A T-cell enhancer cooperates with NF-kappa B to yield cytokine induction of E-selectin gene transcription in endothelial cells.

Huijsduijnen, Rob Hooft van; Whelan, James P.; Pescini, R; Becker‐André, Michael; Schenk, Andrea; DeLamarter, J F

doi:10.1016/s0021-9258(18)41683-3

Cited by 56 publications

(13 citation statements)

References 26 publications

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“…The cytokine-driven expression of luciferase from these constructs were remarkably similar and, most significantly, were lower in terms of fold induction compared to that of the wild-type construct [i.e., the wild-type (construct 1) response to IL-1 and TNF-α was approximately 3.5 times greater than that of either construct 6 or 7 (Figure 1)]. This clearly demonstrates that the second AP-1/CREB site (AP1.2) is involved in transcriptional activation and confirms previous reports (4,5) indicating the involvement of this transcription factor binding site in cytokine-driven induction. The AP-1.2 site on its own, in the absence of any NF-κB sites, is unable to facilitate a cytokine response, as evidenced by the lack of enhanced transcription from construct 4.…”

Section: Acknowledgmentssupporting

confidence: 87%

ELAM-1/E-selectin promoter contains an inducible AP-1/CREB site and is not NF-κB-specific

Jensen

Whitehead

2003

BioTechniques

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Section: Acknowledgmentssupporting

confidence: 87%

ELAM-1/E-selectin promoter contains an inducible AP-1/CREB site and is not NF-κB-specific

Jensen

Whitehead

2003

BioTechniques

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“…The discrepancy between NF-v,_B activation and E-selectin expression may be explained by the involvement of other transcriptional regulator elements. Specifically, the regulation of E-selectin gene expression also depends on a cAMP-responsive element (CRE)-like binding site in the E-selectin promoter (22,26) that is located just upstream of three tandem KB-binding sites. By electrophoretic mobility shift assay, this CRE-like site binds at least three different nuclear factors in ECs, identified by antibody supershift as ATF-2 homodimers, ATF-2/c-Jun heterodimers, and CREB proteins (26)(27)(28).…”

mentioning

confidence: 99%

“…Specifically, the regulation of E-selectin gene expression also depends on a cAMP-responsive element (CRE)-like binding site in the E-selectin promoter (22,26) that is located just upstream of three tandem KB-binding sites. By electrophoretic mobility shift assay, this CRE-like site binds at least three different nuclear factors in ECs, identified by antibody supershift as ATF-2 homodimers, ATF-2/c-Jun heterodimers, and CREB proteins (26)(27)(28). ATF-2 appears essential for E-selectin expression, since E-selectin, but not VCAM-1 induction, is inhibited in ATF-2 knockout mice (29).…”

mentioning

confidence: 99%

Activation and homologous desensitization of human endothelial cells by CD40 ligand, tumor necrosis factor, and interleukin 1.

Karmann

Wang

Fanslow

et al. 1996

The Journal of Experimental Medicine

112

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SummaryWe have reported previously that activation of human umbilical vein endothelial cells (HUVECs) through CD40, using a recombinant soluble form oftrimerized CD40 ligand, leads to induction of E-selectin, vascular cell adhesion molecule-1 (VCAM-1), and intercellular adhesion molecule-1 (ICAM-1). Here, we compare the effects of CD40 ligand with those of tumor necrosis factor (TNF) and interleukin 1 (IL-1). All three ligands induce transient increases in E-selectin (peak 4 h) and VCAM-1 (peak 8-24 h), as well as sustained increases in ICAM-1 (plateau 24 h). Quantitatively, TNF is more potent than 1L-1, which is much more potent than CD40 ligand. The same hierarchy is observed for transcriptional activation of an E-selectin promoter reporter gene construct in transiently transfected HUVECs. TNF and CD40 ligand each induced activation of the transcription factors NF-KB, IRF-1, and ATF-2/c-Jun, measured by electrophoretic mobility shift assays, but this response appeared quantitatively similar. All three agents transiently (peak 30 rain) activatedJun NH2-terminal kinase (]NK), which has been implicated in transcription of E-selectin through its actions on ATF-2/c-Jun. Activation of JNK again showed a hierarchy of potency (TNF> IL-I>> CD40 ligand), although the time course of induction was similar for all three agents. After 44 h ofpretreatment, TNF, IL-1, and CD40 ligand each display homologous desensitization for reinduction of surface expression of E-selectin. A similar pattern of homologous desensitization for reactivation of JNK was observed. We conclude that TNF, IL-1, and CD40 ligand all activate similar responses in ECs, and that homologous desensitization of JNK may explain the inability of individual cytokines to reinduce E-selectin expression.

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“…Mutation of the binding sites for either of these factors results in an almost complete loss of IL-1 inducibility of the E-selectin promoter. While neither of these elements alone is sufficient to confer enhancer activity on a heterologous promoter, NF-ELAM1 was shown to cooperate with NF-KB to augment cytokine-induced expression to levels significantly above that observed with NF-KB alone (31). These results demonstrated that NF-ELAM1 functionally cooperates with NF-KB in IL-1 induction of the E-selectin gene.…”

mentioning

confidence: 85%

“…We have some evidence that DNA methylation plays a role in the tissue-specific expression of the E-selectin gene (51). On the other hand, we and others have defined several proximal promoter elements involved in control of cytokineinduced expression of the human E-selectin gene (12,31,42,56). One of these elements (-94 to -85) is a binding site for the ubiquitous transcription factor NF-KB, which is involved in control of cytokine-induced expression of many immuneand inflammatory-response genes (for reviews, see references 2 and 37).…”

mentioning

confidence: 95%

Cyclic AMP-Independent ATF Family Members Interact with NF-κB and Function in the Activation of the E-Selectin Promoter in Response to Cytokines

Kaszubska¹,

Huijsduijnen²,

Ghersa³

et al. 1993

Molecular and Cellular Biology

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We previously reported that NF-kappa B and a complex we referred to as NF-ELAM1 play a central role in cytokine-induced expression of the E-selectin gene. In this study we identify cyclic AMP (cAMP)-independent members of the ATF family binding specifically to the NF-ELAM1 promoter element. The NF-ELAM1 element (TGACATCA) differs by a single nucleotide substitution from the cAMP-responsive element consensus sequence. We demonstrate that this sequence operates in a cAMP-independent manner to induce transcription and thus define it as a non-cAMP-responsive element (NCRE). We show that ATFa is a component of the NF-ELAM1 complex and its overexpression activates the E-selectin promoter. In addition, ATFa, ATF2, and ATF3 interact directly with NF-kappa B in vitro, linking two unrelated families of transcription factors in a novel protein-protein interaction. Furthermore, we demonstrate that the ability of overexpressed NF-kappa B to transactivate the E-selectin promoter in vivo is dependent on the NF-ELAM1 complex. Our results suggest that a direct interaction between ATFs and NF-kappa B is, at least in part, the mechanism by which these factors specifically regulate E-selectin promoter activity.

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A T-cell enhancer cooperates with NF-kappa B to yield cytokine induction of E-selectin gene transcription in endothelial cells.

Cited by 56 publications

References 26 publications

ELAM-1/E-selectin promoter contains an inducible AP-1/CREB site and is not NF-κB-specific

ELAM-1/E-selectin promoter contains an inducible AP-1/CREB site and is not NF-κB-specific

Activation and homologous desensitization of human endothelial cells by CD40 ligand, tumor necrosis factor, and interleukin 1.

Cyclic AMP-Independent ATF Family Members Interact with NF-κB and Function in the Activation of the E-Selectin Promoter in Response to Cytokines

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