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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1991-8-29
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pubmed:abstractText |
In the present work the distribution of L-glutamate binding sites in the different layers of human cerebellum of normal individuals and of seven patients who died with olivopontocerebellar atrophy (OPCA) was examined with the technique of quantitative autoradiography. Specific L-[3H]glutamate binding was higher in the molecular than in the granule cell layer of normal cerebellar tissue. A significant decrease of L-[3H]glutamate specific binding was observed in the molecular layer of all OPCA tissues. In the granule cell layer L-[3H]glutamate binding was decreased only in two patients who suffered from late-onset sporadic OPCA and in one patient who suffered from a form of OPCA inherited in a dominant manner. Quisqualate-sensitive binding sites were the most abundant binding sites in the molecular layer of normal cerebella, whereas N-methyl-D-aspartic acid (NMDA)-sensitive binding sites were the most abundant type in the granule cell layer. A significant decrease of quisqualate-sensitive and an increase in NMDA-sensitive binding sites were observed in the molecular layer of OPCA cerebellar tissues. No significant changes were observed in the granule cell layer of these tissues.
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pubmed:grant |
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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/2-Amino-5-phosphonovalerate,
http://linkedlifedata.com/resource/pubmed/chemical/3-(2-carboxypiperazin-4-yl)propyl-1-...,
http://linkedlifedata.com/resource/pubmed/chemical/6-Cyano-7-nitroquinoxaline-2,3-dione,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamates,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Ibotenic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/N-Methylaspartate,
http://linkedlifedata.com/resource/pubmed/chemical/Piperazines,
http://linkedlifedata.com/resource/pubmed/chemical/Quinoxalines,
http://linkedlifedata.com/resource/pubmed/chemical/Quisqualic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, AMPA,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Glutamate,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, N-Methyl-D-Aspartate,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Neurotransmitter,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Amino-3-hydroxy-5-methyl-4-iso...
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0360-4012
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
367-75
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1677427-2-Amino-5-phosphonovalerate,
pubmed-meshheading:1677427-6-Cyano-7-nitroquinoxaline-2,3-dione,
pubmed-meshheading:1677427-Adolescent,
pubmed-meshheading:1677427-Adult,
pubmed-meshheading:1677427-Cerebellum,
pubmed-meshheading:1677427-Female,
pubmed-meshheading:1677427-Glutamates,
pubmed-meshheading:1677427-Glutamic Acid,
pubmed-meshheading:1677427-Humans,
pubmed-meshheading:1677427-Ibotenic Acid,
pubmed-meshheading:1677427-Male,
pubmed-meshheading:1677427-N-Methylaspartate,
pubmed-meshheading:1677427-Olivopontocerebellar Atrophies,
pubmed-meshheading:1677427-Piperazines,
pubmed-meshheading:1677427-Quinoxalines,
pubmed-meshheading:1677427-Quisqualic Acid,
pubmed-meshheading:1677427-Receptors, AMPA,
pubmed-meshheading:1677427-Receptors, Glutamate,
pubmed-meshheading:1677427-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:1677427-Receptors, Neurotransmitter,
pubmed-meshheading:1677427-alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid
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pubmed:year |
1991
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pubmed:articleTitle |
Quantitative autoradiographic study of L-glutamate binding sites in normal and atrophic human cerebellum.
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pubmed:affiliation |
Department of Physiology, Medical School, University of Patras, Greece.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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