Linked Life Data

8786695

Source:http://linkedlifedata.com/resource/pubmed/id/8786695

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1996-9-20
pubmed:abstractText
The modulation of ATP-sensitive K+ channel (KATP) activity by specific phosphorylation or dephosphorylation of tyrosine and serine/threonine residues was examined in rat ventricular myocytes using the inside-out patch configuration of the patch clamp technique. The run-down process was suppressed by okadaic acid but accelerated by sodium orthovanadate. After run-down of the channels, the ATP-induced reactivation was blocked by H-7, but enhanced by genistein. The channel activity was decreased by protein phosphatase 2A. However, the activity of partially run-down channels was increased by protein tyrosine phosphatase 1B. Our results suggest that KATP channel activity can be inhibited by phosphorylation of tyrosine residues and stimulated by phosphorylation of serine/threonine residues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0024-3205
pubmed:author
pubmed:issnType
Print
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
897-904
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Reciprocal modulation of ATP-sensitive K+ channel activity in rat ventricular myocytes by phosphorylation of tyrosine and serine/threonine residues.
pubmed:affiliation
Department of Pharmacology, Chonbuk National University Medical School, Chonju, South Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't