Linked Life Data

19336893

Source:http://linkedlifedata.com/resource/pubmed/id/19336893

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2009-4-1
pubmed:abstractText
Kv1.4 channel belongs to the family of voltage-gated potassium channels that mediate transient and rapidly inactivating A-type currents and N-type inactivation. This N-type inactivation can be removed by the deletion of N-terminal domains, which exhibit non-inactivating currents and C-type inactivation. In our previous report, we demonstrated that 20(S)-ginsenoside Rg(3) (Rg(3)), one of the active ingredients of ginseng saponins, inhibits human Kv1.4 (hKv1.4) channel currents through the interaction with amino acids, including Lys (K) residue, which is known as K(+) activation and the extracellular tetraethylammonium (TEA) binding site. In the present study, we examined the effects of Rg(3) on hKv1.4 channel currents without the N-terminal rapid inactivation domain. We constructed hKv1.4Delta2-61 channels by N-terminal deletion of 2-61 amino acid residues. We investigated the effect of Rg(3) on hKv1.4Delta2-61 channel currents. We found that Rg(3) preferentially inhibited non-inactivating outward currents rather than peak outward currents of hKv1.4Delta2-61 channels. The mutation of K531 hKv1.4Delta2-61 to K531Y hKv1.4Delta2-61 and raising of extracellular [K(+)](o) abolished Rg(3) inhibitions on non-inactivating outward currents. Rg(3) treatment increased the C-type inactivation rate, but raising the extracellular [K(+)](o) reversed Rg(3) action. These results provide additional evidence that K531 residue also plays an important role in the Rg(3)-mediated non-inactivating current blockages and in Rg(3)-mediated increase of the C-type inactivation rate in hKv1.4Delta2-61 channels.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0918-6158
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
614-8
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
The effects of ginsenoside Rg(3) on human Kv1.4 channel currents without the N-terminal rapid inactivation domain.
pubmed:affiliation
Department of Physiology, College of Oriental Medicine, Kyung-Hee University, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't