Advanced glycation end products in human cancer tissues: detection of Nepsilon-(carboxymethyl)lysine and argpyrimidine.
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(epsilon)-(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.
van Heijst
Jeroen W J
JW
Department of Internal Medicine, University Hospital Maastricht, Debeyelaan 25, P.O. Box 5800, 6202 AZ Maastricht, the Netherlands.
Niessen
Hans W M
HW
Hoekman
Klaas
K
Schalkwijk
Casper G
CG
D004797:Enzyme-Linked Immunosorbent Assay; D017127:Glycation End Products, Advanced / Q000032:analysis*; D006019:Glycolysis; D006801:Humans; D008239:Lysine / Q000031:analogs & derivatives* / Q000032:analysis; D009363:Neoplasm Proteins / Q000737:chemistry / Q000378:metabolism; D009369:Neoplasms / Q000737:chemistry* / Q000473:pathology*; D011765:Pyruvaldehyde / Q000032:analysis
D017127:Glycation End Products, Advanced; D009363:Neoplasm Proteins; C048496:N(6)-carboxymethyllysine; D011765:Pyruvaldehyde; D008239:Lysine