuclear factor-κB and other transcription factors, less is known about genes that are suppressed by proinflammatory stimuli. Here we show that expression of thioredoxin-interacting protein (Txnip...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3592832?pdf=render |
| _version_ | 1819176198971850752 |
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| author | Yasuyoshi Kanari Yuki Sato Satoru Aoyama Tatsushi Muta |
| author_facet | Yasuyoshi Kanari Yuki Sato Satoru Aoyama Tatsushi Muta |
| author_sort | Yasuyoshi Kanari |
| collection | DOAJ |
| description | Whereas accumulating evidence indicates that a number of inflammatory genes are induced by activation of nuclear factor-κB and other transcription factors, less is known about genes that are suppressed by proinflammatory stimuli. Here we show that expression of thioredoxin-interacting protein (Txnip) is dramatically suppressed both in mRNA and protein levels upon stimulation with lipopolysaccharide in mouse and human macrophages. In addition to lipopolysaccharide, a Toll-like receptor 4 ligand, stimulation with other Toll-like receptor ligands such as CpG DNA also suppressed Txnip expression. Not only the Toll-like receptor ligands, but also other proinflammatory stimulators, such as interleukin-1β and tumor necrosis factor-α elicited the similar response in fibroblasts. Suppression of Txnip by lipopolysaccharide is accompanied by a decrease of the glucose sensing transcription factor MondoA in the nuclei and dissociation of the MondoA:Mlx complex that bound to the carbohydrate-response elements in the Txnip promoter in unstimulated cells. Lipopolysaccharide-mediated decrease of nuclear MondoA was inhibited in the presence of 2-deoxyglucose. Furthermore, blockage of glyceraldehyde-3-phosphate dehydrogenase by iodoacetate alleviated the suppression of Txnip mRNA by lipopolysaccharide, suggesting the involvement of glucose-metabolites in the regulation. Since Txnip is implicated in the regulation of glucose metabolism, this observation links between inflammatory responses and metabolic regulation. |
| first_indexed | 2024-12-22T21:06:57Z |
| format | Article |
| id | doaj.art-d5ccdcbb3c5d44f9918098a84055590c |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-22T21:06:57Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-d5ccdcbb3c5d44f9918098a84055590c2022-12-21T18:12:38ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0183e5902610.1371/journal.pone.0059026Thioredoxin-interacting protein gene expression via MondoA is rapidly and transiently suppressed during inflammatory responses.Yasuyoshi KanariYuki SatoSatoru AoyamaTatsushi MutaWhereas accumulating evidence indicates that a number of inflammatory genes are induced by activation of nuclear factor-κB and other transcription factors, less is known about genes that are suppressed by proinflammatory stimuli. Here we show that expression of thioredoxin-interacting protein (Txnip) is dramatically suppressed both in mRNA and protein levels upon stimulation with lipopolysaccharide in mouse and human macrophages. In addition to lipopolysaccharide, a Toll-like receptor 4 ligand, stimulation with other Toll-like receptor ligands such as CpG DNA also suppressed Txnip expression. Not only the Toll-like receptor ligands, but also other proinflammatory stimulators, such as interleukin-1β and tumor necrosis factor-α elicited the similar response in fibroblasts. Suppression of Txnip by lipopolysaccharide is accompanied by a decrease of the glucose sensing transcription factor MondoA in the nuclei and dissociation of the MondoA:Mlx complex that bound to the carbohydrate-response elements in the Txnip promoter in unstimulated cells. Lipopolysaccharide-mediated decrease of nuclear MondoA was inhibited in the presence of 2-deoxyglucose. Furthermore, blockage of glyceraldehyde-3-phosphate dehydrogenase by iodoacetate alleviated the suppression of Txnip mRNA by lipopolysaccharide, suggesting the involvement of glucose-metabolites in the regulation. Since Txnip is implicated in the regulation of glucose metabolism, this observation links between inflammatory responses and metabolic regulation.http://europepmc.org/articles/PMC3592832?pdf=render |
| spellingShingle | Yasuyoshi Kanari Yuki Sato Satoru Aoyama Tatsushi Muta Thioredoxin-interacting protein gene expression via MondoA is rapidly and transiently suppressed during inflammatory responses. PLoS ONE |
| title | Thioredoxin-interacting protein gene expression via MondoA is rapidly and transiently suppressed during inflammatory responses. |
| title_full | Thioredoxin-interacting protein gene expression via MondoA is rapidly and transiently suppressed during inflammatory responses. |
| title_fullStr | Thioredoxin-interacting protein gene expression via MondoA is rapidly and transiently suppressed during inflammatory responses. |
| title_full_unstemmed | Thioredoxin-interacting protein gene expression via MondoA is rapidly and transiently suppressed during inflammatory responses. |
| title_short | Thioredoxin-interacting protein gene expression via MondoA is rapidly and transiently suppressed during inflammatory responses. |
| title_sort | thioredoxin interacting protein gene expression via mondoa is rapidly and transiently suppressed during inflammatory responses |
| url | http://europepmc.org/articles/PMC3592832?pdf=render |
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