Characterization of a novel 132-bp exon of the human maxi-K channel

Victoria P. Korovkina, Daniel J. Fergus, Amanda J. Holdiman, Sarah K. England

Research output: Contribution to journalArticle

27 Scopus citations

Abstract

The large-conductance Ca2+-activated voltage-dependent K+ channel (maxi-K channel) induces a significant repolarizing current that buffers cell excitability. This channel can derive its diversity by alternative splicing of its transcript-producing isoforms that differ in their sensitivity to voltage and intracellular Ca2+. We have identified a novel 132-bp exon of the maxi-K channel from human myometrial cells that encodes 44 amino acids within the first intracellular loop of the channel protein. Distribution analysis reveals that this exon is expressed predominantly in human smooth muscle tissues with the highest abundance in the uterus and aorta and resembles the previously reported distribution of the total maxi-K channel transcript. Single-channel K+ current measurements in fibroblasts transfected with the maxi-K channel containing this novel 132-bp exon demonstrate that the presence of this insert attenuates the sensitivity to voltage and intracellular Ca2+. Alternative splicing to introduce this 132-bp exon into the maxi-K channel may elicit another mode to modulate cell excitability.

Original languageEnglish
Pages (from-to)C361-C367
JournalAmerican Journal of Physiology - Cell Physiology
Volume281
Issue number1 50-1
DOIs
StatePublished - Jan 1 2001
Externally publishedYes

Keywords

  • Calcium activated
  • Myometrium
  • Potassium channel
  • Splice varient

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