Abstract
Large conductance Ca2+-activated K+ channel was identified and studied in excised inside-out membrane patches of freshly dispersed smooth muscle cells from rabbit gastric antrum. The current-voltage relationship of the single channel was linear from -80 to +80 mV of pipette voltage in which single channel conductance was 249±17.8 pS (n=19) in symmetrical concentration of K+ (145mM) across the patch. Activity of the channel (NPo) depended not only on cytoplasmic calcium concentration but also on membrane potential. MgATP increased NPo in a dose-dependent manner and Mg2+ was prerequisite for the effect. Okadaic acid (l00nM), inhibitor of protein phosphatases, increased NPo further in the presence of MgATP. Therefore, it would be concluded that activity of the calcium-activated K+ channel in gastric smooth muscle cells was controlled by phosphorylation state of the channel protein and the state is further modulated by membrane-delimited protein kinase and protein phosphatase activities.
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Lee, M.Y., Bang, H.W., Lim, I.J. et al. Modulation of large conductance calcium-activated K+ channel by membrane-delimited protein kinase and phosphatase activities. Pflugers Arch. 429, 150–152 (1994). https://doi.org/10.1007/BF02584044
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DOI: https://doi.org/10.1007/BF02584044