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J Biol Chem, Vol. 273, Issue 46, 30239-30243, November 13, 1998
,,,
From the Deoxycytidine kinase (dCK) catalyzes the
rate-limiting step of the deoxynucleoside salvage pathway in mammalian
cells and plays a key role in the activation of several
pharmacologically important nucleoside analogs. Using a highly specific
polyclonal antibody raised against a C-terminal peptide of the human
dCK, we analyzed its subcellular localization by Western blots of
biochemically fractionated nuclear and cytoplasmic fractions as well as
by in situ immunochemistry. Native dCK was found to be
located mainly in the cytoplasm in several cell types, and the enzyme
was more concentrated in the perinuclear and cellular membrane area. In contrast, when dCK was overexpressed in the cells, it was mainly located in the nucleus. The results demonstrate that native dCK is a
cytoplasmic enzyme. However, it has the ability to enter the nucleus
under certain conditions, suggesting the existence of a cytoplasmic
retention mechanism that may have an important function in the
regulation of the deoxynucleoside salvage pathway.
Institute of Molecular Biology and
Biotechnology, Foundation for Research and Technology Hellas,
711 10 Herakleion, Crete, Greece and § Department of
Veterinary Medical Chemistry, The Biomedical Center, S-751 23 Uppsala, Sweden
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