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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2-3
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pubmed:dateCreated |
1999-3-25
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pubmed:abstractText |
The involvement of the protein kinase C substrate, B-50 (GAP-43), in the release of glutamate from small clear-cored vesicles in streptolysin-O-permeated synaptosomes was studied by using anti-B-50 antibodies. Glutamate release was induced from endogenous as well as 3H-labelled pools in a [Ca(2+)]-dependent manner. This Ca(2+)-induced release was partially ATP dependent and blocked by the light-chain fragment of tetanus toxin, demonstrating its vesicular nature. Comparison of the effects of anti-B-50 antibodies on glutamate and noradrenaline release from permeated synaptosomes revealed two major differences. Firstly, Ca(2+)-induced glutamate release was decreased only partially by anti-B-50 antibodies, whereas Ca(2+)-induced noradrenaline release was inhibited almost completely. Secondly, anti-B-50 antibodies significantly reduced basal glutamate release, but did not affect basal noradrenaline release. In view of the differences in exocytotic mechanisms of small clear-cored vesicles and large dense-cored vesicles, these data indicate that B-50 is important in the regulation of exocytosis of both types of neurotransmitters, probably at stages of vesicle recycling and/or vesicle recruitment, rather than in the Ca(2+)-induced fusion step.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/GAP-43 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Norepinephrine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Streptolysins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
|
pubmed:issn |
0014-2999
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
18
|
pubmed:volume |
363
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
229-40
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9881594-Adenosine Triphosphate,
pubmed-meshheading:9881594-Animals,
pubmed-meshheading:9881594-Antibodies, Monoclonal,
pubmed-meshheading:9881594-Calcium,
pubmed-meshheading:9881594-Enzyme Inhibitors,
pubmed-meshheading:9881594-Exocytosis,
pubmed-meshheading:9881594-GAP-43 Protein,
pubmed-meshheading:9881594-Glutamic Acid,
pubmed-meshheading:9881594-Intracellular Membranes,
pubmed-meshheading:9881594-Male,
pubmed-meshheading:9881594-Norepinephrine,
pubmed-meshheading:9881594-Protein Kinase C,
pubmed-meshheading:9881594-Rats,
pubmed-meshheading:9881594-Rats, Wistar,
pubmed-meshheading:9881594-Streptolysins,
pubmed-meshheading:9881594-Synaptosomes
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pubmed:year |
1998
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pubmed:articleTitle |
Anti-B-50 (GAP-43) antibodies decrease exocytosis of glutamate in permeated synaptosomes.
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pubmed:affiliation |
Department of Medical Pharmacology, Rudolf Magnus Institute for Neurosciences, Utrecht University, The Netherlands.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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