Abstract
ONE of the characteristic changes associated with the ageing of human fibroblasts in cell culture is the presence of increasing amounts of altered molecules1–3. Such alterations have been detected for at least three cytoplasmic enzymes: glucose-6-phosphate dehydrogenase (G6PD), 6-phosphogluconate dehydrogenase and hypoxanthine-guanine-phosphoribosyl-transferase. For each enzyme, the proportion of molecules which are modified reaches as much as 25% in cells of the last generations. The origin of these alterations is still only an hypothesis. Some authors1, in agreement with Orgel's error catastrophe theory4, suggest that they are the result of a faulty synthesising machinery; others5–7, however, suggest that they are due to a post-translational effect. We present here a study on the heat lability of some lysosomal and mitochondrial enzymes to test whether the alterations also affect proteins present in these subcellular entities. We compare the results with the predictions of the above hypotheses, and suggest that they probably are best explained in terms of a post-translational modification.
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HOUBEN, A., REMACLE, J. Lysosomal and mitochondrial heat labile enzymes in ageing human fibroblasts. Nature 275, 59–60 (1978). https://doi.org/10.1038/275059a0
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DOI: https://doi.org/10.1038/275059a0
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