Oncostatin M Is a Potent Stimulator of α1-Antitrypsin Secretion in Lung Epithelial Cells: Modulation by Transforming Growth Factor- β and Interferon- γ

1998 ◽  
Vol 18 (4) ◽  
pp. 511-520 ◽  
Author(s):  
Anne Boutten ◽  
Philippe Venembre ◽  
Nathalie Seta ◽  
Jocelyne Hamelin ◽  
Michel Aubier ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epithelial Cells ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Interferon Γ ◽  
Lung Epithelial Cells ◽  
Oncostatin M ◽  
Potent Stimulator ◽  
Lung Epithelial

scholarly journals miR-1343 attenuates pathways of fibrosis by targeting the TGF-β receptors

2016 ◽  
Vol 473 (3) ◽  
pp. 245-256 ◽  
Author(s):  
Lindsay R. Stolzenburg ◽  
Sarah Wachtel ◽  
Hong Dang ◽  
Ann Harris
Keyword(s):  
Growth Factor ◽  
Epithelial Cells ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Lung Epithelial Cells ◽  
Lung Epithelial

A previously uncharacterized miRNA, miR-1343, was found to target and reduce the expression of transforming growth factor β (TGF-β) receptors 1 and 2. This led to significantly repressed TGF-β signalling in lung epithelial cells and fibroblasts and corresponding reductions in experimental markers of fibrosis.

scholarly journals Dermatopontin interacts with transforming growth factor β and enhances its biological activity

1999 ◽  
Vol 337 (3) ◽  
pp. 537-541 ◽  
Author(s):  
Osamu OKAMOTO ◽  
Sakuhei FUJIWARA ◽  
Mayumi ABE ◽  
Yasufumi SATO
Keyword(s):  
Extracellular Matrix ◽  
Biological Activity ◽  
Growth Factor ◽  
Epithelial Cells ◽  
Inhibitory Activity ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Lung Epithelial Cells ◽  
Lung Epithelial ◽  
Tgf Β1

Dermatopontin, a recently found low-molecular-mass component of the extracellular matrix, was studied for its interaction with decorin and transforming growth factor β (TGF-β) and its influence on TGF-β bioactivity. Dermatopontin reacted with decorin with an apparent Kd of 100 nM in a solid-phase assay. Dermatopontin inhibited the formation of the decorin–TGF-β1 complex. Decorin also competed with dermatopontin for the binding of this cytokine. The dermatopontin–decorin complex bound 3-fold more TGF-β1 than did each component individually, and binding was inhibited more strongly by decorin preincubated with dermatopontin than by dermatopontin or decorin alone. Dermatopontin augmented the biological activity of TGF-β1, as analysed by the expression of luciferase in mink lung epithelial cells transfected with a plasminogen activator inhibitor–promoter–luciferase construct, although dermatopontin itself did not show apparent induction of luciferase. Dermatopontin showed weak inhibitory activity on the proliferation of mink lung epithelial cells, and it enhanced the growth-inhibitory activity of TGF-β on these cells. Thus dermatopontin increases the cellular response to TGF-β. These findings strongly suggest that dermatopontin modifies the behaviour of TGF-β through interaction with decorin in the microenvironment of the extracellular matrix in vivo.

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