A possible new role for the anti-ageing peptide carnosine |
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Authors: | A R Hipkiss C Brownson |
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Institution: | (1) Biomolecular Sciences Division, GKT School of Biomedical Sciences, King’s College London, Guy’s Campus London Bridge, London, SE1 1UL (UK), Fax +44 207 848 6399, e-mail: alan.hipkiss@kcl.ac.uk, UA |
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Abstract: | The naturally occurring dipeptide carnosine (β-alanyl-L-histidine) is found in surprisingly large amounts in long-lived tissues and can delay ageing in cultured human fibroblasts.
Carnosine has been regarded largely as an anti-oxidant and free radical scavenger. More recently, an anti-glycating potential
has been discovered whereby carnosine can react with low-molecular-weight compounds that bear carbonyl groups (aldehydes and
ketones). Carbonyl groups, arising mostly from the attack of reactive oxygen species and ow-molecular-weight aldehydes and
ketones, accumulate on proteins during ageing. Here we propose, with supporting evidence, that carnosine can react with protein
carbonyl groups to produce protein-carbonyl-carnosine adducts (‘carnosinylated’ proteins). The various possible cellular fates
of the carnosinylated proteins are discussed. These proposals may help explain anti-ageing actions of carnosine and its presence
in non-mitotic cells of long-lived mammals.
Received 29 November 1999; accepted 27 December 1999 |
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Keywords: | , Protein, aging, ageing, carbonyl, glycation, proteolysis, lipofuscin, advanced glycosylation end-product, |
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