Elliott M S, Crane D L
Old Dominion University, Department of Chemistry and Biochemistry, Norfolk, Virginia 23529.
Biochem Biophys Res Commun. 1990 Aug 31;171(1):393-400. doi: 10.1016/0006-291x(90)91406-i.
Protein kinase C modulates the activity of a highly specific uptake mechanism for queuine in cultured human fibroblasts. Activators of protein kinase C induce an increased uptake rate for the radiolabeled analog of queuine, rQT3. The protein kinase C inhibitors, H-7, staurosporine and sphingosine all induced a dramatic decrease in the uptake rate of rQT3. This suggests that protein kinase C is tied to efficient cellular uptake of queuine. Uptake is prerequisite to the modification of transfer RNA with queuine. Perturbation of queuine-modified transfer RNA levels has been associated with neoplastic transformation, differentiation and growth control.