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IGFBP3 — SMAD2

Text-mined interactions from Literome

Leal et al., J Biol Chem 1999 : IGFBP-3 did not stimulate the cellular phosphorylation of Smad2 and Smad3, key transducers of the transforming growth factor-beta type I/type II receptor ( TbetaR-I.TbetaR-II ) heterocomplex mediated signaling
Fanayan et al., J Biol Chem 2000 (Breast Neoplasms) : Phosphorylation of each Smad was stimulated by TGF-beta1 and, independently, by IGFBP-3 with the two agents together showing a cumulative effect
Fanayan et al., J Biol Chem 2002 (Breast Neoplasms) : Like TGF-beta1, natural and recombinant IGFBP-3 stimulated the time- and dose dependent phosphorylation of TGF-betaR1 as well as Smad2 and Smad3
Kuemmerle et al., Am J Physiol Gastrointest Liver Physiol 2004 : The effects of IGFBP-3 on Smad2 phosphorylation and on smooth muscle cell proliferation were independent of TGF-beta1 and were abolished by transfection of Smad2 siRNA
Ismail et al., Am J Physiol Lung Cell Mol Physiol 2009 : Smad inhibition does not but the phosphatidylinositol 3-kinase (PI3K) signaling pathway inhibitor LY-294002 does inhibit NOX4 and IGFBP-3 gene expression, IGFBP-3 secretion, and cellular proliferation resulting from hypoxia
Zhong et al., J Cell Sci 2011 : Biochemical assays and in vitro experiments revealed that IGFBP3 bound BMP2 and inhibited BMP2 induced Smad signaling in cultured human cells
de Silva et al., Endocrinology 2012 : We conclude that IGFBP-3 activates inhibitory Smad signaling in 3T3-L1 cells and that endogenous IGFBP-3 modulates their adipogenic differentiation by regulating cell sensitivity towards the inhibitory effect of TGFß