Abstract
KNOWLEDGE of the intracellular processes of ageing and breakdown of proteins is still very limited1,2, but the extremely slow turnover of lens proteins in the eye provides a unique opportunity to analyse such processes. Throughout life fibre cells are formed from epithelial cells at the periphery of the lens, being successively covered by younger cells. Protein synthesis ceases soon after the differentiation into fibre cells is completed3. As a result the nucleus of the lens of an adult still contains the proteins formed during foetal life. Here we demonstrate that differences in polypeptide structure observed between the cortex and nucleus4–6 of the lens are due to an ageing process. Our data provide the first example of progressive degradation and deamidation of a protein, probably caused by non-enzymatic mechanisms.
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VAN KLEEF, F., DE JONG, W. & HOENDERS, H. Stepwise degradations and deamidation of the eye lens protein α-crystallin in ageing. Nature 258, 264–266 (1975). https://doi.org/10.1038/258264a0
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DOI: https://doi.org/10.1038/258264a0
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