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Review
. 2001 Oct;159(4):1187-92.
doi: 10.1016/s0002-9440(10)62503-5.

Transforming growth factor-beta, basement membrane, and epithelial-mesenchymal transdifferentiation: implications for fibrosis in kidney disease

P J Stahl  1 , D Felsen
Affiliations
Review

Transforming growth factor-beta, basement membrane, and epithelial-mesenchymal transdifferentiation: implications for fibrosis in kidney disease

P J Stahl et al. Am J Pathol. 2001 Oct.
No abstract available

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Figures

Figure 1.
Figure 1.
Organization of the actin cytoskeleton in normal and transdifferentiated NmuMG cells. Cells were stimulated for 36 hours with vehicle (A) or 100 pmol/L TGF-β1 (B). Reprinted from J Cell Sci 1999, 112:4557–4568 with permission from Company of Biologists Ltd.
Figure 2.
Figure 2.
Schematic representation of collagen type IV chains and supramolecular networks. Type IV collagen comprises a family of six homologous chains. Each chain has a 7S domain at the amino terminus, a long collagenous domain (∼1400 residues), and a noncollagenous domain (NC1) of ∼230 residues at the carboxyl terminus (A). Three α chains assemble into a triple helical protomer, as exemplified by the (α1)2 α2 molecule. Protomers interact head-to-head, end-to-end, and by lateral associations, forming networks of distinct chain compositions. The α1/α2 network is common to all basement membranes (B) Reprinted from J Biol Chem 2000, 275:8051–8061, with permission from the American Society for Biochemistry and Molecular Biology.
Figure 3.
Figure 3.
EMT is a target of TGF-β. TGF-β induces EMT directly, and also participates in a proposed positive feedback loop via up-regulation of MMP-9 and disruption of basement membrane. In addition, it increases the synthesis of collagen I, which stabilizes the mesenchymal phenotype and increases MMP-9.
See this image and copyright information in PMC

Comment on

References

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