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Research article| Volume 129, ISSUE 1, P62-68, March 1995

Non-enzymatic glycation of peripheral nerve proteins in human diabetics

  • Catherine Ryle
    Affiliations
    Institute of Molecular Medicine, University of Oxford and Department of Clinical Neurology, Radcliffe Infirmary, Oxford OX2 6HE, UK
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  • Michael Donaghy
    Correspondence
    Corresponding author. Tel.: 0865-224698; Fax: 0865-790493.
    Affiliations
    Institute of Molecular Medicine, University of Oxford and Department of Clinical Neurology, Radcliffe Infirmary, Oxford OX2 6HE, UK
    Search for articles by this author
DOI:https://doi.org/10.1016/0022-510X(94)00251-I
Non-enzymatic glycation of peripheral nerve proteins in human diabetics
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      Abstract

      We have measured non-enzymatic glycation of proteins in the cytoskeletal and myelin fractions of nerve fascicles from human sural nerves obtained from diabetic and non-diabetic amputation specimens. Levels of the early reversible glycation adduct, measured as furosine did not differ significantly between diabetics and controls in either protein fraction. Pentosidine levels per unit protein were significantly elevated in diabetics relative to controls in both cytoskeletal (5.96 vs 4.47; p = 0.037) and myelin protein (1.35 vs 0.69; p = 0.023) fractions. Protein cross-linkage in the cytoskeletal fraction, probably due to AGEs, was also higher in diabetics than controls (504 vs 349; p = 0.057). These results show that increased AGE accumulation occurs in cytoskeletal, as well as myelin, peripheral nerve proteins in diabetics. This suggests a possible new mechanism contributing to the axonal degeneration polyneuropathy of diabetes which is based upon irreversible glycation of axonal cytoskeletal proteins causing their cross-linkage and altered function.

      Keywords

      Abbreviations:

      AGE (advanced glycation endproduct), DRG (dorsal root ganglion), NF (neurofilament), PMSF (phenyl methyl sulfonyl fluoride)
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      Article info

      Publication history

      Accepted: October 23, 1994
      Received in revised form: October 14, 1994
      Received: March 9, 1994

      Identification

      DOI: https://doi.org/10.1016/0022-510X(94)00251-I

      Copyright

      © 1995 Published by Elsevier Inc.

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