Linked Life Data

15147300

Source:http://linkedlifedata.com/resource/pubmed/id/15147300

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2004-5-18
pubmed:abstractText
There is growing evidence that E-type voltage dependent Ca(2+) channels (Ca(v)2.3) are involved in triggering and controlling pivotal cellular processes like neurosecretion and long-term potentiation. The mechanism underlying a novel Ca(2+) dependent stimulation of E-type Ca(2+) channels was investigated in the context of the recent finding that influx of Ca(2+) through other voltage dependent Ca(2+) channels is necessary and sufficient to directly activate protein kinase C (PKC). With Ba(2+) as charge carrier through Ca(v)2.3 channel alpha(1) subunits expressed in HEK-293 cells, activation of PKC by low concentrations of phorbol ester augmented peak I(Ba) by approximately 60%. In addition, the non-inactivating fraction of I(Ba) was increased by more than three-fold and recovery from short-term inactivation was accelerated. The effect of phorbol ester on I(Ba) was inhibited by application of the specific PKC inhibitor bisindolylmaleimide I. With Ca(2+) as charge carrier, application of phorbol ester did not change the activity of Ca(v)2.3 currents but they were modified by the PKC inhibitor bisindolylmaleimide I. These results suggest that with Ca(2+) as charge carrier the incoming Ca(2+) can activate PKC, thereby augmenting Ca(2+) influx into the cytosol. No modulation of Ca(v)2.3 channels by PKC was observed when an arginine rich region in the II-III loop of Ca(v)2.3 was eliminated. Receptor independent stimulation of PKC and its interaction with Ca(v)2.3 channels therefore represents an important positive feedback mechanism to decode electrical signals into a variety of cellular functions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0953-816X
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2659-68
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:15147300-1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine, pubmed-meshheading:15147300-Barium, pubmed-meshheading:15147300-Calcium, pubmed-meshheading:15147300-Calcium Channels, pubmed-meshheading:15147300-Cell Line, pubmed-meshheading:15147300-Drug Interactions, pubmed-meshheading:15147300-Embryo, Mammalian, pubmed-meshheading:15147300-Enzyme Inhibitors, pubmed-meshheading:15147300-Humans, pubmed-meshheading:15147300-Indoles, pubmed-meshheading:15147300-Ion Channel Gating, pubmed-meshheading:15147300-Kidney, pubmed-meshheading:15147300-Maleimides, pubmed-meshheading:15147300-Membrane Potentials, pubmed-meshheading:15147300-Patch-Clamp Techniques, pubmed-meshheading:15147300-Phorbol Esters, pubmed-meshheading:15147300-Protein Kinase C, pubmed-meshheading:15147300-Protein Structure, Tertiary, pubmed-meshheading:15147300-Protein Subunits, pubmed-meshheading:15147300-Time Factors, pubmed-meshheading:15147300-Transfection
pubmed:year
2004
pubmed:articleTitle
The cytosolic II-III loop of Cav2.3 provides an essential determinant for the phorbol ester-mediated stimulation of E-type Ca2+ channel activity.
pubmed:affiliation
Institute of Vegetative Physiology, University of Cologne, Germany. udo.kloeckner@medizin.uni-halle.de
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't