期刊
EUROPEAN JOURNAL OF BIOCHEMISTRY
卷 267, 期 19, 页码 6067-6073出版社
BLACKWELL SCIENCE LTD
DOI: 10.1046/j.1432-1327.2000.01687.x
关键词
porin; voltage-dependent anion channel (VDAC); mitochondria; cDNA cloning; hexokinase
Mitochondria from malignant tumor cell lines show a higher capability for hexokinase binding than those from normal liver. To explore possible differences in hexokinase binding sites of mitochondria between tumor cells and normal liver, we characterized porin isoforms expressed in tumor cells. Cloning experiments on the three porin isoforms, VDAC1, VDAC2 and VDAC3 from malignant tumor cell line AH130 clearly showed that their primary structures were completely identical to those of the corresponding VDACs of normal liver cells. Possible expression of the fourth porin isoform in AH130 cells was excluded by degenerate primer-based RT-PCR. However, the transcript levels of the three VDAC isoforms in AH130 cells were significantly higher than those in normal liver. These results suggest that the high hexokinase-binding capability of malignant tumor cell mitochondria was not due to any structural difference, but due to a quantitative difference in binding sites.
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