IOVS AJP: Regulatory, Integrative and Comparative Physiology
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(Investigative Ophthalmology and Visual Science. 2005;46:1085-1091.)
© 2005 by The Association for Research in Vision and Ophthalmology, Inc.
DOI:  10.1167/iovs.04-0042
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Heat Shock Protein 27 Delays Ca2+-Induced Cell Death in a Caspase-Dependent and -Independent Manner in Rat Retinal Ganglion Cells

N. Andrew Whitlock,1 Kristie Lindsey,2 Neeraj Agarwal,3 Craig E. Crosson,1 and Jian-Xing Ma4

1From the Hewitt Laboratory of the Ola B. Williams Glaucoma Center, Department of Ophthalmology, and the 2Department of Pharmacology, Medical University of South Carolina, Charleston, South Carolina; the 3Department of Pathology and Anatomy, University of North Texas Health Science Center, Fort Worth, Texas; and the 4Department of Cell Biology, Department of Medicine, University of Oklahoma Health Science Center, Oklahoma City, Oklahoma.

PURPOSE. Hsp27 is a well-characterized and studied antiapoptotic protein. A recent study reported that Hsp27 is upregulated in the retina after retinal ischemic preconditioning. The timing of this upregulation of Hsp27 correlates with the protective effects of the treatment. It was the goal of the current study to determine what role Hsp27 plays in this protection.

METHODS. The rat homologue of Hsp27 (rHsp27) was overexpressed in a transformed rat retinal ganglion cell line and subjected to ischemic stress and calcium overload.

RESULTS. The overexpression of rHsp27 increased cell survival and inhibited caspase-3 activation. However, the inhibition of caspase-3 alone had no effect on cell survival. Proteomic analysis after Ca2+ overload identified four proteins that were repeatedly associated with rHsp27. These proteins include actin, Hsp70, eEF-1{alpha}, and SPIN-2. No association with cytochrome c or any caspase enzymes was detected.

CONCLUSIONS. The results indicate that Hsp27 protects the retinal cells by both caspase-dependent and -independent mechanisms.




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