Abstract
Purine riboside (PuR, purine-1-D-ribofuranoside, nebularine), an adenosine analog, may exert cytotoxic effect both in vivo and in vitro. We have found earlier¹ that this effect investigated in rat thymocytes was concentration-dependent and strongly related to the presence of adenosine kinase (AK) activity. We hypothesized that AK is rate-limiting for cytotoxicity of PuR also in dividing cells. To test this hypothesis we evaluated in vitro whether there is an enzymatic potential to phosphorylate nucleosides and dephosphorylate nucleotides. Our aim was to check the effect of PuR in COS-7 cells and to verify the role of AK in this process. The other enzymes taking part in nucleotide metabolism are also investigated. It appears that relatively low activities of intra- and extracellular 5’nucleotidases and low specificity of AK being able to convert purine riboside to nucleotide make the pathway through this route plausible. 2. METHODS Cell incubations. Cells were cultured in Dulbecco modified Eagle medium with or without 10% fetal calf serum. PuR and adenosine at concentrations
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