May 2008
Volume 49, Issue 13
Free
ARVO Annual Meeting Abstract  |   May 2008
Loss of Alpha Crystallin-Gamma Crystallin Interactions During Aging of the Bovine Lens
Author Affiliations & Notes
  • L. J. Takemoto
    Biology, Kansas State University, Manhattan, Kansas
  • Footnotes
    Commercial Relationships  L.J. Takemoto, None.
  • Footnotes
    Support  NIH Grant EY02932
Investigative Ophthalmology & Visual Science May 2008, Vol.49, 4094. doi:https://doi.org/
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    • Get Citation

      L. J. Takemoto; Loss of Alpha Crystallin-Gamma Crystallin Interactions During Aging of the Bovine Lens. Invest. Ophthalmol. Vis. Sci. 2008;49(13):4094. doi: https://doi.org/.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Purpose: : To quantitate the possible heterologous interactions of alpha crystallins and gamma crystallins from aged and young lens fiber cells

Methods: : Total water soluble alpha crystallins were prepared from the nucleus of aged bovine lens, and total water soluble gamma crystallins were prepared either from the nucleus of aged bovine lens, or cortex of fetal bovine lens, using TSK SW3000 gel filtration chromatography. Aged alpha crystallin, with either aged gamma crystallins or fetal gamma crystallins, were loaded into microequilibrium dialysis chambers, separated by a 100,000 kD cut-off filter, then allowed to equilibrate for 5 days at 37 degress C. At equilibrium, the amount of different gamma crystallin species in each chamber were quantitated by HPLC reverse phase chromatography, to determine if any gamma crystallin species associated with aged alpha crystallins.

Results: : Some, but not all, gamma crystallins from fetal lens associated with alpha crystallins from nucleus of old lens. None of the gamma crystallins from nucleus of old lens associated with aged alpha crystallins.

Conclusions: : Heterologous interactions between alpha crystallins and gamma crystallins decrease during aging. In the nucleus of aged bovine lens, there are no detectable interactions between alpha and gamma crystallins. Loss of such associations may play a role in alterations in short-range protein interactions thought to be important for the transparent properties of the lens.

Keywords: crystallins • aging • protein modifications-post translational 
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