Advanced Glycation End Products in Human Cancer Tissues: Detection of Nε-(Carboxymethyl)lysine and Argpyrimidine

Authors

  • JEROEN W. J. VAN HEIJST,

    1. Departments of Clinical Chemistry, VU University Medical Center, Amsterdam, the Netherlands
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  • HANS W. M. NIESSEN,

    1. Departments of Pathology, VU University Medical Center, Amsterdam, the Netherlands
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  • KLAAS HOEKMAN,

    1. Departments of Oncology, VU University Medical Center, Amsterdam, the Netherlands
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  • CASPER G. SCHALKWIJK

    Corresponding author
    1. Departments of Clinical Chemistry, VU University Medical Center, Amsterdam, the Netherlands
    • Casper G. Schalkwijk, Ph.D., Department of Internal Medicine, University Hospital Maastricht, Debeyelaan 25, P.O. Box 5800, 6202 AZ Maastricht, the Netherlands. Voice: +31 43 3882186; fax: +31 43 3875006. C.Schalkwijk@INTMED.unimaas.nl

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    • Casper G. Schalkwijk, Ph.D., Department of Internal Medicine, University Hospital Maastricht, Debeyelaan 25, P.O. Box 5800, 6202 AZ Maastricht, the Netherlands. Voice: +31 43 3882186; fax: +31 43 3875006. C.Schalkwijk@INTMED.unimaas.nl


Abstract

Abstract: Tumors are generally characterized by an increased glucose uptake and a high rate of glycolysis. Since one consequence of an elevated glycolysis is the nonenzymatic glycation of proteins, we studied the presence of advanced glycation end products (AGEs) in human cancer tissues. We detected the presence of the AGEs Nε-(carboxymethyl)lysine (CML) and argpyrimidine in several human tumors using specific antibodies. Because AGEs have been associated with the etiology of a variety of different diseases, these results suggest that CML and argpyrimidine could be implicated in the biology of human cancer.

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