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PMID: 16037299 Published · ppublish English Journal Article

Advanced glycation end products in human cancer tissues: detection of Nepsilon-(carboxymethyl)lysine and argpyrimidine.

Annals of the New York Academy of Sciences ·Vol. 1043 ·2005-06-00 ·Pages 725-33

van Heijst JW, Niessen HW, Hoekman K, Schalkwijk CG

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 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.

MeSH Terms
Enzyme-Linked Immunosorbent Assay Glycation End Products, Advanced/analysis Glycolysis Humans Lysine/analogs & derivatives,analysis Neoplasm Proteins/chemistry,metabolism Neoplasms/chemistry,pathology Pyruvaldehyde/analysis
Chemicals
Glycation End Products, Advanced Neoplasm Proteins N(6)-carboxymethyllysine Pyruvaldehyde Lysine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
van Heijst Jeroen W J
Department of Internal Medicine, University Hospital Maastricht, Debeyelaan 25, P.O. Box 5800, 6202 AZ Maastricht, the Netherlands.
Niessen Hans W M
Hoekman Klaas
Schalkwijk Casper G
Article Info
Journal
Annals of the New York Academy of Sciences
Abbr.
Ann N Y Acad Sci
ISSN
0077-8923
Published
2005-06-00
Pages
725-33
Language
English
Region
United States
NLM ID
7506858
Subset
IM
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