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A Ca2(+)-activated K+ current in ras-transformed fibroblasts is absent from nontransformed cells

G. RANE of Biological Sciences, Purdue University, West Lafayette, diana 47907 RANE, STANLEY G. A Ca2+-activated rastransformed fibroblasts is absent from nontransformed . Am. J. Physiol. 260 (Cell Physiol. 29): ClO4-C112,1991.-Biochemical similarities between ras protes and the GTP-bdg protes and correlation of ras-ducedcell transformation with altered transmembranecation fluxes dicate that ras protes may act to modulate ion channel activity. To test this idea, whole cell, tight-seal, patch-clamp recordg was usedto compare macroscopics of ras-transformed fibroblasts with s of their nontransformed counterparts. A proment calcium-activated, voltage-dependentpotassium was observed 83-100% of from three separate fibroblast les transformed by two different oncogenic ras alleles, whereasthe same was present at much smaller amplitudes only O-15% of nontransformed . The calciumactivated potassium is blocked by charybdotox and by concentrations of tetraethylammonium above 1 mM, but it is sensitiveto apam. Both normal and ras-transformed have another calcium-activated that is not potassium selective, and, consistent with other studies, normal display a voltage-activated calcium conductance. These results suggest that the mechanisms which ras triggers or matas by cell transformation may volve alterations the number or activity of certa ion channels, particular, a type of calciumactivated potassiumchannel. oncogenes; potassiumchannels (8, 10, 21, 33). These results and earlier http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Cell Physiology The American Physiological Society

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