PMID- 20835844
OWN - NLM
STAT- MEDLINE
DCOM- 20110222
LR  - 20211020
IS  - 1567-2387 (Electronic)
IS  - 1567-2379 (Linking)
VI  - 41
IP  - 6
DP  - 2010 Dec
TI  - The two-pore domain K+ channel TASK-1 is closely associated with brain barriers 
      and meninges.
PG  - 315-23
LID - 10.1007/s10735-010-9293-3 [doi]
AB  - Impairment of the blood-brain barrier (BBB), the blood-cerebrospinal fluid (CSF) 
      barrier and brain-CSF barrier has been implicated in neuropathology of several 
      brain disorders, such as amyotrophic lateral sclerosis, cerebral edema, multiple 
      sclerosis, neural inflammation, ischemia and stroke. Two-pore domain weakly 
      inward rectifying K+ channel (TWIK)-related acid-sensitive potassium (TASK)-1 
      channels (K2p3.1; KCNK3) are among the targets that contribute to the development 
      of these pathologies. For example TASK-1 activity is inhibited by acidification, 
      ischemia, hypoxia and several signaling molecules released under pathologic 
      conditions. We have used immuno-histochemistry to examine the distribution of the 
      TASK-1 protein in structures associated with the BBB, blood-CSF barrier, 
      brain-CSF barrier, and in the meninges of adult rat. Dense TASK-1 
      immuno-reactivity (TASK-1-IR) was observed in ependymal cells lining the fourth 
      ventricle at the brain-CSF interface, in glial cells that ensheath the walls of 
      blood vessels at the glio-vascular interface, and in the meninges. In these 
      structures, TASK-1-IR often co-localized with glial fibrillary associated protein 
      (GFAP) or vimentin. This study provides anatomical evidence for localization of 
      TASK-1 K+ channels in cells that segregate distinct fluid compartments within and 
      surrounding the brain. We suggest that TASK-1 channels, in coordination with 
      other ion channels (e.g., aquaporins and chloride channels) and transporters 
      (e.g., Na+-K+-ATPase and Na+-K+-2Cl(-) and by virtue of its heterogeneous 
      distribution, may differentially contribute to the varying levels of K+ vital for 
      cellular function in these compartments. Our findings are likely to be relevant 
      to recently reported roles of TASK-1 in cerebral ischemia, stroke and 
      inflammatory brain disorders.
FAU - Kanjhan, Refik
AU  - Kanjhan R
AD  - School of Biomedical Sciences, University of Queensland, Brisbane, QLD 4072, 
      Australia. r.kanjhan@uq.edu.au
FAU - Pow, David V
AU  - Pow DV
FAU - Noakes, Peter G
AU  - Noakes PG
FAU - Bellingham, Mark C
AU  - Bellingham MC
LA  - eng
PT  - Journal Article
DEP - 20100911
PL  - Netherlands
TA  - J Mol Histol
JT  - Journal of molecular histology
JID - 101193653
RN  - 0 (Aquaporins)
RN  - 0 (Chloride Channels)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Potassium Channels, Tandem Pore Domain)
RN  - 0 (Vimentin)
RN  - 1HQ3YCN4GS (potassium channel subfamily K member 3)
RN  - RWP5GA015D (Potassium)
SB  - IM
MH  - Animals
MH  - Aquaporins/metabolism
MH  - Blood-Brain Barrier/*metabolism
MH  - Cerebrospinal Fluid/metabolism
MH  - Chloride Channels/metabolism
MH  - Homeostasis/physiology
MH  - Immunohistochemistry
MH  - Meninges/*metabolism
MH  - Nerve Tissue Proteins/metabolism
MH  - Potassium/metabolism
MH  - Potassium Channels, Tandem Pore Domain/genetics/*metabolism
MH  - Rats
MH  - Rats, Wistar
MH  - Vimentin/metabolism
EDAT- 2010/09/14 06:00
MHDA- 2011/02/23 06:00
CRDT- 2010/09/14 06:00
PHST- 2010/07/19 00:00 [received]
PHST- 2010/08/26 00:00 [accepted]
PHST- 2010/09/14 06:00 [entrez]
PHST- 2010/09/14 06:00 [pubmed]
PHST- 2011/02/23 06:00 [medline]
AID - 10.1007/s10735-010-9293-3 [doi]
PST - ppublish
SO  - J Mol Histol. 2010 Dec;41(6):315-23. doi: 10.1007/s10735-010-9293-3. Epub 2010 
      Sep 11.