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      Increased ouabain-sensitive 86Rb+ uptake and sodium and potassium ion-activated adenosine triphosphatase activity in transformed cell lines.

      The Journal of Biological Chemistry
      Adenosine Triphosphatases, metabolism, Animals, Avian Sarcoma Viruses, Binding Sites, Biological Transport, Active, Cell Division, Cell Line, Cell Transformation, Neoplastic, Cells, Cultured, Clone Cells, Cricetinae, Enzyme Activation, drug effects, Kidney, Mice, Mice, Inbred BALB C, Ouabain, pharmacology, Potassium, Protein Binding, Radioisotopes, Rubidium, Simian virus 40, Sodium

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          Abstract

          During the log phase of growth both the active, ouabain-sensitive K+ uptake, measured as 86Rb+, and the sodium and potassium ion-activated ATPase ((Na+ + K+)-ATPase) activity of SV40-transformed 3T3 cells were 2.5-and 5,5-fold higher, respectively, than in untransformed 3T3 cells. A similar higher active K+ uptake was found for Rous sarcoma virus and SV40-transformed baby hamster kidney cells compared with untransformed BHK cells. The active K+ uptake in SV403T3 and normal 3T3 cells decreased when the growth rate of both cell types diminished. Reduction in ouabain-sensitive ATP hydrolysis only occurred later, however, when appreciable decreases in cell viability were seen. Arrhenius plots of the (Na+ + K+)-ATPase activity of SV403T3 cells indicated a discontinuity at 24 degrees, whereas no similar discontinuity was indicated for 3T3 cells. The consequences of elevated K+ transport and (Na+ + K+)-ATPase activity in transformed cells and the possibility that the increased activity might be related to differences inphospholipid fatty acyl chain fluidity are discussed.

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