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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1987-6-11
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pubmed:abstractText |
Neurotransmitters are essential for communication between neurons and hence are vital in the overall integrative functioning of the nervous system. Previous work on acetylcholine metabolism in the fruit fly, Drosophila melanogaster, has also raised the possibility that transmitter metabolism may play a prominent role in either the achievement or maintenance of the normal structure of the central nervous system in this species. Unfortunately, acetylcholine is rather poorly characterized as a neurotransmitter in Drosophila; consequently, we have begun an analysis of the role of glutamate (probably the best characterized transmitter in this organism) in the formation and/or maintenance of nervous system structure. We present here the results of a series of preliminary analyses. To suggest where glutamatergic function may be localized, an examination of the spatial distribution of high affinity [3H]-glutamate binding sites are presented. We present the results of an analysis of the spatial and temporal distribution of enzymatic activities thought to be important in the regulation of transmitter-glutamate pools (i.e., glutamate oxaloacetic transaminase, glutaminase, and glutamate dehydrogenase). To begin to examine whether mutations in any of these functions are capable of affecting glutamatergic activity, we present the results of an initial genetic analysis of one enzymatic function, glutamate oxaloacetic transaminase (GOT), chosen because of its differential distribution within the adult central nervous system and musculature.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aspartate Aminotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamates,
http://linkedlifedata.com/resource/pubmed/chemical/Glutaminase,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-3034
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15-41
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:3106567-Animals,
pubmed-meshheading:3106567-Aspartate Aminotransferases,
pubmed-meshheading:3106567-Binding Sites,
pubmed-meshheading:3106567-Drosophila melanogaster,
pubmed-meshheading:3106567-Female,
pubmed-meshheading:3106567-Genetic Techniques,
pubmed-meshheading:3106567-Glutamate Dehydrogenase,
pubmed-meshheading:3106567-Glutamates,
pubmed-meshheading:3106567-Glutaminase,
pubmed-meshheading:3106567-Injections,
pubmed-meshheading:3106567-Male,
pubmed-meshheading:3106567-Muscles,
pubmed-meshheading:3106567-Nervous System Physiological Phenomena,
pubmed-meshheading:3106567-Tissue Distribution,
pubmed-meshheading:3106567-Tritium
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pubmed:year |
1987
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pubmed:articleTitle |
A genetic analysis of glutamatergic function in Drosophila.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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