scholarly journals Roles for interleukin-1β, phorbol ester and a post-transcriptional regulator in the control of bradykinin B1 receptor gene expression

1998 ◽  
Vol 330 (1) ◽  
pp. 361-366 ◽  
Author(s):  
Xiaofeng ZHOU ◽  
Peter POLGAR ◽  
Linda TAYLOR
Keyword(s):  
Gene Expression ◽  
Protein Synthesis ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Mrna Level ◽  
Mrna Degradation ◽  
Mrna Stabilization ◽  
B1 Receptor ◽  
Kinase C ◽  
Bradykinin B1 Receptor

Bradykinin B1 receptor (BKB1R) is involved in a variety of pathophysiological processes, particularly those related to inflammation. The gene for this receptor is known to be upregulated by interleukin (IL)-1β, a proinflammatory cytokine. However, the molecular mechanisms involved in the regulation of the BKB1R gene expression have not been defined. We demonstrated that IL-1β induces a rapid increase in BKB1R mRNA level and the binding of desArg10-kallidin in human embryo lung fibroblasts (IMR90). This increase in BKB1R mRNA level is protein synthesis-independent as indicated by treatment of cells with cycloheximide (CHX) or puromycin (PUR). By testing the IL-1β effect on BKB1R mRNA degradation, we showed that the IL-1β upregulation of BKB1R expression is achieved through both transcriptional activation and post-transcriptional mRNA stabilization. In addition to the IL-1β effects, translation inhibitors, CHX and PUR increase the steady state BKB1R mRNA level by inhibiting BKB1R mRNA degradation. Removal of the CHX block with subsequent resumption of protein synthesis results in a sizable increase of desArg10-kallidin binding. Using signalling pathway inhibitors, we show that IL-1β functions through a protein tyrosine kinase, not protein kinase C or protein kinase A. However, activation of protein kinase C by phorbol 12-myristate 13-acetate increases the level of BKB1R mRNA and the binding of desArg10-kallidin. This increase is blocked by NF-κB activation inhibitors.

scholarly journals Post-transcriptional regulation of H-ferritin gene expression in human monocytic THP-1 cells by protein kinase C

1996 ◽  
Vol 319 (1) ◽  
pp. 185-189 ◽  
Author(s):  
Jong-Hwei S. PANG ◽  
Chia-Jung WU ◽  
Lee-Young CHAU
Keyword(s):  
Gene Expression ◽  
Protein Synthesis ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Human Fibroblasts ◽  
Leukaemic Cell ◽  
Protein Synthesis Inhibitor ◽  
Kinase C ◽  
Ferritin Gene ◽  
The Stability

The mRNA coding for H-ferritin was highly induced in human monocytic THP-1 cells following treatment with phorbol 12-myristate 13-acetate (PMA). The induction was detected at 3 h, reached maximal levels at 12 h, and was sustained for up to 48 h subsequent to PMA exposure. PMA-induced up-regulation of H-ferritin gene expression was also observed in other leukaemic cell lines, HL60 and U937, but not in non-leukaemic cell types, including human fibroblasts, endothelial cells and smooth muscle cells. The effect of PMA could be completely blocked by the protein kinase C inhibitor, H-7. Furthermore, treatment of THP-1 cells with bacterial phospholipase C also produced a marked increase in expression of H-ferritin mRNA, suggesting the activation of protein kinase C was responsible for the accumulation of mRNA. Nuclear run-off experiments demonstrated that PMA did not increase the transcriptional rate of the H-ferritin gene. In contrast, the half-life of the H-ferritin mRNA measured in the presence of actinomycin D was greatly prolonged in PMA-treated cells. The induction of H-ferritin mRNA by PMA required no protein synthesis. Conversely, treatment of THP-1 cells with protein synthesis inhibitor, cycloheximide, resulted in a 4–5-fold increase in H-ferritin mRNA. The increase in the stability of the H-ferritin mRNA was also observed in cells treated with cycloheximide. Taken together, these results suggest that the stability of H-ferritin mRNA in THP-1 is subjected to regulation via a protein kinase C-mediated phosphorylation on existing putative protein factor(s).

scholarly journals Posttranscriptional regulation of GAP-43 gene expression in PC12 cells through protein kinase C-dependent stabilization of the mRNA.

1993 ◽  
Vol 120 (5) ◽  
pp. 1263-1270 ◽  
Author(s):  
N I Perrone-Bizzozero ◽  
V V Cansino ◽  
D T Kohn
Keyword(s):  
Gene Expression ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Pc12 Cells ◽  
Phorbol Ester ◽  
Phorbol Esters ◽  
Calcium Ionophore ◽  
Mrna Levels ◽  
Mrna Stabilization ◽  
Kinase C

We have previously shown that nerve growth factor (NGF) selectively stabilizes the GAP-43 mRNA in PC12 cells. To study the cellular mechanisms for this post-transcriptional control and to determine the contribution of mRNA stability to GAP-43 gene expression, we examined the effects of several agents that affect PC12 cell differentiation on the level of induction and rate of degradation of the GAP-43 mRNA. The NGF-mediated increase in GAP-43 mRNA levels and neurite outgrowth was mimicked by the phorbol ester TPA, but not by dibutyryl cAMP or the calcium ionophore A12783. Downregulation of protein kinase C (PKC) by high doses of phorbol esters or selective PKC inhibitors prevented the induction of this mRNA by NGF, suggesting that NGF and TPA act through a common PKC-dependent pathway. In mRNA decay studies, phorbol esters caused a selective 6-fold increase in the half-life of the GAP-43 mRNA, which accounts for most of the induction of this mRNA by TPA. The phorbol ester-induced stabilization of GAP-43 mRNA was blocked by the protein kinase inhibitor polymyxin B and was partially inhibited by dexamethasone, an agent that blocks GAP-43 expression and neuronal differentiation in PC12 cells. In contrast, the rates of degradation and the levels of the GAP-43 mRNA in control and TPA-treated cells were not affected by cycloheximide treatment. Thus, changes in GAP-43 mRNA turnover do not appear to require continuous protein synthesis. In conclusion, these data suggest that PKC activity regulates the levels of the GAP-43 mRNA in PC12 cells through a novel, translation-independent mRNA stabilization mechanism.

Bradykinin B1 receptor stimulates the proximal tubule Na+-ATPase activity through protein kinase C pathway

2003 ◽  
Vol 115 (3) ◽  
pp. 195-201 ◽  
Author(s):  
C Caruso-Neves ◽  
A.T Malaquias ◽  
F.F Lóss ◽  
V.M Corrêa da Costa ◽  
V.O Gomes ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Atpase Activity ◽  
Proximal Tubule ◽  
B1 Receptor ◽  
Kinase C ◽  
Bradykinin B1 Receptor

scholarly journals Intracellular Calcium Release and Protein Kinase C Activation Stimulate Sonic Hedgehog Gene Expression During Gastric Acid Secretion

2010 ◽  
Vol 139 (6) ◽  
pp. 2061-2071.e2 ◽  
Author(s):  
Mohamad El–Zaatari ◽  
Yana Zavros ◽  
Art Tessier ◽  
Meghna Waghray ◽  
Steve Lentz ◽  
...  
Keyword(s):  
Gene Expression ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Acid Secretion ◽  
Gastric Acid Secretion ◽  
Sonic Hedgehog ◽  
Calcium Release ◽  
Kinase C ◽  
Sonic Hedgehog Gene ◽  
Protein Kinase C Activation

Interleukin-1? induction of TNF-? gene expression: Involvement of protein kinase C

1992 ◽  
Vol 152 (2) ◽  
pp. 264-273 ◽  
Author(s):  
John R. Bethea ◽  
G. Yancey Gillespie ◽  
Etty N. Benveniste
Keyword(s):  
Gene Expression ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Interleukin 1 ◽  
Kinase C ◽  
Tnf Gene
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