Chaperone-independent mitochondrial translocation and protection by αB-crystallin in RPE cells

Rebecca S. McGreal, Lisa A. Brennan, Wanda Lee Kantorow, Jeffrey D. Wilcox, Jianning Wei, Daniel Chauss, Marc Kantorow

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


αB-crystallin is a small heat shock protein that exhibits chaperone activity and can protect multiple cell types against oxidative stress damage. Altered levels and specific mutations of αB-crystallin are associated with multiple degenerative diseases. We previously found that αB-crystallin translocates to lens and retinal cell mitochondria upon oxidative stress exposure where it provides protection against oxidative stress damage. To date, the role of the chaperone function of αB-crystallin in mitochondrial translocation and protection has not been established. Here, we sought to determine the relationship between the chaperone activity of αB-crystallin and its ability to translocate to and protect retinal cell mitochondria against oxidative stress damage. Our data provide evidence that three forms of αB-crystallin exhibiting different chaperone activity levels including wild-type, R120G (decreased chaperone activity) and M68A (increased chaperone activity) provide comparable levels of mitochondrial translocation and protection to retinal cells exposed to oxidative stress. The results provide evidence that mitochondrial translocation and protection by αB-crystallin is independent of its chaperone activity and that other functions of αB-crystallin may also be independent of its chaperone activity.

Original languageEnglish (US)
Pages (from-to)10-17
Number of pages8
JournalExperimental Eye Research
StatePublished - May 2013
Externally publishedYes


  • Chaperone
  • Mitochondria
  • Oxidative stress
  • RPE
  • Retinal cells
  • Small heat shock protein
  • αB-crystallin

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience


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