scholarly journals Nitric oxide inhibition induces early activation of type I collagen gene in renal resistance vessels and glomeruli in transgenic mice. Role of endothelin.

1998 ◽  
Vol 101 (12) ◽  
pp. 2780-2789 ◽  
Author(s):  
C Chatziantoniou ◽  
J J Boffa ◽  
R Ardaillou ◽  
J C Dussaule
2015 ◽  
Vol 116 (3) ◽  
pp. 408-417 ◽  
Author(s):  
Georgia Schäfer ◽  
Jessica K. Hitchcock ◽  
Tamlyn M. Shaw ◽  
Arieh A. Katz ◽  
M. Iqbal Parker

Nitric Oxide ◽  
2009 ◽  
Vol 21 (3-4) ◽  
pp. 184-191 ◽  
Author(s):  
Guido Lazzerini ◽  
Serena Del Turco ◽  
Giuseppina Basta ◽  
Ana O’Loghlen ◽  
Antonella Zampolli ◽  
...  

2000 ◽  
Vol 56 (3) ◽  
pp. 181-188 ◽  
Author(s):  
M. Criado ◽  
O. Flores ◽  
Ma J. Vázquez ◽  
A. Esteller

2004 ◽  
Vol 89 (2) ◽  
pp. 155-162 ◽  
Author(s):  
Juan Sáinz ◽  
Antonio Osuna ◽  
Rosemary Wangensteen ◽  
Juan de Dios Luna ◽  
Isabel Rodríguez-Gómez ◽  
...  

1993 ◽  
Vol 121 (5) ◽  
pp. 1165-1172 ◽  
Author(s):  
B J Dzamba ◽  
H Wu ◽  
R Jaenisch ◽  
D M Peters

Mov13 fibroblasts, which do not express endogenous alpha 1(I) collagen chains due to a retroviral insertion, were used to study the role of type I collagen in the process of fibronectin fibrillogenesis. While Mov13 cells produced a sparse matrix containing short fibronectin fibrils, transfection with a wild type pro alpha 1(I) collagen gene resulted in the production of an extensive matrix containing fibronectin fibrils of normal length. To study the amino acids involved in the fibronectin-collagen interaction, mutations were introduced into the known fibronectin binding region of the pro alpha 1(I) collagen gene. Substitution of Gln and Ala at positions 774 and 777 of the alpha 1(I) chain for Pro resulted in the formation of short fibronectin fibrils similar to what was observed in untransfected Mov13 cells. Type I collagen carrying these substitutions bound weakly to fibronectin-sepharose and could be eluted off with 1 M urea. The effect of this mutation on fibronectin fibrillogenesis could be rescued by adding either type I collagen or a peptide fragment (CB.7) which contained the wild type fibronectin binding region of the alpha 1(I) chain to the cell culture. These results suggest that fibronectin fibrillogenesis in tissue culture is dependent on type I collagen synthesis, and define an important role for the fibronectin binding site in this process.


2007 ◽  
Vol 293 (1) ◽  
pp. G154-G164 ◽  
Author(s):  
Milan Dodig ◽  
Ben Ogunwale ◽  
Srinivasan Dasarathy ◽  
Min Li ◽  
Bingcheng Wang ◽  
...  

Hepatic stellate cells (HSC) differ in their phenotype depending on the initiation and progression of their activation. Our hypothesis was that different mechanisms govern type I collagen synthesis depending on stage of HSC activation. We investigated the role of α5β1-integrin as a regulator of type I collagen gene COL1A1 expression in primary and passaged HSC cultures using transgenic mouse containing type I collagen gene COL1A1 promoter linked to the chloramphenicol acetyltransferase (CAT) reporter gene. The α5β1 protein levels increased during the activation and were highest in day 6 primary cultures but decreased in passaged HSC. CAT activity, reflecting COL1A1 expression, was upregulated by α5β1-integrin. Inhibition of α5β1-integrin by echistatin and blocking antibody resulted in reduced transgene activity only in early primary cultures (compared with the control, 53.3 ± 12% echistatin and 58.8 ± 7% blocking antibody, respectively, P < 0.05). Treatment of passaged HSC with either echistatin or blocking antibody had no effect. Fibronectin, an α5β1-integrin ligand, increased transgene activity in primary (210 ± 33%, P < 0.05) but not in passaged HSC cultures (119 ± 8%). This α5β1-integrin effect appears to be at least in part mediated by CCAAT enhancer binding protein-β (C/EBPβ), because fibronectin increased and α5-gene silencing by small interfering RNA decreased C/EBPβ levels. In addition, C/EBPβ knockout mice showed reduced type I collagen synthesis compared with wild-type littermates. Therefore α5β1-integrin is an important regulator of type I collagen production in early primary HSC cultures but appears to have no direct role once the HSC are fully activated.


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