Maillard products as biomarkers in cancer.
Because tumors exert increased glycolysis rates, a high intracellular carbonyl stress with the formation of Maillard products may evolve. Therefore, we studied the presence of N epsilon-(carboxymethyl)lysine (CML) modification in breast cancer tissues from 20 patients and found significant cytoplasmatic staining in tumor cells that was independent of the tumor stage, tumor type, and microanatomic localization. Studying breast cancer cell lines, we also found strong cytoplasmatic CML staining that was again independent of their invasive or metastatic behavior. Our results reveal that tumor cells show a strong cytoplasmatic immunoreactivity to CML without evident association with breast carcinoma type, differentiation, tumor stage, or intratumoral localization. We conclude that CML formation is a general tumor cell-associated process.
Bachmeier
Beatrice E
BE
Department of Clinical Chemistry and Clinical Biochemistry, Ludwig-Maximilians-University Munich, D-80336 Munich, Germany.
Nerlich
Andreas G
AG
Rohrbach
Helmut
H
Schleicher
Erwin D
ED
Friess
Ulrich
U
D014408:Biomarkers, Tumor / Q000032:analysis*; D001943:Breast Neoplasms / Q000097:blood* / Q000473:pathology / Q000601:surgery; D003593:Cytoplasm / Q000473:pathology; D005260:Female; D006019:Glycolysis; D006801:Humans; D007150:Immunohistochemistry; D008239:Lysine / Q000031:analogs & derivatives* / Q000032:analysis; D015416:Maillard Reaction; D009361:Neoplasm Invasiveness
D014408:Biomarkers, Tumor; C048496:N(6)-carboxymethyllysine; D008239:Lysine