scholarly journals Transcriptional regulation through cytokine and glucocorticoid response elements of rat acute phase plasma protein genes by C/EBP and JunB.

1991 ◽  
Vol 266 (30) ◽  
pp. 20390-20399
Author(s):  
H. Baumann ◽  
G.P. Jahreis ◽  
K.K. Morella ◽  
K.A. Won ◽  
S.C. Pruitt ◽  
...  
Keyword(s):  
Transcriptional Regulation ◽  
Acute Phase ◽  
Plasma Protein ◽  
Response Elements ◽  
Glucocorticoid Response ◽  
Glucocorticoid Response Elements

scholarly journals The permissive role of glucocorticoids on interleukin-1 stimulation of angiotensinogen gene transcription is mediated by an interaction between inducible enhancers.

1990 ◽  
Vol 10 (8) ◽  
pp. 4389-4395 ◽  
Author(s):  
D Ron ◽  
A R Brasier ◽  
K A Wright ◽  
J F Habener
Keyword(s):  
Acute Phase ◽  
Acute Phase Response ◽  
Interleukin 1 ◽  
Luciferase Reporter ◽  
Nf Kappa B ◽  
Response Elements ◽  
Glucocorticoid Response ◽  
Glucocorticoid Response Elements ◽  
Permissive Role

The acute-phase activation of the rat angiotensinogen (rAT) gene in liver cells is a transcriptional event mediated through an interleukin-1-inducible, NF kappa B-binding, cis-acting element (the acute-phase response element [APRE]). Using a cell culture model for the acute-phase response, we showed that the increase in angiotensionogen mRNA in H35 rat hepatoma cells requires costimulation with glucocorticoids and cytokines. Stably transfected rAT promoter-luciferase reporter genes were also activated by cytokines only in the presence of glucocorticoids. This permissive role of glucocorticoids is dependent on the expression of functional glucocorticoid receptors, because in HepG2 cells naturally deficient in such receptors, rAT gene-luciferase reporter constructs responded to interleukin-1 only when cotransfected with an expression vector for the glucocorticoid receptor. Point mutations in the two rAT gene glucocorticoid response elements located adjacent to the APRE led to loss of interleukin-1 inducibility. Induction of luciferase activity in transfected cells occurred even in the presence of cycloheximide, demonstrating that this synergistic response did not depend on new protein synthesis. Thus, a direct interaction between the interleukin-1-inducible NF kappa B-binding APRE and glucocorticoid response elements, located in cis, underlies the acute-phase activation of the rAT gene.

The permissive role of glucocorticoids on interleukin-1 stimulation of angiotensinogen gene transcription is mediated by an interaction between inducible enhancers

1990 ◽  
Vol 10 (8) ◽  
pp. 4389-4395
Author(s):  
D Ron ◽  
A R Brasier ◽  
K A Wright ◽  
J F Habener
Keyword(s):  
Acute Phase ◽  
Acute Phase Response ◽  
Interleukin 1 ◽  
Luciferase Reporter ◽  
Nf Kappa B ◽  
Response Elements ◽  
Glucocorticoid Response ◽  
Glucocorticoid Response Elements ◽  
Permissive Role

The acute-phase activation of the rat angiotensinogen (rAT) gene in liver cells is a transcriptional event mediated through an interleukin-1-inducible, NF kappa B-binding, cis-acting element (the acute-phase response element [APRE]). Using a cell culture model for the acute-phase response, we showed that the increase in angiotensionogen mRNA in H35 rat hepatoma cells requires costimulation with glucocorticoids and cytokines. Stably transfected rAT promoter-luciferase reporter genes were also activated by cytokines only in the presence of glucocorticoids. This permissive role of glucocorticoids is dependent on the expression of functional glucocorticoid receptors, because in HepG2 cells naturally deficient in such receptors, rAT gene-luciferase reporter constructs responded to interleukin-1 only when cotransfected with an expression vector for the glucocorticoid receptor. Point mutations in the two rAT gene glucocorticoid response elements located adjacent to the APRE led to loss of interleukin-1 inducibility. Induction of luciferase activity in transfected cells occurred even in the presence of cycloheximide, demonstrating that this synergistic response did not depend on new protein synthesis. Thus, a direct interaction between the interleukin-1-inducible NF kappa B-binding APRE and glucocorticoid response elements, located in cis, underlies the acute-phase activation of the rAT gene.

scholarly journals Acute-phase response factor, a nuclear factor binding to acute-phase response elements, is rapidly activated by interleukin-6 at the posttranslational level

1993 ◽  
Vol 13 (1) ◽  
pp. 276-288
Author(s):  
U M Wegenka ◽  
J Buschmann ◽  
C Lütticken ◽  
P C Heinrich ◽  
F Horn
Keyword(s):  
Transcriptional Regulation ◽  
Acute Phase ◽  
Interleukin 6 ◽  
Acute Phase Response ◽  
Acute Phase Protein ◽  
Phase Response ◽  
Response Factor ◽  
Nuclear Factor ◽  
Response Elements ◽  
Phase Protein

Interleukin-6 (IL-6) is known to be a major mediator of the acute-phase response in liver. We show here that IL-6 triggers the rapid activation of a nuclear factor, termed acute-phase response factor (APRF), both in rat liver in vivo and in human hepatoma (HepG2) cells in vitro. APRF bound to IL-6 response elements in the 5'-flanking regions of various acute-phase protein genes (e.g., the alpha 2-macroglobulin, fibrinogen, and alpha 1-acid glycoprotein genes). These elements contain a characteristic hexanucleotide motif, CTGGGA, known to be required for the IL-6 responsiveness of these genes. Analysis of the binding specificity of APRF revealed that it is different from NF-IL6 and NF-kappa B, transcription factors known to be regulated by cytokines and involved in the transcriptional regulation of acute-phase protein genes. In HepG2 cells, activation of APRF was observed within minutes after stimulation with IL-6 or leukemia-inhibitory factor and did not require ongoing protein synthesis. Therefore, a preexisting inactive form of APRF is activated by a posttranslational mechanism. We present evidence that this activation occurs in the cytoplasm and that a phosphorylation is involved. These results lead to the conclusions that APRF is an immediate target of the IL-6 signalling cascade and is likely to play a central role in the transcriptional regulation of many IL-6-induced genes.

scholarly journals The Glucose-6-Phosphatase Catalytic Subunit Gene Promoter Contains Both Positive and Negative Glucocorticoid Response Elements

2005 ◽  
Vol 19 (12) ◽  
pp. 3001-3022 ◽  
Author(s):  
Beth T. Vander Kooi ◽  
Hiroshi Onuma ◽  
James K. Oeser ◽  
Christina A. Svitek ◽  
Shelley R. Allen ◽  
...  
Keyword(s):  
Gene Promoter ◽  
Catalytic Subunit ◽  
Subunit Gene ◽  
Response Elements ◽  
Glucocorticoid Response ◽  
Glucocorticoid Response Elements

scholarly journals Acute-phase response factor, a nuclear factor binding to acute-phase response elements, is rapidly activated by interleukin-6 at the posttranslational level.

1993 ◽  
Vol 13 (1) ◽  
pp. 276-288 ◽  
Author(s):  
U M Wegenka ◽  
J Buschmann ◽  
C Lütticken ◽  
P C Heinrich ◽  
F Horn
Keyword(s):  
Transcriptional Regulation ◽  
Acute Phase ◽  
Interleukin 6 ◽  
Acute Phase Response ◽  
Acute Phase Protein ◽  
Phase Response ◽  
Response Factor ◽  
Nuclear Factor ◽  
Response Elements ◽  
Phase Protein

Interleukin-6 (IL-6) is known to be a major mediator of the acute-phase response in liver. We show here that IL-6 triggers the rapid activation of a nuclear factor, termed acute-phase response factor (APRF), both in rat liver in vivo and in human hepatoma (HepG2) cells in vitro. APRF bound to IL-6 response elements in the 5'-flanking regions of various acute-phase protein genes (e.g., the alpha 2-macroglobulin, fibrinogen, and alpha 1-acid glycoprotein genes). These elements contain a characteristic hexanucleotide motif, CTGGGA, known to be required for the IL-6 responsiveness of these genes. Analysis of the binding specificity of APRF revealed that it is different from NF-IL6 and NF-kappa B, transcription factors known to be regulated by cytokines and involved in the transcriptional regulation of acute-phase protein genes. In HepG2 cells, activation of APRF was observed within minutes after stimulation with IL-6 or leukemia-inhibitory factor and did not require ongoing protein synthesis. Therefore, a preexisting inactive form of APRF is activated by a posttranslational mechanism. We present evidence that this activation occurs in the cytoplasm and that a phosphorylation is involved. These results lead to the conclusions that APRF is an immediate target of the IL-6 signalling cascade and is likely to play a central role in the transcriptional regulation of many IL-6-induced genes.

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