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

Ann N Y Acad Sci. 2005 Jun;1043:725-33. doi: 10.1196/annals.1333.084.

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*
  • Lysine / analysis
  • Neoplasm Proteins / chemistry
  • Neoplasm Proteins / metabolism
  • Neoplasms / chemistry*
  • Neoplasms / pathology*
  • Pyruvaldehyde / analysis

Substances

  • Glycation End Products, Advanced
  • Neoplasm Proteins
  • N(6)-carboxymethyllysine
  • Pyruvaldehyde
  • Lysine