Linked Life Data

7583309

Source:http://linkedlifedata.com/resource/pubmed/id/7583309

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1995-12-14
pubmed:abstractText
The effects of Ca2+ /phospholipid dependent (PKC) phosphorylation on the current amplitudes of alpha 1 and alpha 2 glycine receptors expressed in Xenopus oocytes were examined by whole cell voltage clamp recording. In studies using phorbol esters, PKC phosphorylation has been shown to reduce glycine-induced currents. Endogenous PKC activation by pretreatment with serum, however, enhanced the currents to around 140% in both alpha 1 and alpha 2 glycine receptors. This effect was completely blocked by a specific PKC inhibitor, GF109203X. Instead, treatment with a potent PKC activator, 12-O-tetradecanoylphorbol-13-acetate (TPA) revealed a decrease in glycine-gated channel currents. Thus, the present results demonstrate that glycine receptor phosphorylation mediated by endogenous pathway of PKC activation potentiates glycine-induced currents and phorbol esters may have a direct action on glycine receptor channels independent of PKC activation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-8993
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
687
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
214-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Activation of endogenous protein kinase C enhances currents through alpha 1 and alpha 2 glycine receptor channels.
pubmed:affiliation
Department of Physiology, Kobe university School of Medicine, Japan.
pubmed:publicationType
Journal Article