Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1986-10-21
|
| pubmed:abstractText |
In patch-clamp records of K+ ATP channels in an insulin-secreting cell line (RINm5F) inhibition evoked by exposing the internal surface of the membrane to ATP is followed not just by the recovery of K+ ATP channel activity when the ATP is removed but by a marked activation of K+ ATP channels. This phenomenon is not a direct consequence of channel closure as inhibition induced by quinidine and quinine is followed upon the removal of the drug only by the recovery of K+ ATP channel activity and not by post-inhibitory activation. If ATP is applied to the exposed internal surface of a membrane patch when all of its K+ ATP channel have run down subsequent removal of the ATP causes their activation. The magnitude and duration of the reactivation of K+ ATP channels is shown to depend upon both the concentration of ATP and the length of time for which the membrane is exposed to ATP. We therefore have a paradoxical situation in that K+ channels which are inhibited by intracellular ATP require intracellular ATP to retain the ability to open.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0031-6768
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
407
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
238-40
|
| pubmed:dateRevised |
2011-11-17
|
| pubmed:meshHeading | |
| pubmed:year |
1986
|
| pubmed:articleTitle |
ATP maintains ATP-inhibited K+ channels in an operational state.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|