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Published online
doi:10.1083/jcb.200611044
The Journal of Cell Biology, Vol. 176, No. 6, 787-793
The Rockefeller University Press, 0021-9525 $30.00
© Yang et al.
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Absence of integrin-mediated TGFß1 activation in vivo recapitulates the phenotype of TGFß1-null mice



Zhiwei Yang, Zhenyu Mu, Branka Dabovic, Vladimir Jurukovski, Dawen Yu, Joanne Sung, Xiaozhong Xiong, and John S. Munger

Department of Cell Biology, New York University School of Medicine, New York, NY 10016

Correspondence to John S. Munger: john.munger{at}med.nyu.edu

The multifunctional cytokine transforming growth factor (TGF) ß1 is secreted in a latent complex with its processed propeptide (latency-associated peptide [LAP]). TGFß1 must be functionally released from this complex before it can engage TGFß receptors. One mechanism of latent TGFß1 activation involves interaction of the integrins {alpha}vß6 and {alpha}vß8 with an RGD sequence in LAP; other putative latent TGFß1 activators include thrombospondin-1, oxidants, and various proteases. To assess the contribution of RGD-binding integrins to TGFß1 activation in vivo, we created a mutation in Tgfb1 encoding a nonfunctional variant of the RGD sequence (RGE). Mice with this mutation (Tgfb1RGE/RGE) display the major features of Tgfb1–/– mice (vasculogenesis defects, multiorgan inflammation, and lack of Langerhans cells) despite production of normal levels of latent TGFß1. These findings indicate that RGD-binding integrins are requisite latent TGFß1 activators during development and in the immune system.

Abbreviations used in this paper: E, embryonic day; ES, embryonic stem; LAP, latency-associated peptide; LC, Langerhans cell; LTBP, latent TGFß-binding protein; MMP, matrix metalloproteinase; TSP1, thrombospondin-1.


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