The Apamin-Sensitive Ca2+-Dependent K+ Channel: Molecular Properties, Differentiation, Involvement in Muscle Disease, and Endogeneous Ligands in Mammalian Brain

1988 ◽  
pp. 135-145 ◽  
Author(s):  
M. Lazdunski ◽  
G. Romey ◽  
H. Schmid-Antomarchi ◽  
J. F. Renaud ◽  
C. Mourre ◽  
...  
Keyword(s):  
Molecular Properties ◽  
Muscle Disease ◽  
Mammalian Brain ◽  
K Channel

The Apamin-Sensitive Ca2+-Dependent K+ Channel. Molecular Properties, Differentiation, and Endogeneous Ligands in Mammalian Brain

1985 ◽  
pp. 164-171 ◽  
Author(s):  
M. Lazdunski ◽  
M. Fosset ◽  
M. Hugues ◽  
C. Mourre ◽  
J. F. Renaud ◽  
...  
Keyword(s):  
Molecular Properties ◽  
Mammalian Brain ◽  
K Channel

A novel K+ channel with unique localizations in mammalian brain: Molecular cloning and characterization

Neuron ◽  
1992 ◽  
Vol 8 (3) ◽  
pp. 473-481 ◽  
Author(s):  
Paul M. Hwang ◽  
Charles E. Glatt ◽  
David S. Bredt ◽  
Gary Yellen ◽  
Solomon H. Snyder
Keyword(s):  
Molecular Cloning ◽  
Mammalian Brain ◽  
K Channel

Voltage-gated K+ Channel from Mammalian Brain: 3D Structure at 18Å of the Complete (α)4(β)4 Complex

2003 ◽  
Vol 326 (4) ◽  
pp. 1005-1012 ◽  
Author(s):  
Elena V. Orlova ◽  
Marianthi Papakosta ◽  
Frank P. Booy ◽  
Marin van Heel ◽  
J.Oliver Dolly
Keyword(s):  
3D Structure ◽  
Mammalian Brain ◽  
K Channel ◽  
Voltage Gated

Cloning and functional expression of a liver isoform of the small conductance Ca2+-activated K+ channel SK3

2001 ◽  
Vol 280 (4) ◽  
pp. C836-C842 ◽  
Author(s):  
Elisabeth T. Barfod ◽  
Ann L. Moore ◽  
Steven D. Lidofsky
Keyword(s):  
Rat Liver ◽  
Metabolic Stress ◽  
Functional Expression ◽  
Mammalian Brain ◽  
K Channel ◽  
Molecular Characteristics ◽  
Amino Acid Residues ◽  
Sk Channels ◽  
Hek 293 ◽  
Small Conductance

Small conductance Ca2+-activated K+(SK) channels have been cloned from mammalian brain, but little is known about the molecular characteristics of SK channels in nonexcitable tissues. Here, we report the isolation from rat liver of an isoform of SK3. The sequence of the rat liver isoform differs from rat brain SK3 in five amino acid residues in the NH3terminus, where it more closely resembles human brain SK3. SK3 immunoreactivity was detectable in hepatocytes in rat liver and in HTC rat hepatoma cells. Human embryonic kidney (HEK-293) cells transfected with liver SK3 expressed 10 pS K+ channels that were Ca2+ dependent (EC50 630 nM) and were blocked by the SK channel inhibitor apamin (IC50 0.6 nM); whole cell SK3 currents inactivated at membrane potentials more positive than −40 mV. Notably, the Ca2+ dependence, apamin sensitivity, and voltage-dependent inactivation of SK3 are strikingly similar to the properties of hepatocellular and biliary epithelial SK channels evoked by metabolic stress. These observations raise the possibility that SK3 channels influence membrane K+ permeability in hepatobiliary cells during liver injury.

scholarly journals mShal, a subfamily of A-type K+ channel cloned from mammalian brain.

1991 ◽  
Vol 88 (10) ◽  
pp. 4386-4390 ◽  
Author(s):  
M. D. Pak ◽  
K. Baker ◽  
M. Covarrubias ◽  
A. Butler ◽  
A. Ratcliffe ◽  
...  
Keyword(s):  
Mammalian Brain ◽  
K Channel ◽  
Type K

scholarly journals Immunolocalization of the Ca2+-activated K+channel Slo1 in axons and nerve terminals of mammalian brain and cultured neurons

2006 ◽  
Vol 496 (3) ◽  
pp. 289-302 ◽  
Author(s):  
Hiroaki Misonou ◽  
Milena Menegola ◽  
Lynn Buchwalder ◽  
Eunice W. Park ◽  
Andrea Meredith ◽  
...  
Keyword(s):  
Mammalian Brain ◽  
K Channel ◽  
Nerve Terminals ◽  
Cultured Neurons

scholarly journals Kv2.1 mediates spatial and functional coupling of L-type calcium channels and ryanodine receptors in mammalian neurons

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Nicholas C Vierra ◽  
Michael Kirmiz ◽  
Deborah van der List ◽  
L Fernando Santana ◽  
James S Trimmer
Keyword(s):  
Ryanodine Receptors ◽  
Spatial Proximity ◽  
Mammalian Brain ◽  
K Channel ◽  
Functional Coupling ◽  
Brain Neurons ◽  
Close Spatial Proximity ◽  
Unique Mechanism ◽  
Ca2 Channels

The voltage-gated K+ channel Kv2.1 serves a major structural role in the soma and proximal dendrites of mammalian brain neurons, tethering the plasma membrane (PM) to endoplasmic reticulum (ER). Although Kv2.1 clustering at neuronal ER-PM junctions (EPJs) is tightly regulated and highly conserved, its function remains unclear. By identifying and evaluating proteins in close spatial proximity to Kv2.1-containing EPJs, we discovered that a significant role of Kv2.1 at EPJs is to promote the clustering and functional coupling of PM L-type Ca2+ channels (LTCCs) to ryanodine receptor (RyR) ER Ca2+ release channels. Kv2.1 clustering also unexpectedly enhanced LTCC opening at polarized membrane potentials. This enabled Kv2.1-LTCC-RyR triads to generate localized Ca2+ release events (i.e., Ca2+ sparks) independently of action potentials. Together, these findings uncover a novel mode of LTCC regulation and establish a unique mechanism whereby Kv2.1-associated EPJs provide a molecular platform for localized somatodendritic Ca2+ signals in mammalian brain neurons.

scholarly journals Molecular properties of the apamin-binding component of the Ca2+-dependent K+ channel Radiation-inactivation, affinity labelling and solubilization

1984 ◽  
Vol 142 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Heidy SCHMID-ANTOMARCHI ◽  
Michel HUGUES ◽  
Robert NORMAN ◽  
Clive ELLORY ◽  
Marc BORSOTTO ◽  
...  
Keyword(s):  
Molecular Properties ◽  
K Channel ◽  
Radiation Inactivation ◽  
Affinity Labelling ◽  
Binding Component

scholarly journals ATP-sensitive K+ channel activation provides transient protection to the anoxic turtle brain

1998 ◽  
Vol 275 (6) ◽  
pp. R2023-R2027 ◽  
Author(s):  
Marta Pék-Scott ◽  
Peter L. Lutz
Keyword(s):  
Channel Blocker ◽  
Protective Role ◽  
Initial Energy ◽  
Mammalian Brain ◽  
K Channel ◽  
Protective Function ◽  
Channel Arrest ◽  
Major Route ◽  
Butanedione Monoxime ◽  
Energy Failure

There is wide speculation that ATP-sensitive K+(KATP) channels serve a protective function in the mammalian brain, being activated during periods of energy failure. The aim of the present study was to determine if KATP channels also have a protective role in the anoxia-tolerant turtle brain. After ouabain administration, rates of change in extracellular K+ were measured in the telencephalon of normoxic and anoxic turtles ( Trachemys scripta). The rate of K+ efflux was reduced by 50% within 1 h of anoxia and by 70% at 2 h of anoxia, and no further decrease was seen at 4 h of anoxia. The addition of the KATP channel blocker glibenclamide or 2,3-butanedione monoxime prevented the anoxia-induced decrease in K+ efflux during the first hour of anoxia, but the effect of these blockers was diminished at 2 h of anoxia and was not seen after 4 h of anoxia. This pattern of change in KATP channel blocker sensitivity can be related to a previously established temporary fall and subsequent recovery of tissue ATP during early anoxia. We suggest that activated KATP channels are involved in the downregulation of membrane ion permeability (channel arrest) during the initial energy crisis period but are switched off when the full anoxic state is established and tissue ATP levels have been restored. We also found that, in contrast to those in mammals, KATP channels are not a major route for K+ efflux in the energy-depleted turtle brain.

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