2739

GLO1

glyoxalase I;GLO1;glyoxalase I

S-D-lactoylglutathione methylglyoxal lyase|aldoketomutase|epididymis secretory protein Li 74|glx I|glyoxalase domain containing 1|ketone-aldehyde mutase|lactoyl glutathione lyase|lactoylglutathione lyase|methylglyoxalase

6p21.3-p21.1

protein-coding

Three clones with differential metastatic potential were established from the parental SN12C human renal cell carcinoma (HRCC). We previously reported that in the two high metastatic SN12C clones, two isoforms of ubiquitin carboxyl-terminal hydrolase isozyme L1 (UCHL1) showed decreased expression by using two-dimensional electrophoresis (2DE) covering a pH range (pH 3.010.0) followed by liquid chromatographytandem mass spectrometry. However, in the case of the low metastatic clone, the spot volume for UCHL1 was almost the same as for the parental SN12C. In the present study, we found one protein spot which was correlated with the metastatic potential of SN12C clones by using 2DE over a narrow pH range (pH 4.07.0). The protein glyoxalase 1 (GLO1) appeared to be directly proportional to the metastatic potential of the SN12C clones. GLO1 was the only protein which consistently varied according to the metastatic potentials of SN12C clones. GLO1 was increased in high metastatic cell lines by western blot analysis. These findings suggest that GLO1 is associated with the metastatic potential of SN12C HRCC clones. We expanded our experimental range to include clones of scirrhous gastric cancer cell lines (OCUM2M, OCUM2D and OCUM2MLN) and similar results were obtained, thereby further strengthening our original findings.