Conclusion
In contrast to deoxycytidine kinase from leukemic blasts7, the recombinant dCK is a poor substrate for protein kinase C. Protein kinase A effectively phosphorylates the recombinant dCK. However, neither substrate specificity, nor kinetic parameters of dCK were changed upon phosphorylation. Nevertheless, treatment of partially purified lymphocyte dCK with recombinant phosphoprotein phosphatase completely destroys its phosphotransferase activity. These data suggest that phosphorylation plays a role in the regulation of lymphocyte dCK
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Sasvári-Székely, M., Spasokoukotskaja, T., Szoke, M., Csapo, Zs., Turi, A., Szanto, I., Eriksson, S., and Staub, M., 1998, Activation of deoxycytidine kinase during inhibition of DNA synthesis by 2-chloro-2′-deoxyadenosine (Cladribine) in human lymphocytes. Biochemical Pharmacol., 56, 1175–1179.
Spasokoukotskaja, T., Sasvári-Székely, M., Keszler, G., Albertioni, F., Eriksson, S., and Staub, M., 1999, Treatment of normal and malignant cells with nucleoside analogues and etoposide enhances deoxycytidine kinase activity. Eur.J. Cancer 35, 1862–1867.
Staub, M., Csapó, Zs., Spasokoukotskaja, T., and Sasvári-Székely, M., 1998, Deoxycytidine kinase can be, also potentiated by the G-protein activator NaF in cells. Adv. Exp. Med. Biol. 431, 425–428.
Chottiner, E., G., Shewach, D.S., Datta, N.S., Ashcraft, E., Gribbin, D., Ginsburg, D., Fox, I.H., and Mitchell, B.S., 1991, Cloning and expression of human deoxycytidine kinase cDNA. Proc. Natl. Acad. Sci. USA 88, 1531–1535.
Arnér, E.S.J., Spasokoukotskaja, T., and Eriksson, S., 1992, Selective assay for thymidine kinase 1 and 2 and deoxycytidine kinase and their activities in extracts from human cells and tissues. Biochem. Biophys. Res. Commun. 188, 712–718.
Wang, L., Karlsson, A., Arnér, E.S., and Eriksson, S., 1993, Substrate specificity of mitochondrial2′-deoxyguanosine kinase. Efficient phosphorylation of 2-chlorodeoxyadenosine. J. Biol. Chem. 268, 22847–22852.
Wang, L. M., and Kucera, G. L., 1994, Deoxycytidine kinase is phosphorylated in vitro by protein kinase C. Biochim. Biophys. Acta-Mol. Cell Res., 1224, 161–167.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2002 Kluwer Academic Publishers
About this chapter
Cite this chapter
Spasokoukotskaja, T. et al. (2002). Effect of Phosphorylation on Deoxycytidine Kinase Activity. In: Zoref-Shani, E., Sperling, O. (eds) Purine and Pyrimidine Metabolism in Man X. Advances in Experimental Medicine and Biology, vol 486. Springer, Boston, MA. https://doi.org/10.1007/0-306-46843-3_55
Download citation
DOI: https://doi.org/10.1007/0-306-46843-3_55
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-306-46515-4
Online ISBN: 978-0-306-46843-8
eBook Packages: Springer Book Archive