ISPO

Published in Cancer Detection and Prevention 2000; 24(Supplement 1).

BCL-2 in L929 cells inhibits tumor necrosis factor-mediated increase of glycolysis and accelerates tricarboxylic acid cycle

YH Kim PhD, SS Kim PhD

Dept Biochemistry, College of Science, Yonsei University, Seoul, Korea, Kimss518@bubble.yonsei.ac.kr

Summary In order to understand the effects of bcl-2 on glucose metabolism, activities of glycolytic enzymes (hexokinase, 6-phosphofructo- I -kinase, and pyruvate kinase), lactate dehydrogenase, pyruvate carboxylase, and phosphoenolpyruvate carboxykinase in L929 cells and bcl-2 transfected L929 cells were examined in the absence or presence of TNF treatment. In TNF-treated L929 cells, the activities of glycolytic enzyme and lactate dehydrogenase were highly increased, but there were no changes in pyruvate carboxylase and phosphoenolpyruvate carboxykinase activities. The levels of activities of the glycolytic enzymes and lactate dehydrogenase in bcl-2 transfected L929 cells were lower than those of control L929 cells upon TNF treatment. On the other hand, the activity of pyruvate carboxylase in bcl-2 transfected L929 cells was increased approximately 20~~~l00O/o at 6 h when compared to the control L929 cells upon TNF treatment. The activity of phosphoenolpyruvate carboxykinase of bcl-2 transfected L929 cells was slightly lower than that of L929 cells. The data suggest that bcl-2 prevents abrupt increase of glycolysis and lactate dehydrogenase activity mediated by TNF and accelerate tricarboxylic acid cycle to produce ATP, but not gluconeogenesis in TNF-resistant bcl-2 transfected L929 cells.

For more information, contact Kimss518@bubble.yonsei.ac.kr

Paper presented at the International Symposium on Impact of Biotechnology on Cancer Diagnostic & Prognostic Indicators; Geneva, Switzerland; October 28 - 31, 2000; in the section on chemotherapy.

http://www.cancerprev.org/Journal/Issues/24/101/413/3767