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A mechanism of suppression of TGF–β/SMAD signaling by NF-κB/RelA
Open accessAbstract
A number of pathogenic and proinflammatory stimuli, and the transforming growth factor-β (TGF-β) exert opposing activities in cellular and immune responses. Here we show that the RelA subunit of nuclear factor κB (NF-κB/RelA) is necessary for the inhibition of TGF-β-induced phosphorylation, nuclear translocation, and DNA binding of SMAD signaling complexes by tumor necrosis factor-α (TNF-α). The antagonism is mediated through up-regulation of Smad7 synthesis and induction of stable associations between ligand-activated TGF-β receptors and inhibitory Smad7. Down-regulation of endogenous Smad7 by expression of antisense mRNA releases TGF-β/SMAD-induced transcriptional responses from suppression by cytokine-activated NF-κB/RelA. Following stimulation with bacterial lipopolysaccharide (LPS), or the proinflammatory cytokines TNF-α and interleukin-1β (IL-1β, NF-κB/RelA induces Smad7 synthesis through activation of Smad7 gene transcription. These results suggest a mechanism of suppression of TGF-β/SMAD signaling by opposing stimuli mediated through the activation of inhibitory Smad7 by NF-κB/RelA.
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Metadata
- Authors
- Bitzer, M., von Gersdorff, G., Liang, D., Dominguez-Rosales, A., Beg, A. A., Rojkind, M., & Böttinger, E. P.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2000-01-15
- Volume
- 14
- Issue
- 2
- Pages
- 187-197
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W4297022993
- Cited by
- 421
- References
- 1
- Type
- posted content
- Language
- en
- Open access
- diamond
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