December 2002
Volume 43, Issue 13
Free
ARVO Annual Meeting Abstract  |   December 2002
A mutant SV40 Large T Antigen (E107K) that Does Not Bind Rb Dramatically Inhibits Lens Fiber Cell Differentiation
Author Affiliations & Notes
  • Q Chen
    Molec & Cell Biology Baylor College Medicine Houston TX
  • D Liang
    Department of Molecular and Cellular Biology Baylor College of Medicine Houston TX
  • L Fromm
    Skirball Institute New York University Medical School New York NY
  • PA Overbeek
    Department of Molecular and Cellular Biology Baylor College of Medicine Houston TX
  • Footnotes
    Commercial Relationships   Q. Chen, None; D. Liang, None; L. Fromm, None; P.A. Overbeek, None. Grant Identification: Support: NIH Grant EY10448, Knight Templar Eye FDN
Investigative Ophthalmology & Visual Science December 2002, Vol.43, 2331. doi:
  • Views
  • Share
  • Tools
    • Alerts
      ×
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation

      Q Chen, D Liang, L Fromm, PA Overbeek; A mutant SV40 Large T Antigen (E107K) that Does Not Bind Rb Dramatically Inhibits Lens Fiber Cell Differentiation . Invest. Ophthalmol. Vis. Sci. 2002;43(13):2331.

      Download citation file:


      © ARVO (1962-2015); The Authors (2016-present)

      ×
  • Supplements
Abstract

Abstract: : Purpose: Full-length SV40 large T antigen binds to the retinoblastoma protein and causes cellular transformation when expressed in lens fiber cells. In order to determine whether transformation involves inhibition of other factors in addition to Rb, we expressed a mutant version of SV40 large T antigen (E107K) that does not bind Rb in lenses of transgenic mice. Methods: E107K was linked to the αA-crystallin promoter in the CPV2 vector. Transgenic mice were characterized by histology, immunohistochemistry, in situ hybridization and western blotting assays. A cell culture system was used for crystallin reporter assays as well as immunoprecipitations to assay for interactions among E107K, full-length T antigen, CBP/p300 and c-maf. Results: At embryonic day 15.5 (E15.5), the E107K transgene was expressed in lens fiber cells and also, unexpectedly, in lens epithelial cells. Lens histology revealed small hollow lenses in the transgenic eyes due to the inhibition of fiber cell elongation. The fiber cells did not incorporate BrdU, supporting the prediction that E107K does not bind pRb. TUNEL assays showed no evidence for apoptosis in the fiber cells. In situ hybridization and immunohistochemistry assays showed that the expression of fiber cell differentiation markers (ß-, γ-crystallin, CP49 and MIP26) was significantly reduced. Western blotting showed that there were almost no ß- and γ-crystallin proteins in E107K transgenic lenses, while c-maf and CBP/p300 proteins were still synthesized. Cell culture studies revealed that full-length T antigen modestly inhibits c-maf plus CBP/p300 coactivation, while E107K almost completely blocks coactivation of the γF crystallin promoter. E107K does not block CBP/p300 nuclear localization. In addition, immunoprecipitations indicated that E107K binds to CBP/p300 much like full-length T antigen. However, E107K can completely block the binding of c-maf to CBP/p300. Conclusion: A point mutant of SV40 large T antigen that no longer binds to pRb has lost its transforming ability, but is nonetheless a potent repressor of fiber cell differentiation. E107K interferes with CBP/p300 coactivation, crystallins and other differentiation markers. Our data further demonstrate that CBP/p300 coactivation is critical during lens development.

Keywords: 378 crystallins • 605 transcription factors • 417 gene/expression 
×
×

This PDF is available to Subscribers Only

Sign in or purchase a subscription to access this content. ×

You must be signed into an individual account to use this feature.

×