Sequence and functional expression in Xenopus oocytes of a human insulinoma and islet potassium channel
- Univ. of Chicago, IL (United States)
Regulation of insulin secretion involves the coordinated control of ion channels in the {beta}-cell membrane. The authors have isolated and characterized cDNA and genomic clones encoding a voltage-dependent K{sup +} channel isoform expressed in human islets and in a human insulinoma. This K{sup +} channel isoform, designated hPCN1, with a deduced amino acid sequence of 613 residues is related to the Shaker family of Drosophila K{sup +} channels. hPCN1 is homologous to two other human K{sup +} channel isoforms. They have isolated, hPCN2 and hPCN3, with 55% and 65% amino acid sequence identity, respectively. The electrophysiological characteristics of hPCN1 were determined after microinjuection of synthetic RNA into Xenopus oocytes. Two-microelectrode voltage-clamp recordings of oocytes injected with hPCN1 RNA revealed a voltage-dependent outward K{sup +} current that inactivated slowly with time. Outward currents were inhibited by 4-aminopyridine with a K{sub i} less that 0.01 mM and were relatively insensitive to tetraethylammonium ion or Ba{sup 2+}. A delayed rectifier K{sup +} channel such as hPCN1 could restore the resting membrane potential of {beta} cells after depolarization and thereby contribute to the regulation of insulin secretion.
- OSTI ID:
- 5030939
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 88:1; ISSN 0027-8424
- Country of Publication:
- United States
- Language:
- English
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GENE AMPLIFICATION
OOCYTES
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PYRIDINES
ANIMALS
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LIGHT NUCLEI
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550201* - Biochemistry- Tracer Techniques