April 2010
Volume 51, Issue 13
Free
ARVO Annual Meeting Abstract  |   April 2010
-Crystallin and Cytochrome C Form a Mitochondrial Complex With MsrA in Lens Cells
Author Affiliations & Notes
  • R. McGreal
    Biomedical Sciences, Florida Atlantic University, Boca Raton, Florida
  • W. Lee
    Biomedical Sciences, Florida Atlantic University, Boca Raton, Florida
  • M. Demos
    Biomedical Sciences, Florida Atlantic University, Boca Raton, Florida
  • L. Brennan
    Biomedical Sciences, Florida Atlantic University, Boca Raton, Florida
  • M. Kantorow
    Biomedical Sciences, Florida Atlantic University, Boca Raton, Florida
  • Footnotes
    Commercial Relationships  R. McGreal, None; W. Lee, None; M. Demos, None; L. Brennan, None; M. Kantorow, None.
  • Footnotes
    Support  NIH grant EY13022
Investigative Ophthalmology & Visual Science April 2010, Vol.51, 1183. doi:
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      R. McGreal, W. Lee, M. Demos, L. Brennan, M. Kantorow; -Crystallin and Cytochrome C Form a Mitochondrial Complex With MsrA in Lens Cells. Invest. Ophthalmol. Vis. Sci. 2010;51(13):1183.

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Abstract

Purpose: : Oxidation of α -crystallin and cytochrome c (cyt c) at specific methionine residues results in loss of their respective chaperone and oxidoreductase activities. Both α -crystallin and cyt c are oxidized in the lenses of Methionine Sulfoxide Reductase A (MsrA) knockout mice in vivo and their activities are dependent on repair by MsrA. Both cyt c, α -crystallin and MsrA are localized to lens cells suggesting they may form a functional complex in specific lens cell sub-types. Here, we examined possible interactions between α -crystallin and cyt c in lens cells as a first step towards establishing a possible role for α -crystallin and MsrA in modulating the apoptotic and oxidoreductase activities of cyt c.

Methods: : Levels of cyt c and α -crystallin (total, α A and α B-crystallin) were examined by RT-PCR and western analysis of microdissected mouse and human lenses. Protein complexes were analyzed by co-immune precipitation analysis of extracts from cultured human lens epithelial cells (HLEB3 and SRA04/01) and whole human lenses. Protein complexes were further examined by microdissection of whole human and mouse lenses followed by immunoflourescent microscopy and organelle imaging.

Results: : As expected, high levels of α -crystallin, MsrA and cyt c were detected in the lens epithelium. Unexpectedly, significant levels of cyt c were also detected in lens fibers. MsrA, cyt c and α -crystallin formed stable complexes that were detected in all lens tissues. These complexes preferentially resided in lens mitochondria.

Conclusions: : These results suggest that MsrA, α -crystallin and cyt c form complexes in lens epithelia and fibers. They suggest that both the oxidative stress repair activity of MsrA and the chaperone function of α -crystallin may modulate the activity of cyt c in the lens affecting both lens mitochondrial function, apoptosis and possibly lens differentiation.

Keywords: apoptosis/cell death • chaperones • mitochondria 
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