IndraLab

Statements



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"We report here that CO reliably and repeatedly activates Slo1 BK channels in excised membrane patches in the absence of Ca (2+) in a voltage-sensor-independent manner."

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"Because of the rapid reversibility of CO and cyanide binding, they proposed that CO activates the Slo1 BK Ca channel by binding to a transition metal cluster 62."

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"What is noteworthy is that CO, a gaseous messenger akin to nitric oxide (NO), increases the BK channel activity in different systems (Perez-Garcia et al., 2000; Wang and Wu, 1997; Xi et al., 2004)."

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"In contrast, CO repeatedly stimulates the human Slo1 BK Ca channel opening possibly by binding to an unknown iron site because cyanide prohibits this heme independent CO stimulation."

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"Heme binding strongly inhibits the channel under hypoxic conditions, whereas under normoxic conditions, carbon monoxide (CO), which is generated by heme oxygenase-2 (HO-2) during heme degradation, activates the BK channel (Jaggar et al., 2005)."

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"Their data corroborate previous findings of Wang et al. (Wang et al., 1997b) who showed that the effect of gaseous CO on K channels was not mediated by cGMP, but contradict the findings of De Backer et al. (De Backer and Lefebvre, 2007) in which CO mediated relaxation in circular smooth muscle strips of the murine gastric fundus and jejunum was sGC and BK channel dependent."

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"Heme binding strongly inhibits the channel under hypoxic conditions, whereas under normoxic conditions, carbon monoxide (CO), which is generated by heme oxygenase-2 (HO-2) during heme degradation, activates the BK channel (Jaggar et al., 2005)."

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"Carbon monoxide (CO), which is another endogenous like NO, can increase native BK channel activity."

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"Carbon monoxide (CO), which is another endogenous like NO, can increase native BK channel activity."

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"Thus CO stimulates the BK channel activity even when the concentrations of these free multivalent cations are negligible."

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"XREF_BIBR Therefore, the conformational changes in the BK channel protein induced by CO may resemble those by Ca 2+ and H+; XREF_BIBR, XREF_BIBR, XREF_BIBR CO increases the gate open probability without requiring activation of the VSDs."

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"CO enhances maxi K channel activity in glomus cells."

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"CO was found to enhance maxiK channel activity directly (as also shown in type I cells; Riesco-Fagundo et al., 2001 ), and removal of any of the substrates of HO-2 (including O 2 ) markedly suppressed[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"CO activates the BK channel [16] and TREK1 channel [17] and inhibits the Kv2.1 channel [11] and the inward rectifier K channel [18]."

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"Thus, it appeared that tonic HO-2 production of CO caused basal maxiK activity to be high, and when O 2 was decreased, channel activity was dramatically suppressed."

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"It has been further suggested that CO, along with NO, can also directly augment BK channel activity when applied at sufficiently-high concentrations."

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"Furthermore, CO was able to mimic the effects of HO-2 substrate provision and augment maxiK channel activity several-fold."

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"Thus the role of maxiK channel activation by CO as a physiological means by which CO acts as an inhibitory gasotransmitter remain to be resolved."

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"Heme-oxygenase-2 (3b), which is tightly associated with cell membrane BK channels (4b), uses O 2 as a substrate to produce carbon monoxide (CO), which enhances BK channel open probability during normoxia."

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"Heme-oxygenase-2 (3b), which is tightly associated with cell membrane BK channels (4b), uses O 2 as a substrate to produce carbon monoxide (CO), which enhances BK channel open probability during normoxia."