Tumor necrosis factor-alpha induction of novel gene products in human endothelial cells including a macrophage-specific chemotaxin.

Dixit, Vishva M.; Green, S; Sarma, Vidya; Holzman, Lawrence B.; Wolf, F W; O’Rourke, Karen; Ward, Peter A.; Prochownik, Edward V.; Marks, Rebecca A.

doi:10.1016/s0021-9258(19)39896-5

Cited by 351 publications

(44 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…TNF-a is an inducer of A20 expression [Dixit et al, 1990], and A20 is an important regulator for NOD2-induced signal transduction [Hitotsumatsu et al, 2008], so we guess that TNF-a should decrease NOD2-induced response by up-regulation of A20. In this study, we found that TNF-a induced the up-regulation of A20, but TNF-a pretreatment of THP-1 cells increased MDP-induced cytokine production.…”

Section: Discussionmentioning

confidence: 99%

“…TNF-a has been reported to up-regulate NOD2 expression in intestinal epithelial cells [Rosenstiel et al, 2003]. However, TNF-a also induces the expression of A20 [Dixit et al, 1990], an ubiquitin-editing enzyme which plays important roles in the negative regulation of inflammatory response [Catrysse et al, 2014]. So the roles of TNF-a on NOD2-induced inflammatory response are uncertain.…”

Section: Tnf-a Pre-treatment Up-regulates Mdp-induced Production Of Cytokinesmentioning

confidence: 99%

See 1 more Smart Citation

TNF‐α‐Induced NOD2 and RIP2 Contribute to the Up‐Regulation of Cytokines Induced by MDP in Monocytic THP‐1 Cells

Chen

Xiao

Xie

et al. 2018

J of Cellular Biochemistry

View full text Add to dashboard Cite

Nucleotide-binding oligomerization domain containing 2 (NOD2)-induced signal transduction and cytokine production is regulated by a number of factors. However, the feedback effect of the pro-inflammatory TNF-α on NOD2-induced inflammation is not fully understood. In this study, we found unexpectedly that TNF-α up-regulated NOD2 ligand MDP-induced production of the CXC chemokines, including CXCL1, 2, and 8, and the pro-inflammatory cytokines, including IL-1β, IL-6, and TNF-α, in a dose-dependent manner at both mRNA and protein levels in monocytic THP-1 cells. Though TNF-α induced the up-regulation of ubiquitin-editing enzyme A20, an important negative regulator for Toll-like receptor- and NOD2-induced inflammatory responses, the over-expression of A20 by gene transfer did not reversed MDP-induced production of cytokines, suggested that A20 did not regulate the functions of NOD2 in THP-1 cells. Meanwhile, we found that TNF-α up-regulated NOD2 and its down-stream adaptor protein RIP2 at both mRNA and protein levels. MDP induced the activation of ERK, JNK, p38 and NF-κB, and TNF-α pre-treatment augmented this activation. The results from pharmacological inhibition assay showed that cytokine production was dependent on MAPK signaling. In addition, we found that the pre-treatment of THP-1 cells with MDP down-regulated the mRNA levels of cytokine induced by MDP re-treatment. MDP pre-treatment up-regulated NOD2, but down-regulated RIP2, and down-regulated NOD2 signal transduction induced by MDP re-stimulation. Taking together, these results suggested that TNF-α is a positive regulator for NOD2 functions via up-regulation of NOD2 and its signal adaptor RIP2, and TNF-α-induced A20 does not regulate MDP-induced inflammatory responses in THP-1 cells. J. Cell. Biochem. 119: 5072-5081, 2018. © 2017 Wiley Periodicals, Inc.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Tnf-a Pre-treatment Up-regulates Mdp-induced Production Of Cytokinesmentioning

confidence: 99%

TNF‐α‐Induced NOD2 and RIP2 Contribute to the Up‐Regulation of Cytokines Induced by MDP in Monocytic THP‐1 Cells

Chen

Xiao

Xie

et al. 2018

J of Cellular Biochemistry

View full text Add to dashboard Cite

show abstract

“…7 A20 was originally identified as a TNFα-inducible protein in human umbilical vein endothelial cells. 8 The physiological function of A20 is considered as a negative feedback regulation of NF-κB signaling. Activation of NF-κB signaling rapidly induces A20 expression, while A20 inhibits NF-κB signaling by deubiquitinating receptor-interacting protein 1 (RIP1), 9 receptor-interacting protein 2 (RIP2), 10 NF-kappa-B essential modulator (NEMO, also known as the inhibitor of nuclear factor kappa-B kinase subunit gamma; IKK-γ), 11 and TNF receptor-associated factor 6 (TRAF6).…”

Section: Introductionmentioning

confidence: 99%

Combined A20 and tripartite motif‐containing 44 as poor prognostic factors for breast cancer patients of the Japanese population

Sato

Azuma

Kinowaki

et al. 2020

Pathology International

View full text Add to dashboard Cite

We previously reported that a strong immunoreactivity of tripartite motif‐containing 44 (TRIM44) predicts the poor prognosis of patients with invasive breast cancer, and proposed that TRIM44 activates nuclear factor‐κB (NF‐κB) signaling as a causative mechanism. In the present study, we examined the clinicopathological roles of A20, which is known to be an NF‐κB responsive gene, with TRIM44, in an updated cohort. Tissue samples of invasive breast cancer were obtained from 140 Japanese female breast cancer patients who underwent surgical treatment. Immunoreactivities of A20 and TRIM44 were analyzed using specific antibodies for each protein. A positive A20 immunoreactivity was significantly associated with a shorter disease‐free survival (P = 0.043) and was positively correlated with TRIM44 immunoreactivity (P = 0.039). Combined use of the immunoreactivities for two proteins revealed that double‐positive status for both A20 and TRIM44 immunoreactivities was associated with a shorter disease‐free survival (P = 0.012) and was an independent factor for poor prognosis. These results indicate that a combined A20 and TRIM44 immunoreactivity predicted the prognosis of patients with invasive breast cancer. Moreover, the positive correlation between A20 and TRIM44 immunoreactivities suggested that the activation of NF‐κB signaling by TRIM44 could occur in clinical breast cancer tissues.

show abstract

“…1 | INTRODUCTION A20, also referred to as tumor necrosis factor alpha (TNFα)induced protein 3 (TNFAIP3), was first identified as a TNFα responsive gene in endothelial cells coding a novel type of zinc finger protein. 1,2 A20 is a dual ubiquitin-editing protein that exerts de-ubiquitinating (DUB) activity through the amino-terminal ovarian tumor (OTU) family domain, and E3 ligase activity through the carboxy-terminal zinc finger (ZF) domain. 3 A20 was shown to restrict the TNFαinduced activation of nuclear factor-κB (NF-κB) via deubiquitination and polyubiquitination of receptor interacting protein1 (RIP1).…”

mentioning

confidence: 99%

A20 restores phorbol ester‐induced differentiation of THP‐1 cells in the absence of nuclear factor‐κB activation

Osako

Itsumi

Yamaguchi

et al. 2017

J of Cellular Biochemistry

View full text Add to dashboard Cite

A20, also referred to as tumor necrosis factor alpha (TNFα)-induced protein 3 (TNFAIP3), is an ubiquitin-editing enzyme whose expression is enhanced by NF-κB activation, and plays an important role in silencing NF-κB activity. Another well-known role for A20 is to protect cells from TNFα-induced apoptosis. Depletion of NF-κB in differentiating U937 monocytic leukemia cells is known to cause apoptotic cell death; however, much remains to be explored about the molecules that are expressed in an NF-κB-dependent manner and which support monocyte-macrophage differentiation. Using the monocytic cell line THP-1, and peripheral blood monocytes, we show here a sustained increase in A20 expression during monocyte-macrophage differentiation, which coincided with high NF-κB-dependent transcriptional activity. Depletion of NF-κB by stable expression of a super-repressor form of IκBα in THP-1 cells caused remarkable cell death during phorbol 12-myristate 13-acetate (PMA)-induced differentiation. A20 expression in these cells did not alter this NF-κB suppression, but was sufficient to protect the cells and restore the cell surface expression of a differentiation marker (CD11b) and phagocytic activity. Mutational analyses revealed that this A20 activity requires the carboxy-terminal zinc-finger domain, but not its deubiquitinase activity. Based on these findings, we conclude that A20, when ectopically expressed, can support both survival and differentiation of THP-1 cells in the absence of sustained NF-κB activity.

show abstract

Tumor necrosis factor-alpha induction of novel gene products in human endothelial cells including a macrophage-specific chemotaxin.

Cited by 351 publications

References 35 publications

TNF‐α‐Induced NOD2 and RIP2 Contribute to the Up‐Regulation of Cytokines Induced by MDP in Monocytic THP‐1 Cells

TNF‐α‐Induced NOD2 and RIP2 Contribute to the Up‐Regulation of Cytokines Induced by MDP in Monocytic THP‐1 Cells

Combined A20 and tripartite motif‐containing 44 as poor prognostic factors for breast cancer patients of the Japanese population

A20 restores phorbol ester‐induced differentiation of THP‐1 cells in the absence of nuclear factor‐κB activation

Contact Info

Product

Resources

About