ABSTRACT
AIM: To study the metalloproteome of DU-145 prostate carcinoma cells in comparison to prostate from control and selenium-deficient rats. MATERIALS AND METHODS: Total proteome of the samples was compared by two-dimensional electrophoresis (2-DE) and metalloproteome was analysed by size-exclusion chromatography coupled to inductively coupled plasma mass spectrometry (SEC-ICP/MS). Immunotests were used to quantify protein expression of superoxide dismutase, thioredoxin reductase and metallothionein. RESULTS: There was no general relation between protein expression and metal load. SEC-ICP/MS spectra for many metals varied significantly in terms of peak number and intensity between individuals of the same sample group. However, nickel and zinc peaks were consistently suppressed in DU-145 cells under selenium deficiency. Concurrent redistribution of cobalt binding to a low molecular weight fraction (presumably cobalamin) was observed. CONCLUSION: Metal load of proteins in comparison to their expression might point to yet unknown mechanisms of oncogenesis and may lead to new biomarkers of cancer.