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   <subfield code="a">10.1007/s000180050039</subfield>
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   <subfield code="a">A possible new role for the anti-ageing peptide carnosine</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[A. R. Hipkiss*, C. Brownson]</subfield>
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   <subfield code="a">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.</subfield>
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   <subfield code="a">Birkhäuser Verlag Basel,, 2000</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">Key words. Protein</subfield>
   <subfield code="2">nationallicence</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">aging</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">ageing</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">carbonyl</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">glycation</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">proteolysis</subfield>
   <subfield code="2">nationallicence</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">lipofuscin</subfield>
   <subfield code="2">nationallicence</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">advanced glycosylation end-product</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">Hipkiss*</subfield>
   <subfield code="D">A. R.</subfield>
   <subfield code="u">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</subfield>
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   <subfield code="a">Brownson</subfield>
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   <subfield code="u">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</subfield>
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   <subfield code="D">A. R.</subfield>
   <subfield code="u">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</subfield>
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   <subfield code="u">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</subfield>
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   <subfield code="a">Metadata rights reserved</subfield>
   <subfield code="b">Springer special CC-BY-NC licence</subfield>
   <subfield code="2">nationallicence</subfield>
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