Abstract:
:Transforming growth factor (TGF)-beta1 can cause fibrosis diseases by enhancing production of collagen. However, the intracellular signaling mechanism for TGF-beta1 stimulation of this process has not been fully elucidated. The present study focused on this mechanism and the cross-talk between the MAPK and Smad pathways. Extracellular signal-regulated kinase (ERK)2 ablation by a small interfering RNA led to marked inhibition of TGF-beta1-induced collagen synthesis and enhanced phosphorylation of the Smad2 linker site in NIH/3T3 fibroblast cells. However, ERK1 ablation had minimal effects. Ablation of either ERK2 or ERK1 had no effect on the phosphorylation of the Smad2 C-terminal site. Furthermore, a Smad2 mutant with reduced phosphorylation of the Smad2 linker site inhibited TGF-beta1-induced collagen synthesis. These results indicate that ERK2, rather than ERK1, plays a predominantly positive role in TGF-beta1-induced collagen synthesis, and that ERK2 enhances collagen synthesis, at least partially, through activation of the Smad2 linker site.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Li F,Zeng B,Chai Y,Cai P,Fan C,Cheng Tdoi
10.1016/j.bbrc.2009.05.084subject
Has Abstractpub_date
2009-08-21 00:00:00pages
289-93issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(09)01049-3journal_volume
386pub_type
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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