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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1990-5-4
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pubmed:abstractText |
Electrogenic sodium- and chloride-dependent gamma-aminobutyric acid (GABA) transport in crude synaptosomal membrane vesicles is partly inhibited by saturating levels of either of the substrate analogues cis-3-aminocyclohexanecarboxylic acid (ACHC) or beta-alanine. However, both of them together potently and fully inhibit the process. Transport of beta-alanine, which exhibits an apparent Km of about 44 microM, is also electrogenic and sodium and chloride dependent and competitively inhibited by GABA with a Ki of about 3 microM. This value is very similar to the Km of 2-4 microM found for GABA transport. On the other hand, ACHC does not inhibit beta-alanine transport at all. Upon solubilization of the membrane proteins with cholate and fractionation with ammonium sulfate, a fraction is obtained which upon reconstitution into proteoliposomes exhibits 4- to 10-fold-increased GABA transport. This activity is fully inhibited by low concentrations of ACHC and is not sensitive at all to beta-alanine. GABA transport in this preparation exhibits an apparent Km of about 2.5 microM and it is competitively inhibited by ACHC (Ki approximately 7 microM). These data indicate the presence of two GABA transporter subtypes in the membrane vesicles: the A type, sensitive to ACHC, and the B type, sensitive to beta-alanine.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-1011247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-13428781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-187950,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-234775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-2414778,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-2576384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-2888595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-2903047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-2964510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-3093232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-3349023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-3536902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-4044581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-4360030,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-5036031,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-589464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-6101962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-6141802,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-6433216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-656383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-6838850,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-6849911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2108440-836500
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
87
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2550-4
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2108440-Animals,
pubmed-meshheading:2108440-Biological Transport,
pubmed-meshheading:2108440-Brain,
pubmed-meshheading:2108440-Carrier Proteins,
pubmed-meshheading:2108440-Cell Membrane,
pubmed-meshheading:2108440-Chlorides,
pubmed-meshheading:2108440-GABA Plasma Membrane Transport Proteins,
pubmed-meshheading:2108440-Kinetics,
pubmed-meshheading:2108440-Membrane Proteins,
pubmed-meshheading:2108440-Membrane Transport Proteins,
pubmed-meshheading:2108440-Nerve Tissue Proteins,
pubmed-meshheading:2108440-Organic Anion Transporters,
pubmed-meshheading:2108440-Rats,
pubmed-meshheading:2108440-Sodium,
pubmed-meshheading:2108440-Synaptosomes,
pubmed-meshheading:2108440-beta-Alanine,
pubmed-meshheading:2108440-gamma-Aminobutyric Acid
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pubmed:year |
1990
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pubmed:articleTitle |
Two pharmacologically distinct sodium- and chloride-coupled high-affinity gamma-aminobutyric acid transporters are present in plasma membrane vesicles and reconstituted preparations from rat brain.
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pubmed:affiliation |
Department of Biochemistry, Hadassah Medical School, Hebrew University, Jerusalem, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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