IndraLab

"Smad7 is an inhibitor of TGF-beta signaling by preventing Smad3 and/or Smad2 phosphorylation and recruitment of Smad2 and Smad3 complex (XREF_FIG)."

"Both subunits of the receptor were equally expressed in the two cell types, overexpression of these receptor subunits did not modify the activation of PAI-1 SBE in myofibroblasts and, more important[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

"U87MG cells were treated with miR-132 mimic, miR-132 inhibitor or corresponding controls, and western blotting was performed to detect the protein level of phosphorylated SMAD2 and phosphorylated SMAD[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

"XREF_BIBR, XREF_BIBR, XREF_BIBR, XREF_BIBR In renal fibroblasts relaxin prevents TGF- beta induced collagen synthesis by suppression of SMAD2 phosphorylation and complex formation of SMAD3."

"The protein levels of alpha-smooth muscle actin (alpha-SMA), type 1 collagen (Col1), Smad2, Smad3, phosphorylated Smad2 (p-smad2), p-smad3 and Smad7 were assessed by Western blot analysis."

"Following cytokine stimulation, cells were fixed and stained for flow cytometric detection of SMAD2 protein phosphorylated at Ser465/467 sites and the SMAD3 protein phosphorylated at Ser423/425 sites according to the manufacturer’s protocols (catalog # 562586, BD Biosciences) ."

"We found that disruption of Smad2 induced smad3 phosphorylation and activity in cisplatin-treated TECs."

"As indicated in xref and ( xref ), TGF-β1 treatment induced an increase in phosphorylated Smad2 and phosphorylated Smad3 (p-Smad3)."

"Furthermore, both SMAD2 and SMAD3 are activated by phosphorylation, and our results support that patients whose TAFs exhibit a low (<1) pSMAD3/pSMAD2 ratio may be refractory to nintedanib and possibly to other antifibrotic drugs, whereas those with high (>1) pSMAD3/pSMAD2 ratio may elicit positive responses (where pSMAD2 and pSMAD3 refers to phosphorylated SMAD2 and SMAD3, respectively) (Figure 3D)."

"Another interesting and novel observation of this study was the mutual amplification of effects such that knockdown of Smad2 or inhibition of Rac1 (without direct modulation of Smad3) enhanced growth inhibition, Smad3 specific transcriptional activity, and C-terminal phosphorylation of Smad3, while knockdown of Smad3 (without direct modulation of Smad2) enhanced both Smad2 specific responses such as cellular migration (this study) and Smad2 phosphorylation by TGF-beta [XREF_BIBR]."

"Western analysis to detect phospho-Smad2/3 revealed that while treatment with RA did not induce C-terminal phosphorylation of either Smad, treatment with TGFβ in the presence or absence of RA resulted in robust phosphorylation of the Smad3 S423 and S425 residues (Figure 2E). These results suggest that the effects of RA on TGFβ-mediated signaling are not due to changes in Smad3 phosphorylation status. However, in cells treated with both TGFβ and RA, we did detect a significant decrease in Smad2 phosphorylation of the equivalent residues without changes in Smad2 levels (Figure 2E), suggesting that RA may interfere with the actions of TGFβ by reducing Smad2 activation by phosphorylation."