May 2003
Volume 44, Issue 13
Free
ARVO Annual Meeting Abstract  |   May 2003
Protein Phosphatase-1 Acts as an Important Antiapoptotic Regulator in Lens Epithelial Cells
D.W. Li; Y. Mao; J. Wang; P.C. Schmid; J. Liu
Author Affiliations & Notes
  • D.W. Li
    The Hormel Institute, University of Minnesota, Austin, MN, United States
  • Y. Mao
    Molecular Biology, University of Medicine and Dentistry of New Jersey, Stratford, NJ, United States
  • J. Wang
    Molecular Biology, University of Medicine and Dentistry of New Jersey, Stratford, NJ, United States
  • P.C. Schmid
    Molecular Biology, University of Medicine and Dentistry of New Jersey, Stratford, NJ, United States
  • J. Liu
    Molecular Biology, University of Medicine and Dentistry of New Jersey, Stratford, NJ, United States
  • Footnotes
    Commercial Relationships  D.W. Li, None; Y. Mao, None; J. Wang, None; P.C. Schmid, None; J. Liu, None.
  • Footnotes
    Support  EY11372
Investigative Ophthalmology & Visual Science May 2003, Vol.44, 3139. doi:
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      D.W. Li, Y. Mao, J. Wang, P.C. Schmid, J. Liu; Protein Phosphatase-1 Acts as an Important Antiapoptotic Regulator in Lens Epithelial Cells . Invest. Ophthalmol. Vis. Sci. 2003;44(13):3139.

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Abstract

Abstract: : Purpose: Our previous studies have revealed that protein phosphatase-1 is important for survival of lens epithelial cells. With differential sensitivity of PP-1 and PP-2A to okadaic acid, we have previously shown that inhibition of protein phosphatase-1 but not –2A induces apoptosis of both rat and rabbit lens epithelial cells. To further confirm this observation, we have examined the effect of calyculin A, another inhibitor for protein phosphatase-1 and –2A. Methods: Rabbit lens epithelial cells were grown to 100% confluence in MEM and then treated with calyculin A from 1 to 12 nM for 2 to 24 hours. The treated and control cells were analyzed with cell flow cytometry and DNA fragmentation for apoptosis. The proteins extracted from both treated and control cells were analyzed with Western blot. Results: Treatment of N/N1003A cells with calyculin A in a concentration from 3 nM to 12 nM induces apoptosis. The percentage of apoptosis is dependent upon the treatment time and concentration of calyculin A. Calyculin A activates a death program including p53, members of the Bcl-2 family and also caspase-3. Conclusions: Protein phosphatase-1 acts as an important antiapoptotic regulator in lens epithelial cells. Supported by EY 11372 and the Hormel Foundation. None.

Keywords: signal transduction • apoptosis/cell death • cataract 
© 2003, 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.
Copyright © 2024 Association for Research in Vision and Ophthalmology.
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