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Originally published In Press as doi:10.1167/iovs.09-3588 on May 20, 2009
 (Investigative Ophthalmology and Visual Science. 2009;50:4786-4793.)
© 2009 by The Association for Research in Vision and Ophthalmology, Inc.
doi:10.1167/iovs.09-3588
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Membrane Association of Proteins in the Aging Human Lens: Profound Changes Take Place in the Fifth Decade of Life

Michael G. Friedrich1,2 and Roger J. W. Truscott1

1From the Save Sight Institute, Sydney University, Sydney, NSW, Australia; and the 2Department of Chemistry, University of Wollongong, Wollongong, NSW, Australia.

PURPOSE. To characterize age-related changes to proteins in the center of the human lens.

METHODS. Human lenses of different ages were dissected using trephines. Sucrose density gradient centrifugation was used to separate the proteins from two defined nuclear regions. Densitometry of Coomassie-stained protein bands was compared with lipid analysis with the use of mass spectrometry.

RESULTS. A profound change in the density gradient profiles of lenses occurred at approximately age 40. As soluble crystallins decreased, four higher density bands appeared that were absent in younger lenses. These four bands contained crystallins, as well as membrane lipids, and appear to have resulted from the interaction of denatured crystallins with fiber cell membranes.

CONCLUSIONS. Changes in lens proteins and membranes can be detected in each decade of life; however, major changes to the lens crystallins of the nucleus take place between age 40 and 50, after the loss of free soluble alpha crystallin. These alterations are consistent with large-scale binding of crystallin aggregates to fiber cell membranes after middle age.






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