MAD proteins, originally defined in Drosophila, are essential components of the signaling pathways of the transforming growth factor-beta receptor family. Using a differential display approach in cultured endothelial cells subjected to multiple soluble and biomechanical stimuli, Topper et al. (1997) isolated a human endothelial cell cDNA encoding MADH7, which they called SMAD7.
The predicted 426-amino acid MADH7 protein lacks the C-terminal putative phosphorylation sites present in other MAD proteins, suggesting that it may be distinctly regulated. In situ hybridization and immunohistochemical analyses on human tissues showed that MADH7 is expressed predominantly in vascular endothelium.
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