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Calcium-Activated Potassium Channels Expressed from Cloned Complementary DNAs

Tipo de material: TextoTextoSeries ; Neuron, 9(2), p.209-216, 1992Trabajos contenidos:
  • Adelman, J.P
  • Shen, K.Z
  • Kavanaugh, M.P
  • Warren, R.A
  • Wu, Y.N
  • Lagrutta, A
  • Bond, C.T
  • Bond, C.T
Recursos en línea: Resumen: Calcium-activated potassium channels were expressed in Xenopus oocytes by injection of RNA transcribed in vitro from complementary DNAs derived from the s/o locus of Drosophila melanogaster. Many cDNAs were found that encode closely related proteinsof about 1200 aa. The predicted sequences of these proteins differ by thesubstitution of blocksof aminoacids at five identified positions within the putative intracellular region between residues 327 and 797. Excised inside-out membrane patches showed potassium channel openings only with micromolar calcium present at the cytoplasmic side; activity increased steeply both with depolarization and with increasing calcium concentration. The singlechannel conductance was 126 pS with symmetrical potassium concentrations. The mean open time of the channels was clearly different for channels having different subsituent blocks of amino acids. The results suggest that alternative splicing gives rise to a large family of functionally diverse, calcium-activated potassium channels.
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Calcium-activated potassium channels were expressed in Xenopus oocytes by injection of RNA transcribed in vitro from complementary DNAs derived from the s/o locus of Drosophila melanogaster. Many cDNAs were found that encode closely related proteinsof about 1200 aa. The predicted sequences of these proteins differ by thesubstitution of blocksof aminoacids at five identified positions within the putative intracellular region between residues 327 and 797. Excised inside-out membrane patches showed potassium channel openings only with micromolar calcium present at the cytoplasmic side; activity increased steeply both with depolarization and with increasing calcium concentration. The singlechannel conductance was 126 pS with symmetrical potassium concentrations. The mean open time of the channels was clearly different for channels having different subsituent blocks of amino acids. The results suggest that alternative splicing gives rise to a large family of functionally diverse, calcium-activated potassium channels.

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