December 2002
Volume 43, Issue 13
Free
ARVO Annual Meeting Abstract  |   December 2002
A novel TGF-beta sigaling in EMT-related gene expression
C-K Joo
Author Affiliations & Notes
  • C-K Joo
    Ophthalmology & Visual Science Catholic University of Korea Seoul Republic of Korea
  • Footnotes
    Commercial Relationships   C. Joo, None. Grant Identification: Support: MOST Grant 00-J-LF-01-B-78
Investigative Ophthalmology & Visual Science December 2002, Vol.43, 2986. doi:
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      C-K Joo; A novel TGF-beta sigaling in EMT-related gene expression . Invest. Ophthalmol. Vis. Sci. 2002;43(13):2986.

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Abstract

Abstract: : Purpose: It has been reported that transdifferentiation such as epithelium-mesenchyme transition (EMT) is the multiple process in time-dependent regulation of various genes. To investigate an early event of EMT induced by TGF-beta, we focused on Crk-associated substrate (Cas), a adaptor protein localized at focal adhesions and stress fiber, which is known to have important functions in cell migration and the induction of immediate early gene expression. Methods: Analysis of Cas phosphorylation induced by TGF-beta was performed by immunoprecipitation using anti-Cas antibody and immunoblotting with anti-phosphotyrosine antibody. The activities of several kinases were analyzed by immunocomplex kinase assay using various substrates. In addition, to verify TGF-beta signal pathway, we also utilized other methods such as immunofluorescence staining, cell transfection, and the analysis for fibronectin promoter-responsive luciferase activity. Results: The tyrosine phosphorylation of Cas induced by TGF-beta is cell-type specific and related to src kinase signal pathway. Addition of TGF-beta to various epithelial cell lines, including human lens, kidney, breast, and skin, rapidly induced tyrosine phosphorylation of Cas and association between Cas and Crk. TGF-beta also stimulated the activity of Src kinase family and Src kinase specific inhibitors completely blocked the tyrosine phosphorylation of Cas by TGF-beta. Tyrosine phosphorylation of Cas was induced in an epithelial cell type specific manner. In addition, stable transfection of E-cadherin to L cells and E-cadherin blocking assay revealed that E-cadherin-mediated cell-cell interaction was required to Cas phosphorylation by TGF-beta. Especially, we found that TGF-beta-responsive fibronectin gene expression was subject to this Src-Cas mediated signaling pathway. Conclusion: Our data suggest that rapid Cas phosphorylation and Src kinase activation induced by TGF-beta may play a novel role in EMT-related gene expression.

Keywords: 339 cell adhesions/cell junctions • 383 cytoskeleton • 580 signal transduction 
© 2002, The Association for Research in Vision and Ophthalmology, Inc., all rights reserved. Permission to republish any abstract or part of an abstract in any form must be obtained in writing from the ARVO Office prior to publication.
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