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rdf:type |
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lifeskim:mentions |
umls-concept:C0007765,
umls-concept:C0010453,
umls-concept:C0030685,
umls-concept:C0033634,
umls-concept:C0034693,
umls-concept:C0034721,
umls-concept:C0391871,
umls-concept:C0439799,
umls-concept:C0596630,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1707723,
umls-concept:C1963578
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pubmed:issue |
1
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pubmed:dateCreated |
1999-4-1
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pubmed:abstractText |
The role of protein kinase C (PKC) in the control of neurotransmitter release from cultured rat cerebellar granule cells was investigated. Release of preloaded [3H]-D-aspartate which is incorporated into synaptic vesicles in this preparation was evoked by electrical field stimulation or elevated KCl. PKC activation by phorbol esters resulted in a large facilitation of field-evoked Ca(2+)-dependent [3H]-D-aspartate release and a lesser enhancement of KCl-stimulated release. Inhibition of PKC by Ro 31-8220 or staurosporine virtually abolished field-evoked release but had no effect on KCl-evoked release. Field-evoked, but not KCl-evoked, synaptic vesicle exocytosis monitored by the fluorescent vesicle probe FM2-10 was inhibited by staurosporine. PKC was not directly modulating neurite Ca2+ channels coupled to release, as Ro 31-8220 did not inhibit these channels. Activation or inhibition of PKC modulated field-evoked plasma membrane depolarization, but had no effect on KCl-evoked depolarization, consistent with a regulation of Na+ or K+ channels activated by field stimulation. No modulation of field-evoked neurite Na+ influx was seen using phorbol esters. Phorbol ester-induced facilitation of field-evoked [3H]-D-aspartate release and neurite Ca2+ entry was non-additive with that produced by the specific K+ channel antagonist dendrotoxin-1, suggesting that PKC modulates transmitter release from field-stimulated cerebellar granule cells by inhibiting a dendrotoxin-1-sensitive K+ channel.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Elapid Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/FM2 10,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Macrolides,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neurotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Phorbol Esters,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proton-Translocating ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridinium Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Quaternary Ammonium Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Tetanus Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium,
http://linkedlifedata.com/resource/pubmed/chemical/bafilomycin A1,
http://linkedlifedata.com/resource/pubmed/chemical/dendrotoxin,
http://linkedlifedata.com/resource/pubmed/chemical/myristoylated alanine-rich C...
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0953-816X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
101-9
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9987015-Animals,
pubmed-meshheading:9987015-Anti-Bacterial Agents,
pubmed-meshheading:9987015-Aspartic Acid,
pubmed-meshheading:9987015-Calcium,
pubmed-meshheading:9987015-Cell Membrane,
pubmed-meshheading:9987015-Cerebellum,
pubmed-meshheading:9987015-Elapid Venoms,
pubmed-meshheading:9987015-Electric Stimulation,
pubmed-meshheading:9987015-Electrophysiology,
pubmed-meshheading:9987015-Enzyme Inhibitors,
pubmed-meshheading:9987015-Exocytosis,
pubmed-meshheading:9987015-Fluorescent Dyes,
pubmed-meshheading:9987015-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:9987015-Macrolides,
pubmed-meshheading:9987015-Membrane Potentials,
pubmed-meshheading:9987015-Membrane Proteins,
pubmed-meshheading:9987015-Neurites,
pubmed-meshheading:9987015-Neurotoxins,
pubmed-meshheading:9987015-Phorbol Esters,
pubmed-meshheading:9987015-Potassium Channels,
pubmed-meshheading:9987015-Protein Kinase C,
pubmed-meshheading:9987015-Proteins,
pubmed-meshheading:9987015-Proton-Translocating ATPases,
pubmed-meshheading:9987015-Pyridinium Compounds,
pubmed-meshheading:9987015-Quaternary Ammonium Compounds,
pubmed-meshheading:9987015-Rats,
pubmed-meshheading:9987015-Rats, Wistar,
pubmed-meshheading:9987015-Synaptic Transmission,
pubmed-meshheading:9987015-Synaptic Vesicles,
pubmed-meshheading:9987015-Tetanus Toxin,
pubmed-meshheading:9987015-Tritium
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pubmed:year |
1999
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pubmed:articleTitle |
Protein kinase C modulates field-evoked transmitter release from cultured rat cerebellar granule cells via a dendrotoxin-sensitive K+ channel.
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pubmed:affiliation |
Department of Pharmacology and Neuroscience, Ninewells Medical School, University of Dundee, UK. mcousin@cmri.usyd.edu.au
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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