title: Heat shock protein 27 delays Ca2+-induced cell death in a caspase-dependent and -independent manner in rat retinal ganglion cells.
abstract: OBJECTIVE
  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 Ca(2+) overload identified four proteins that were repeatedly associated with rHsp27. These proteins include actin, Hsp70, eEF-1alpha, 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.
authors.affiliation: Hewitt Laboratory of the Ola B. Williams Glaucoma Center, Department of Ophthalmology, Medical University of South Carolina, Charleston, SC 29425, USA.
authors.forename: N Andrew
authors.initials: NA
authors.lastname: Whitlock
authors.forename: Kristie
authors.initials: K
authors.lastname: Lindsey
authors.forename: Neeraj
authors.initials: N
authors.lastname: Agarwal
authors.forename: Craig E
authors.initials: CE
authors.lastname: Crosson
authors.forename: Jian-Xing
authors.initials: JX
authors.lastname: Ma
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D053148:Caspase 3; D061945:Caspase Inhibitors; D020169:Caspases / Q000378:metabolism*; D002461:Cell Line, Transformed; D002470:Cell Survival / Q000187:drug effects / Q000502:physiology; D019610:Cytoprotection; D004789:Enzyme Activation; D005434:Flow Cytometry; D019084:Fluorescent Antibody Technique, Indirect; D015870:Gene Expression / Q000502:physiology; D055551:HSP27 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000235:genetics / Q000502:physiology*; D009363:Neoplasm Proteins / Q000235:genetics / Q000502:physiology*; D009687:Nuclear Proteins / Q000378:metabolism; D018384:Oxidative Stress; D010445:Peptide Elongation Factors / Q000378:metabolism; D051381:Rats; D012165:Retinal Ganglion Cells / Q000166:cytology* / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D015854:Up-Regulation
chemical_list: D000199:Actins; D061945:Caspase Inhibitors; D055551:HSP27 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C486114:Hspb1 protein, rat; D009363:Neoplasm Proteins; D009687:Nuclear Proteins; D010445:Peptide Elongation Factors; C463239:SPIN2A protein, human; C057342:peptide elongation factor 1H; C505407:CASP3 protein, human; C505410:Casp3 protein, rat; D053148:Caspase 3; D020169:Caspases; D002118:Calcium