scholarly journals Targeting two-pore domain K+channels TREK-1 and TASK-3 for the treatment of depression: a new therapeutic concept

2014 ◽  
Vol 172 (3) ◽  
pp. 771-784 ◽  
Author(s):  
M Borsotto ◽  
J Veyssiere ◽  
H Moha ou Maati ◽  
C Devader ◽  
J Mazella ◽  
...  
Keyword(s):  
Therapeutic Concept ◽  
K Channels ◽  
Treatment Of Depression ◽  
Pore Domain ◽  
And Task

scholarly journals Study Of Gating Mechanism Of Two Pore Domain K+ Channels Gated By Extracellular Alkalinization: TASK-2 And TASK-3

2009 ◽  
Vol 96 (3) ◽  
pp. 668a
Author(s):  
Fernando D. Gonzalez-Nilo ◽  
Christophe Chipot ◽  
Alex Digenova ◽  
Cristell Navarro ◽  
Wendy Gonzalez-Diaz ◽  
...  
Keyword(s):  
K Channels ◽  
Gating Mechanism ◽  
Pore Domain ◽  
And Task

Gating of two-pore domain K+ channels by extracellular pH

2006 ◽  
Vol 34 (5) ◽  
pp. 899-902 ◽  
Author(s):  
M.I. Niemeyer ◽  
F.D. González-Nilo ◽  
L. Zúñiga ◽  
W. González ◽  
L.P. Cid ◽  
...  
Keyword(s):  
Extracellular Ph ◽  
Selectivity Filter ◽  
Open Probability ◽  
K Channels ◽  
Task Channels ◽  
Pore Mouth ◽  
Inactivation Gating ◽  
Opening And Closing ◽  
Pore Domain ◽  
And Task

Potassium channels have a conserved selectivity filter that is important in determining which ions are conducted and at what rate. Although K+ channels of different conductance characteristics are known, they differ more widely in the way their opening and closing, the gating, is governed. TASK and TALK subfamily proteins are two-pore region KCNK K+ channels gated open by extracellular pH. We discuss the mechanism for this gating in terms of electrostatic effects on the pore changing the occupancy and open probability of the channels in a way reminiscent of C-type inactivation gating at the selectivity filter. Essential to this proposed mechanism is the replacement of two highly conserved aspartate residues at the pore mouth by asparagine or histidine residues in the TALK and TASK channels.

scholarly journals Expression of TASK and TREK, two-pore domain K+ channels, in human myometrium

Reproduction ◽  
2005 ◽  
Vol 129 (4) ◽  
pp. 525-530 ◽  
Author(s):  
Xilian Bai ◽  
George J Bugg ◽  
Susan L Greenwood ◽  
Jocelyn D Glazier ◽  
Colin P Sibley ◽  
...  
Keyword(s):  
Membrane Potential ◽  
Pregnant Women ◽  
Human Myometrium ◽  
Rt Pcr ◽  
Excitable Cells ◽  
K Channels ◽  
Myometrial Cells ◽  
Channel Proteins ◽  
A Site ◽  
Pore Domain

Two-pore domain K+channels are an emerging family of K+channels that may contribute to setting membrane potential in both electrically excitable and non-excitable cells and, as such, influence cellular function. The human uteroplacental unit contains both excitable (e.g. myometrial) and non-excitable cells, whose function depends upon the activity of K+channels. We have therefore investigated the expression of two members of this family, TWIK (two-pore domain weak inward rectifying K+channel)-related acid-sensitive K+channel (TASK) and TWIK-related K+channel (TREK) in human myometrium. Using RT-PCR the mRNA expression of TASK and TREK isoforms was examined in myometrial tissue from pregnant women. mRNAs encoding TASK1, 4 and 5 and TREK1 were detected whereas weak or no signals were observed for TASK2, TASK3 and TREK2. Western blotting for TASK1 gave two bands of approximately 44 and 65 kDa, whereas TREK1 gave bands of approximately 59 and 90 kDa in myometrium from pregnant women. TASK1 and TREK1 immunofluorescence was prominent in intracellular and plasmalemmal locations within myometrial cells. Therefore, we conclude that the human myometrium is a site of expression for the two-pore domain K+channel proteins TASK1 and TREK1.

Uterine Excitability and Ion Channels and Their Changes with Gestation and Hormonal Environment

2020 ◽  
Vol 83 (1) ◽  
Author(s):  
Susan Wray ◽  
Sarah Arrowsmith
Keyword(s):  
Ion Channels ◽  
Inward Rectifier ◽  
Cation Channels ◽  
Annual Review ◽  
Publication Date ◽  
K Channels ◽  
Voltage Gated ◽  
New Findings ◽  
Voltage Dependent ◽  
Pore Domain

We address advances in the understanding of myometrial physiology, focusing on excitation and the effects of gestation on ion channels and their relevance to labor. This review moves through pioneering studies to exciting new findings. We begin with the myometrium and its myocytes and describe how excitation might initiate and spread in this myogenic smooth muscle. We then review each of the ion channels in the myometrium: L- and T-type Ca2+ channels, KATP (Kir6) channels, voltage-dependent K channels (Kv4, Kv7, and Kv11), twin-pore domain K channels (TASK, TREK), inward rectifier Kir7.1, Ca2+-activated K+ channels with large (KCNMA1, Slo1), small (KCNN1–3), and intermediate (KCNN4) conductance, Na-activated K channels (Slo2), voltage-gated (SCN) Na+ and Na+ leak channels, nonselective (NALCN) channels, the Na K-ATPase, and hyperpolarization-activated cation channels. We finish by assessing how three key hormones— oxytocin, estrogen, and progesterone—modulate and integrate excitability throughout gestation. Expected final online publication date for the Annual Review of Physiology, Volume 83 is February 10, 2021. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

Structure and function of two-pore-domain K channels: contributions from genetic model organisms

2005 ◽  
Vol 26 (7) ◽  
pp. 361-367 ◽  
Author(s):  
S BUCKINGHAM ◽  
J KIDD ◽  
R LAW ◽  
C FRANKS ◽  
D SATTELLE
Keyword(s):  
Genetic Model ◽  
Structure And Function ◽  
Model Organisms ◽  
K Channels ◽  
And Function ◽  
Pore Domain

scholarly journals Inward Rectification of TWIK-1 Two-Pore Domain K+ Channels

2013 ◽  
Vol 104 (2) ◽  
pp. 132a
Author(s):  
Liqun Ma ◽  
Haijun Chen
Keyword(s):  
Inward Rectification ◽  
K Channels ◽  
Pore Domain
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