CNOT7/hCAF1 is involved in ICAM-1 and IL-8 regulation by tristetraprolin

Shi, Jun; Li, Jiashu; Hu, Rong; Shi, Yi; Su, Xin; Li, Qin; Zhang, Feng

doi:10.1016/j.cellsig.2014.07.020

Cited by 13 publications

(25 citation statements)

References 25 publications

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“…The regulation of ICAM-1 mRNA stability is a well-accepted and important mechanism underlying posttranscriptional control of ICAM-1 gene expression [40, 41]. PPARα agonists have already been implicated in regulating mRNA stability of other genes.…”

Section: Discussionmentioning

confidence: 99%

Peroxisome proliferator-activated receptor (PPAR) α and δ activators induce ICAM-1 expression in quiescent non stimulated endothelial cells

et al. 2016

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BackgroundPeroxisome proliferator-activated receptors (PPARs) are ligand-activated transcription factors that are implicated in the regulation of lipid and glucose homeostasis. PPAR agonists have been shown to control inflammatory processes, in part by inhibiting the expression of distinct proinflammatory genes such as vascular cell adhesion molecule-1 (VCAM-1), IL-8, and intercellular adhesion molecule-1 (ICAM-1). ICAM-1 is an important endothelial membrane receptor that facilitates the transmigration of leukocytes across the endothelium. To date, the influence of PPARα and δ activators on the expression of ICAM-1 in non-induced, quiescent endothelial cells has been unclear. Therefore, we examined the effects of various PPARα and δ agonists on the expression of ICAM-1 in non-stimulated primary human endothelial cells.ResultsWe found that PPARα and PPARδ agonists significantly induced ICAM-1 surface, intracellular protein, and mRNA expression in a time and concentration-dependent manner. The PPARδ induced ICAM-1 expression could be paralleled with a significantly increased T-cell adherence to the endothelial cells whereas PPARα failed to do so. Transcriptional activity studies using an ICAM-1 reporter gene constructs revealed that PPARδ, but not PPARα agonists induced gene expression by stimulating ICAM-1 promoter activity via an Sp1 transcription factor binding site and inhibit the binding of the transcription factors Sp1 and Sp3. Furthermore, we performed mRNA stability assays and found that PPARα and PPARδ agonists increased ICAM-1 mRNA stability.ConclusionTherefore, our data provide the first evidence that PPARα and PPARδ agonists induce ICAM-1 expression in non-stimulated endothelial cells via transcriptional and posttranscriptional mechanisms.

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Section: Discussionmentioning

confidence: 99%

Peroxisome proliferator-activated receptor (PPAR) α and δ activators induce ICAM-1 expression in quiescent non stimulated endothelial cells

et al. 2016

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“…4C, [22]). It is known that CNOT7 silencing stabilized ICAM1 and CXCIL8 mRNAs and increased ICAM-1 and IL-8 production following TNF-α stimulation [23]. It is of special interest as osteopontin, a factor that up-regulates ICAM-1 (Fig.…”

Section: Quantitative Real-time Pcr (Qpcr) Of Selected Gravitationallmentioning

confidence: 99%

“…This interesting interaction reveals that mechanical vibration might influence cell adhesion and survival of the chondrocytes. In human pulmonary microvascular endothelial cells CNOT7/hCAF1 are involved in ICAM-1 and IL-8 regulation by tristetraprolin [23].…”

Section: Pathway Analyses Revealed Interactions Of Icam With Psmd4 Anmentioning

confidence: 99%

Pathway Analysis Hints Towards Beneficial Effects of Long-Term Vibration on Human Chondrocytes

Lützenberg

Solano

Buken

et al. 2018

Cell Physiol Biochem

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Background/Aims: Spaceflight negatively influences the function of cartilage tissue in vivo. In vitro human chondrocytes exhibit an altered gene expression of inflammation markers after a two-hour exposure to vibration. Little is known about the impact of long-term vibration on chondrocytes. Methods: Human cartilage cells were exposed for up to 24 h (VIB) on a specialised vibration platform (Vibraplex) simulating the vibration profile which occurs during parabolic flights and compared to static control conditions (CON). Afterwards, they were investigated by phase-contrast microscopy, rhodamine phalloidin staining, microarray analysis, qPCR and western blot analysis. Results: Morphological investigations revealed no changes between CON and VIB chondrocytes. F-Actin staining showed no alterations of the cytoskeleton in VIB compared with CON cells. DAPI and TUNEL staining did not identify apoptotic cells. ICAM-1 was elevated and vimentin, beta-tubulin and osteopontin proteins were significantly reduced in VIB compared to CON cells. qPCR of cytoskeletal genes, ITGB1, SOX3, SOX5, SOX9 did not reveal differential regulations. Microarray analysis detected 13 differentially expressed genes, mostly indicating unspecific stimulations. Pathway analyses demonstrated interactions of PSMD4 and CNOT7 with ICAM. Conclusions: Long-term vibration did not damage human chondrocytes in vitro. The reduction of osteopontin protein and the down-regulation of PSMD4 and TBX15 gene expression suggest that in vitro long-term vibration might even positively influence cultured chondrocytes.

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“…Several independent groups have reported that mammalian TTP promotes deadenylation of target mRNA by recruiting the carbon catabolite repressor protein 4-negative on TATA-less (CCR4–NOT) deadenylase complex, a large (1 mDa) complex containing at least 10 subunits [31,56–59]. The Drosophila melanogaster orthologue of TTP employs a similar mechanism to regulate the expression of anti-microbial products [60,61].…”

Section: Ttp Function Is Modulated By Phosphorylationmentioning

confidence: 99%

The control of inflammation via the phosphorylation and dephosphorylation of tristetraprolin: a tale of two phosphatases

Clark

Dean

2016

Biochemical Society Transactions

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Twenty years ago, the first description of a tristetraprolin (TTP) knockout mouse highlighted the fundamental role of TTP in the restraint of inflammation. Since then, work from several groups has generated a detailed picture of the expression and function of TTP. It is a sequence-specific RNA-binding protein that orchestrates the deadenylation and degradation of several mRNAs encoding inflammatory mediators. It is very extensively post-translationally modified, with more than 30 phosphorylations that are supported by at least two independent lines of evidence. The phosphorylation of two particular residues, serines 52 and 178 of mouse TTP (serines 60 and 186 of the human orthologue), has profound effects on the expression, function and localisation of TTP. Here, we discuss the control of TTP biology via its phosphorylation and dephosphorylation, with a particular focus on recent advances and on questions that remain unanswered.

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CNOT7/hCAF1 is involved in ICAM-1 and IL-8 regulation by tristetraprolin

Cited by 13 publications

References 25 publications

Peroxisome proliferator-activated receptor (PPAR) α and δ activators induce ICAM-1 expression in quiescent non stimulated endothelial cells

Peroxisome proliferator-activated receptor (PPAR) α and δ activators induce ICAM-1 expression in quiescent non stimulated endothelial cells

Pathway Analysis Hints Towards Beneficial Effects of Long-Term Vibration on Human Chondrocytes

The control of inflammation via the phosphorylation and dephosphorylation of tristetraprolin: a tale of two phosphatases

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