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Advanced Glycation End Products in Human Cancer Tissues: Detection of N ε ‐(Carboxymethyl)lysine and Argpyrimidine
Author(s) -
HEIJST JEROEN W. J.,
NIESSEN HANS W. M.,
HOEKMAN KLAAS,
SCHALKWIJK CASPER G.
Publication year - 2005
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1333.084
Subject(s) - glycation , lysine , chemistry , cancer , glycolysis , biochemistry , metabolism , medicine , amino acid , receptor
A bstract : 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 N ε ‐(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.