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Regulation of Passive Potassium Transport of Normal and Transformed 3T3 Mouse Cell Cultures by External Calcium Concentration and Temperature

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Journal J Membr Biol
Date 1981 Jan 1
PMID 6268792
Citations 2
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Abstract

Regulation of passive potassium ion transport by the external calcium concentration and temperature was studied on cell cultures of 3T3 mouse cells and their DNA-virus transformed derivatives. Upon lowering of external calcium concentration, passive potassium efflux generally exhibits a sharp increase at about 0.1 mM. The fraction of calcium-regulated potassium efflux is largely independent of temperature in the cases of the transformed cells, but shows a sharp increase for 3T3 cells upon increasing temperature above 32 degrees C. In the same range of temperature, the 3T3 cells exhibit the phenomenon of high-temperature inactivation of the residual potassium efflux at 1 mM external calcium. At comparable cellular growth densities, the transformed cell lines do not show high-temperature inactivation of "residual" potassium efflux. These results are consistent with the notion of a decisive role of the internal K+ concentration in the cell-density dependent regulation of cell proliferation. In particular, the growth-inhibiting effect of lowering the external Ca2+ concentrations is considered as largely due to a rise of passive K+ efflux and a subsequent decrease of internal K+ concentration. The experimental data on the Ca2+ dependence of passive K+ flux are quantitatively described by a theoretical model based on the constant field relations including negative surface charges on the external face of the membrane, which cooperatively bind Ca2+ ions and may concomitantly undergo a lateral redistribution. The present evidence is consistent with acidic phospholipids as representing these negative surface charges.

Citing Articles

Mechanism, regulation and physiological significance of the loop diuretic-sensitive NaCl/KCl symport system in animal cells.

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K+ efflux in NIH mouse 3T3 cells and transformed derivatives: dependence on extracellular Ca2+ and phorbol esters.

Lubin M Proc Natl Acad Sci U S A. 1988; 85(14):5097-101.

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