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Am J Physiol Cell Physiol 281: C361-C367, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 1, C361-C367, July 2001

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

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

Department of Physiology and Biophysics, University of Iowa, Iowa City, Iowa 52242

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.

potassium channel; calcium activated; splice varient; myometrium


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