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Journal of Histochemistry and Cytochemistry, Vol. 51, 105-112, January 2003, Copyright © 2003, The Histochemical Society, Inc.

ARTICLE

Post-translational Regulation of Glucose-6-phosphate Dehydrogenase Activity in (Pre)neoplastic Lesions in Rat Liver

Wilma M. Frederiksa, Klazina S. Boscha, Jonas S.S.G. De Jonga, and Cornelis J.F. Van Noordena
a Academic Medical Center, University of Amsterdam, Department of Cell Biology and Histology, Amsterdam, The Netherlands

Correspondence to: Wilma M. Frederiks, Dept. of Cell Biology and Histology, Academic Medical Center, Meibergdreef 15, 1105 AZ Amsterdam, The Netherlands. E-mail: w.m.frederiks@amc.uva.nl

Glucose-6-phosphate dehydrogenase (G6PD; EC 1.1.1.49) is the key regulatory enzyme of the pentose phosphate pathway and produces NADPH and riboses. In this study, the kinetic properties of G6PD activity were determined in situ in chemically induced hepatocellular carcinomas, and extralesional and control parenchyma in rat livers and were directly compared with those of the second NADPH-producing enzyme of the pentose phosphate pathway, phosphogluconate dehydrogenase (PGD). Distribution patterns of G6PD activity, protein, and mRNA levels were also compared to establish the regulation mechanisms of G6PD activity. In (pre)neoplastic lesions, the Vmax of G6PD was 150-fold higher and the Km for G6P was 10-fold higher than in control liver parenchyma, whereas in extralesional parenchyma, the Vmax was similar to that in normal parenchyma but the Km was fivefold lower. This means that virtual fluxes at physiological substrate concentrations are 20-fold higher in lesions and twofold higher in extralesional parenchyma than in normal parenchyma. The Vmax of PGD was fivefold higher in lesions than in normal and extralesional liver parenchyma, whereas the Km was not affected. Amounts of G6PD protein and mRNA were similar in lesions and in extralesional liver parenchyma. These results demonstrate that G6PD is strongly activated post-translationally in (pre)neoplastic lesions to produce NADPH. (J Histochem Cytochem 51:105–112, 2003)

Key Words: glucose-6-phosphate, dehydrogenase, phosphogluconate, dehydrogenase, (pre)neoplasm, hepatoma, enzyme histochemistry, immunohistochemistry, in situ hybridization, image analysis


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