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PMID: 1917908 Published · ppublish English Journal Article Review

Calcium-activated potassium channels: regulation by calcium.

Journal of bioenergetics and biomembranes ·Vol. 23 ·No. 4 ·1991-08-00 ·Pages 537-60

McManus OB

Abstract

A wide variety of calcium-activated K channels has been described and can be conveniently separated into three classes based on differences in single-channel conductance, voltage dependence of channel opening, and sensitivity to blockers. Large-conductance calcium-activated K channels typically require micromolar concentrations of calcium to open, and their sensitivity to calcium increases with membrane depolarization, suggesting that they may be involved in repolarization events. Small-conductance calcium-activated K channels are generally more sensitive to calcium at negative membrane potentials, but their sensitivity to calcium is independent of membrane potential, suggesting that they may be involved in regulating membrane properties near the resting potential. Intermediate-conductance calcium-activated K channels are a loosely defined group, where membership is determined because a channel does not fit in either of the other two groups. Within each broad group, variations in calcium sensitivity and single-channel conductance have been observed, suggesting that there may be families of closely related calcium-activated K channels. Kinetic studies of the gating of calcium-activated potassium channels have revealed some basic features of the mechanisms involved in activation of these channels by calcium, including the number of calcium ions participating in channel opening, the number of major conformations of the channels involved in the gating process, and the number of transition pathways between open and closed states. Methods of analysis have been developed that may allow identification of models that give accurate descriptions of the gating of these channels. Although such kinetic models are likely to be oversimplifications of the behavior of a large macromolecule, these models may provide some insight into the mechanisms that control the gating of the channel, and are subject to falsification by new data.

MeSH Terms
Animals Calcium/physiology Humans Potassium Channels/metabolism
Chemicals
Potassium Channels Calcium
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
McManus O B
Department of Membrane Biochemistry and Biophysics, Merck Institute for Therapeutic Research, Rahway, New Jersey 07065.
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Article Info
Journal
Journal of bioenergetics and biomembranes
Abbr.
J Bioenerg Biomembr
ISSN
0145-479X
DOI
10.1007/BF00785810
Published
1991-08-00
Pages
537-60
Language
English
Region
United States
NLM ID
7701859
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00785810 View journal details
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