Linked Life Data

1588923

Source:http://linkedlifedata.com/resource/pubmed/id/1588923

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1992-6-23
pubmed:abstractText
Bath application of micromolar concentrations of forskolin to Xenopus oocytes that express either Torpedo electroplax or mouse muscle nicotinic acetylcholine (ACh) receptors leads to a reduction in the size of the ACh-elicited currents. This inhibition is concentration dependent and rapidly reversible, with full onset and recovery occurring within the exchange time of the recording chamber. Torpedo and mouse ACh receptors exhibit differential sensitivity to forskolin, with the Torpedo receptor showing higher affinity than the mouse receptor, with Ki values of 6.5 microM and 22 microM, respectively. The affinity for forskolin increases with ACh concentration, which rules out the possibility that forskolin acts as a competitive inhibitor. Single-channel analysis using excised patches shows that forskolin has no effect on either the single-channel amplitude or mean open time but, instead, reduces the number of channel openings per unit time, suggesting that forskolin either is a very slow channel blocker or alters receptor gating such that a fraction of the channels enter a state from which they are no longer available to open. Finally, through the use of a series of mouse-Torpedo hybrid ACh receptors, it is shown that the structural features responsible for the observed species difference in the affinity of ACh receptors for forskolin, and thus at least part of the binding site, are located on the gamma subunit.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0026-895X
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
908-13
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Forskolin acts as a noncompetitive inhibitor of nicotinic acetylcholine receptors.
pubmed:affiliation
Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia 19104-6084.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't