Volume 60, Issue 3 pp. 1175-1178
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Stable Expression and Regulation of a Rat Brain K+ Channel

Stuart D. Critz

Corresponding Author

Stuart D. Critz

Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, Texas, U.S.A.

Address correspondence and reprint requests to Dr. S. D. Critz at Department of Molecular Physiology and Biophysics, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, U.S.A.Search for more papers by this author
Barbara A. Wible

Barbara A. Wible

Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, Texas, U.S.A.

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Hector S. Lopez

Hector S. Lopez

Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, Texas, U.S.A.

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Arthur M. Brown

Arthur M. Brown

Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, Texas, U.S.A.

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First published: March 1993
Citations: 54

Abstract

Abstract: The Shaw-type K+ channel Kv3.1 was stably transfected in human embryonic kidney cells. Voltage dependence of activation, K+ permeability, sensitivity to external tetraethylammonium, and unitary conductance were similar to Kv 3.1 channels expressed transiently in Xenopus oocytes. Kv 3.1 channels appear to be regulated because the protein kinase C activator phorbol 12,13-dibutyrate decreased Kv 3.1 currents. Based on these results, we find that the stable expression of voltage-gated K+ channels in human embryonic kidney cells appears to be well suited for analysis of both biophysical and biochemical regulatory processes.

Abbreviations

  • DMSO
  • dimethyl sulfoxide
  • PDBu
  • phorbol 12,13-dibutyrate
  • PKC
  • protein kinase C
  • TEA
  • tetraethylammonium
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