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Structural requirements for O2 sensing by the human tandem-P domain channel, hTREK1

Miller, P., Kemp, Paul J. and Peers, C. 2005. Structural requirements for O2 sensing by the human tandem-P domain channel, hTREK1. Biochemical and Biophysical Research Communications 331 (4) , pp. 1253-1256. 10.1016/j.bbrc.2005.04.042

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Abstract

TREK1 is a member of the tandem-P domain K+ channel family which is expressed almost exclusively in the nervous system. It is modulated by a number of important factors including arachidonic acid and cell swelling. Since both factors are associated with brain ischemia, it has been suggested that activation of TREK1 may confer neuroprotection. However, it has been reported that the stably expressed human homologue of TREK1 is inhibited by hypoxia, calling into question its neuroprotective role in ischemia. Here, using transient transfection of HEK 293 cells with several hTREK1 mutations and whole-cell patch-clamp, we show that: hypoxic inhibition: (a) requires the C-terminal domain of the channel; (b) does not involve redox modulation of the C-terminal domain cysteine residues C365 and C399; and (c) is critically dependent on the glutamate residue at position 306. These data suggest strongly that neuroprotection is unlikely to be provided by this channel in low O2 environments and continue to cast a shadow of doubt over the precise role that TREK may have during hypoxic episodes.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: Elsevier
ISSN: 0006-291X
Last Modified: 04 Jun 2017 06:39
URI: http://orca-mwe.cf.ac.uk/id/eprint/63407

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