Stabilization of RNA Strands in Protein Synthesis by Type I Procollagen C-Proteinase Enhancer Protein, a Potential RNA-Binding Protein, in Hepatic Stellate Cells

2002 ◽  
Vol 290 (3) ◽  
pp. 898-902 ◽  
Author(s):  
Atsushi Matsui ◽  
Mikio Yanase ◽  
Tomoaki Tomiya ◽  
Hitoshi Ikeda ◽  
Kenji Fujiwara ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Hepatic Stellate Cells ◽  
Rna Binding ◽  
Binding Protein ◽  
Protein A ◽  
Rna Binding Protein ◽  
Stellate Cells ◽  
Type I ◽  
Type I Procollagen

scholarly journals Activation of ferritinophagy is required for the RNA-binding protein ELAVL1/HuR to regulate ferroptosis in hepatic stellate cells

Autophagy ◽  
2018 ◽  
Vol 14 (12) ◽  
pp. 2083-2103 ◽  
Author(s):  
Zili Zhang ◽  
Zhen Yao ◽  
Ling Wang ◽  
Hai Ding ◽  
Jiangjuan Shao ◽  
...  
Keyword(s):  
Hepatic Stellate Cells ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Stellate Cells

scholarly journals RNA-binding protein ZFP36/TTP protects against ferroptosis by regulating autophagy signaling pathway in hepatic stellate cells

Autophagy ◽  
2019 ◽  
Vol 16 (8) ◽  
pp. 1482-1505 ◽  
Author(s):  
Zili Zhang ◽  
Mei Guo ◽  
Yujia Li ◽  
Min Shen ◽  
Desong Kong ◽  
...  
Keyword(s):  
Signaling Pathway ◽  
Hepatic Stellate Cells ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Stellate Cells

scholarly journals The RNA-binding protein HuR/ELAVL1 regulates IFN-β mRNA abundance and the type I IFN response

2015 ◽  
Vol 45 (5) ◽  
pp. 1500-1511 ◽  
Author(s):  
Barbara Herdy ◽  
Thomas Karonitsch ◽  
Gregory I. Vladimer ◽  
Chris S.H. Tan ◽  
Alexey Stukalov ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Mrna Abundance ◽  
Type I ◽  
Type I Ifn

scholarly journals The RNA binding protein La/SS-B promotes RIG-I-mediated type I and type III IFN responses following Sendai viral infection

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Rebecca Mahony ◽  
Lindsay Broadbent ◽  
Jacen S. Maier-Moore ◽  
Ultan F. Power ◽  
Caroline A. Jefferies
Keyword(s):  
Viral Infection ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Type I ◽  
Type Iii ◽  
Type Iii Ifn

TGF-β1 modulates matrix metalloproteinase-13 expression in hepatic stellate cells by complex mechanisms involving p38MAPK, PI3-kinase, AKT, and p70S6k

2004 ◽  
Vol 287 (5) ◽  
pp. G974-G987 ◽  
Author(s):  
Carmen G. Lechuga ◽  
Zamira H. Hernández-Nazara ◽  
José-Alfredo Domínguez Rosales ◽  
Elena R. Morris ◽  
Ana Rosa Rincón ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Hepatic Stellate Cells ◽  
Type I Collagen ◽  
De Novo ◽  
Stellate Cells ◽  
Type I ◽  
Collagen Mrna ◽  
Matrix Metalloproteinase 13 ◽  
De Novo Protein Synthesis ◽  
Tgf Β1

Transforming growth factor-β1 (TGF-β1), the main cytokine involved in liver fibrogenesis, induces expression of the type I collagen genes in hepatic stellate cells by a transcriptional mechanism, which is hydrogen peroxide and de novo protein synthesis dependent. Our recent studies have revealed that expression of type I collagen and matrix metalloproteinase-13 (MMP-13) mRNAs in hepatic stellate cells is reciprocally modulated. Because TGF-β1 induces a transient elevation of α1(I) collagen mRNA, we investigated whether this cytokine was able to induce the expression of MMP-13 mRNA during the downfall of the α1(I) collagen mRNA. In the present study, we report that TGF-β1 induces a rapid decline in steady-state levels of MMP-13 mRNA at the time that it induces the expression of α1(I) collagen mRNA. This change in MMP-13 mRNA expression occurs within the first 6 h postcytokine administration and is accompanied by a twofold increase in gene transcription and a fivefold decrease in mRNA half-life. This is followed by increased expression of MMP-13 mRNA, which reaches maximal values by 48 h. Our results also show that this TGF-β1-mediated effect is de novo protein synthesis-dependent and requires the activity of p38MAPK, phosphatidylinositol 3-kinase, AKT, and p70S6k. Altogether, our data suggest that regulation of MMP-13 by TGF-β1 is a complex process involving transcriptional and posttranscriptional mechanisms.

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