Cerebellar glutamate metabolizing enzymes in spinocerebellar ataxia type I
We measured the levels of three glutamate metabolizing enzymes, namely, glutamate dehydrogenase (GDH), aspartate aminotransferase (AAT), and glutamine synthetase (GS) in cerebellar and occipital cortices of nine patients with dominantly-inherited olivopontocerebellar atrophy (OPCA; spinocerebellar a...
Gespeichert in:
Veröffentlicht in: | Metabolic brain disease 1994-03, Vol.9 (1), p.97-103 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 103 |
---|---|
container_issue | 1 |
container_start_page | 97 |
container_title | Metabolic brain disease |
container_volume | 9 |
creator | KISH, S. J LI-JAN CHANG DIXON, L. M ROBITAILLE, Y DISTEFANO, L |
description | We measured the levels of three glutamate metabolizing enzymes, namely, glutamate dehydrogenase (GDH), aspartate aminotransferase (AAT), and glutamine synthetase (GS) in cerebellar and occipital cortices of nine patients with dominantly-inherited olivopontocerebellar atrophy (OPCA; spinocerebellar ataxia type I). As compared with the controls, mean GDH activities in cerebellar cortex of the OPCA patients were normal whereas levels of AAT (-17%) and the glial enzyme GS (-27%) were significantly reduced. No statistically significant changes were observed in occipital cortex, a morphologically unaffected brain area. We suggest that the decreased GS levels could reflect impaired capacity of astrocytes to metabolize glutamate which might contribute to the degenerative processes in OPCA cerebellum. |
doi_str_mv | 10.1007/BF01996077 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_76652253</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>76652253</sourcerecordid><originalsourceid>FETCH-LOGICAL-c311t-93aa0f4e89004ec9645ab361193f84f8b8b9d20766953368e5eebdd5a6641c703</originalsourceid><addsrcrecordid>eNpFkE1Lw0AYhBdRaq1evAs5iAch-m73-6jFaqXgRc9hs3lTVvJlNgHbX2-KoT3NYZ4ZhiHkmsIDBVCPz0ugxkhQ6oRMqVAsVkyKUzIFrUWsuIFzchHCNwAwQc2ETJShXEozJe8LbDHForBttCn6zpa2w6jEzqZ14Xe-2kRY7bYlhshXUWh8Vbtjwnb219uo2zYYrS7JWW6LgFejzsjX8uVz8RavP15Xi6d17BilXWyYtZBz1AaAozOSC5sySalhuea5TnVqsjmoYZ5gTGoUiGmWCSslp04Bm5G7_96mrX96DF1S-uD2gyqs-5AMSTGfD9kZuf8HXVuH0GKeNK0vbbtNKCT745LjcQN8M7b2aYnZAR2fGvzb0bfB2SJvbeV8OGCccq24Zn_xW3R1</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>76652253</pqid></control><display><type>article</type><title>Cerebellar glutamate metabolizing enzymes in spinocerebellar ataxia type I</title><source>MEDLINE</source><source>SpringerLink Journals - AutoHoldings</source><creator>KISH, S. J ; LI-JAN CHANG ; DIXON, L. M ; ROBITAILLE, Y ; DISTEFANO, L</creator><creatorcontrib>KISH, S. J ; LI-JAN CHANG ; DIXON, L. M ; ROBITAILLE, Y ; DISTEFANO, L</creatorcontrib><description>We measured the levels of three glutamate metabolizing enzymes, namely, glutamate dehydrogenase (GDH), aspartate aminotransferase (AAT), and glutamine synthetase (GS) in cerebellar and occipital cortices of nine patients with dominantly-inherited olivopontocerebellar atrophy (OPCA; spinocerebellar ataxia type I). As compared with the controls, mean GDH activities in cerebellar cortex of the OPCA patients were normal whereas levels of AAT (-17%) and the glial enzyme GS (-27%) were significantly reduced. No statistically significant changes were observed in occipital cortex, a morphologically unaffected brain area. We suggest that the decreased GS levels could reflect impaired capacity of astrocytes to metabolize glutamate which might contribute to the degenerative processes in OPCA cerebellum.</description><identifier>ISSN: 0885-7490</identifier><identifier>EISSN: 1573-7365</identifier><identifier>DOI: 10.1007/BF01996077</identifier><identifier>PMID: 7914669</identifier><identifier>CODEN: MBDIEE</identifier><language>eng</language><publisher>New York, NY: Springer</publisher><subject>Adult ; Amino Acids - metabolism ; Aspartate Aminotransferases - metabolism ; Biological and medical sciences ; Cerebellar Cortex - enzymology ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; Female ; Glutamate Dehydrogenase - metabolism ; Glutamate-Ammonia Ligase - metabolism ; Glutamates - metabolism ; Glutamic Acid ; Humans ; Male ; Medical sciences ; Neurology ; Occipital Lobe - enzymology ; Olivopontocerebellar Atrophies - enzymology</subject><ispartof>Metabolic brain disease, 1994-03, Vol.9 (1), p.97-103</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c311t-93aa0f4e89004ec9645ab361193f84f8b8b9d20766953368e5eebdd5a6641c703</citedby><cites>FETCH-LOGICAL-c311t-93aa0f4e89004ec9645ab361193f84f8b8b9d20766953368e5eebdd5a6641c703</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4148748$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7914669$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>KISH, S. J</creatorcontrib><creatorcontrib>LI-JAN CHANG</creatorcontrib><creatorcontrib>DIXON, L. M</creatorcontrib><creatorcontrib>ROBITAILLE, Y</creatorcontrib><creatorcontrib>DISTEFANO, L</creatorcontrib><title>Cerebellar glutamate metabolizing enzymes in spinocerebellar ataxia type I</title><title>Metabolic brain disease</title><addtitle>Metab Brain Dis</addtitle><description>We measured the levels of three glutamate metabolizing enzymes, namely, glutamate dehydrogenase (GDH), aspartate aminotransferase (AAT), and glutamine synthetase (GS) in cerebellar and occipital cortices of nine patients with dominantly-inherited olivopontocerebellar atrophy (OPCA; spinocerebellar ataxia type I). As compared with the controls, mean GDH activities in cerebellar cortex of the OPCA patients were normal whereas levels of AAT (-17%) and the glial enzyme GS (-27%) were significantly reduced. No statistically significant changes were observed in occipital cortex, a morphologically unaffected brain area. We suggest that the decreased GS levels could reflect impaired capacity of astrocytes to metabolize glutamate which might contribute to the degenerative processes in OPCA cerebellum.</description><subject>Adult</subject><subject>Amino Acids - metabolism</subject><subject>Aspartate Aminotransferases - metabolism</subject><subject>Biological and medical sciences</subject><subject>Cerebellar Cortex - enzymology</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</subject><subject>Female</subject><subject>Glutamate Dehydrogenase - metabolism</subject><subject>Glutamate-Ammonia Ligase - metabolism</subject><subject>Glutamates - metabolism</subject><subject>Glutamic Acid</subject><subject>Humans</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Neurology</subject><subject>Occipital Lobe - enzymology</subject><subject>Olivopontocerebellar Atrophies - enzymology</subject><issn>0885-7490</issn><issn>1573-7365</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1Lw0AYhBdRaq1evAs5iAch-m73-6jFaqXgRc9hs3lTVvJlNgHbX2-KoT3NYZ4ZhiHkmsIDBVCPz0ugxkhQ6oRMqVAsVkyKUzIFrUWsuIFzchHCNwAwQc2ETJShXEozJe8LbDHForBttCn6zpa2w6jEzqZ14Xe-2kRY7bYlhshXUWh8Vbtjwnb219uo2zYYrS7JWW6LgFejzsjX8uVz8RavP15Xi6d17BilXWyYtZBz1AaAozOSC5sySalhuea5TnVqsjmoYZ5gTGoUiGmWCSslp04Bm5G7_96mrX96DF1S-uD2gyqs-5AMSTGfD9kZuf8HXVuH0GKeNK0vbbtNKCT745LjcQN8M7b2aYnZAR2fGvzb0bfB2SJvbeV8OGCccq24Zn_xW3R1</recordid><startdate>19940301</startdate><enddate>19940301</enddate><creator>KISH, S. J</creator><creator>LI-JAN CHANG</creator><creator>DIXON, L. M</creator><creator>ROBITAILLE, Y</creator><creator>DISTEFANO, L</creator><general>Springer</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19940301</creationdate><title>Cerebellar glutamate metabolizing enzymes in spinocerebellar ataxia type I</title><author>KISH, S. J ; LI-JAN CHANG ; DIXON, L. M ; ROBITAILLE, Y ; DISTEFANO, L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c311t-93aa0f4e89004ec9645ab361193f84f8b8b9d20766953368e5eebdd5a6641c703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Adult</topic><topic>Amino Acids - metabolism</topic><topic>Aspartate Aminotransferases - metabolism</topic><topic>Biological and medical sciences</topic><topic>Cerebellar Cortex - enzymology</topic><topic>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</topic><topic>Female</topic><topic>Glutamate Dehydrogenase - metabolism</topic><topic>Glutamate-Ammonia Ligase - metabolism</topic><topic>Glutamates - metabolism</topic><topic>Glutamic Acid</topic><topic>Humans</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Neurology</topic><topic>Occipital Lobe - enzymology</topic><topic>Olivopontocerebellar Atrophies - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KISH, S. J</creatorcontrib><creatorcontrib>LI-JAN CHANG</creatorcontrib><creatorcontrib>DIXON, L. M</creatorcontrib><creatorcontrib>ROBITAILLE, Y</creatorcontrib><creatorcontrib>DISTEFANO, L</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Metabolic brain disease</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>KISH, S. J</au><au>LI-JAN CHANG</au><au>DIXON, L. M</au><au>ROBITAILLE, Y</au><au>DISTEFANO, L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cerebellar glutamate metabolizing enzymes in spinocerebellar ataxia type I</atitle><jtitle>Metabolic brain disease</jtitle><addtitle>Metab Brain Dis</addtitle><date>1994-03-01</date><risdate>1994</risdate><volume>9</volume><issue>1</issue><spage>97</spage><epage>103</epage><pages>97-103</pages><issn>0885-7490</issn><eissn>1573-7365</eissn><coden>MBDIEE</coden><abstract>We measured the levels of three glutamate metabolizing enzymes, namely, glutamate dehydrogenase (GDH), aspartate aminotransferase (AAT), and glutamine synthetase (GS) in cerebellar and occipital cortices of nine patients with dominantly-inherited olivopontocerebellar atrophy (OPCA; spinocerebellar ataxia type I). As compared with the controls, mean GDH activities in cerebellar cortex of the OPCA patients were normal whereas levels of AAT (-17%) and the glial enzyme GS (-27%) were significantly reduced. No statistically significant changes were observed in occipital cortex, a morphologically unaffected brain area. We suggest that the decreased GS levels could reflect impaired capacity of astrocytes to metabolize glutamate which might contribute to the degenerative processes in OPCA cerebellum.</abstract><cop>New York, NY</cop><pub>Springer</pub><pmid>7914669</pmid><doi>10.1007/BF01996077</doi><tpages>7</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0885-7490 |
ispartof | Metabolic brain disease, 1994-03, Vol.9 (1), p.97-103 |
issn | 0885-7490 1573-7365 |
language | eng |
recordid | cdi_proquest_miscellaneous_76652253 |
source | MEDLINE; SpringerLink Journals - AutoHoldings |
subjects | Adult Amino Acids - metabolism Aspartate Aminotransferases - metabolism Biological and medical sciences Cerebellar Cortex - enzymology Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Female Glutamate Dehydrogenase - metabolism Glutamate-Ammonia Ligase - metabolism Glutamates - metabolism Glutamic Acid Humans Male Medical sciences Neurology Occipital Lobe - enzymology Olivopontocerebellar Atrophies - enzymology |
title | Cerebellar glutamate metabolizing enzymes in spinocerebellar ataxia type I |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T15%3A10%3A39IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cerebellar%20glutamate%20metabolizing%20enzymes%20in%20spinocerebellar%20ataxia%20type%20I&rft.jtitle=Metabolic%20brain%20disease&rft.au=KISH,%20S.%20J&rft.date=1994-03-01&rft.volume=9&rft.issue=1&rft.spage=97&rft.epage=103&rft.pages=97-103&rft.issn=0885-7490&rft.eissn=1573-7365&rft.coden=MBDIEE&rft_id=info:doi/10.1007/BF01996077&rft_dat=%3Cproquest_cross%3E76652253%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=76652253&rft_id=info:pmid/7914669&rfr_iscdi=true |