May 2003
Volume 44, Issue 13
ARVO Annual Meeting Abstract  |   May 2003
Alpha-crystallins Interact with Bax and Bcl-xs to Prevent Staurosporine-induced Apoptosis
Author Affiliations & Notes
  • Y. Mao
    Molecular Biology, UMDNJ-SOM, Stratford, NJ, United States
  • H. Xiang
    Molecular Biology, UMDNJ-SOM, Stratford, NJ, United States
  • D.W. Li
    The Hormel Institute, University of Minnesota, Austin, MN, United States
  • Footnotes
    Commercial Relationships  Y. Mao, None; H. Xiang, None; D.W. Li, None.
  • Footnotes
    Support  EY11372
Investigative Ophthalmology & Visual Science May 2003, Vol.44, 1232. doi:
  • Views
  • Share
  • Tools
    • Alerts
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation

      Y. Mao, H. Xiang, D.W. Li; Alpha-crystallins Interact with Bax and Bcl-xs to Prevent Staurosporine-induced Apoptosis . Invest. Ophthalmol. Vis. Sci. 2003;44(13):1232.

      Download citation file:

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

  • Supplements

Abstract: : Purpose: Alpha-Crystallins, members of the small heat shock protein family, are distinct antiapoptotic regulators. Regarding the antiapoptotic mechanisms, we have previously demonstrated that alphaB-crystallin prevent stress-induced apoptosis through interactions with procaspase-3 and partially processed procapspase-3 to repress caspase-3 activation and also through negative regulation of MAP kinases. Here, we demonstrate that human alphaA- and alphaB-crystallins prevent staurosporine-induced apoptosis through regulation of Bcl-2 family members. Methods: Human alphaA- and alphaB-crystallins, and the related vector-transfected stable expression clones were established with human lens epithelial cells under G418 screening. Expression of human alphaA- and alphaB-crystallins was determined with Western blot and fluorescence microscopy. The interaction between alpha-crystallins and members of the Bcl-2 family were explored with in vitro GST pulldown assays and in vivo co-immunoprecipitation. Results: Both alpha-crystallins from human lenses bind directly to Bax and Bcl-XS. This binding prevents their translocation from cytosol to mitochondria after staurosporine treatment. alpha-crystallins also block staurosporine-stimulated upregulation of Bak, which is largely accumulated in mitochondria. Consequently, alpha-crystallins block the release of cytochrome C, repress activation of caspase-3 and prevent degradation of PARP. Conclusions:Our results demonstrate that alpha-crystallins prevent staurosporine-induced apoptosis through interactions with members of Bcl-2 family, thus providing another novel antiapoptotic mechanism for alpha-crystallins. Supported by EY 11372 and the Hormel Foundation. None.

Keywords: crystallins • apoptosis/cell death • cell death/apoptosis 

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.