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Dithiols and monothiols are linked with GABA transport in membrane vesicles of rat brain synaptosomes
The properties of γ-aminobutyric acid (GABA) transport into membrane vesicles derived from synaptosomes of rat brain have been studied using membrane-permeable and -impermeable sulfhydryl reagents, dithiol-specific reagents and oxidizing reagents. GABA transport is inhibited, reversibly, by very low...
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Published in: | FEBS letters 1987-11, Vol.224 (2), p.391-395 |
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description | The properties of γ-aminobutyric acid (GABA) transport into membrane vesicles derived from synaptosomes of rat brain have been studied using membrane-permeable and -impermeable sulfhydryl reagents, dithiol-specific reagents and oxidizing reagents. GABA transport is inhibited, reversibly, by very low concentrations of the membrane-permeable trivalent arsenical, phenylarsine oxide. Preincubation with this reagent only partially protects GABA transport from inactivation by
N-ethylmaleimide (NEM). Thorin, a negatively charged trivalent arsenical, has no influence on GABA transport at concentrations 100-fold higher than that of the inhibitory phenylarsine oxide. The impermeant oxidizing agent, potassium ferricyanide, did not inhibit transport whereas the permeant reagent, diamide, was inhibitory. These data indicate that the GABA transporter possesses an activity-linked dithiol in a hydrophobic region of the carrier not accessible to charged, polar reagents.
p-Chloromercuribenzenesulfonate (PCMBS) also inhibits but does not protect against NEM inactivation, suggesting the occurrence of an activity-linked monothiol in a polar region of the carrier. |
doi_str_mv | 10.1016/0014-5793(87)80490-8 |
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N-ethylmaleimide (NEM). Thorin, a negatively charged trivalent arsenical, has no influence on GABA transport at concentrations 100-fold higher than that of the inhibitory phenylarsine oxide. The impermeant oxidizing agent, potassium ferricyanide, did not inhibit transport whereas the permeant reagent, diamide, was inhibitory. These data indicate that the GABA transporter possesses an activity-linked dithiol in a hydrophobic region of the carrier not accessible to charged, polar reagents.
p-Chloromercuribenzenesulfonate (PCMBS) also inhibits but does not protect against NEM inactivation, suggesting the occurrence of an activity-linked monothiol in a polar region of the carrier.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(87)80490-8</identifier><identifier>PMID: 3691796</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Biological Transport - drug effects ; brain ; Carrier Proteins ; GABA Plasma Membrane Transport Proteins ; GABA, γ-aminobutyric acid ; gamma -aminobutyric acid ; gamma-Aminobutyric Acid - metabolism ; Kinetics ; Male ; Membrane Proteins ; Membrane Transport Proteins ; N-Ethylmaleimide ; NEM, N-ethylmaleimide ; Nerve Tissue Proteins - metabolism ; Neurotransmitter ; Organic Anion Transporters ; PCMBS, p-chloromercuribenzenesulfonate ; Phenylarsine oxide ; Rats ; Sulfhydryl Compounds ; Sulfhydryl reagent ; Sulfhydryl Reagents - pharmacology ; Synaptosomes - metabolism ; Thorin, 4-(2-arsonophenyl)azo-3-hydroxy-2,7-naphthalenedisulfonic acid ; γ-Aminobutyric acid</subject><ispartof>FEBS letters, 1987-11, Vol.224 (2), p.391-395</ispartof><rights>1987</rights><rights>FEBS Letters 224 (1987) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4978-c5c44368dfd364b999cb5167c343b1cf7159327b4fa9fca5d7a212af4ed9f6443</citedby><cites>FETCH-LOGICAL-c4978-c5c44368dfd364b999cb5167c343b1cf7159327b4fa9fca5d7a212af4ed9f6443</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0014579387804908$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3549,27924,27925,45780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3691796$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Robillard, G.T.</creatorcontrib><creatorcontrib>Schaaf, J.M.</creatorcontrib><creatorcontrib>Teelken, A.W.</creatorcontrib><title>Dithiols and monothiols are linked with GABA transport in membrane vesicles of rat brain synaptosomes</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The properties of γ-aminobutyric acid (GABA) transport into membrane vesicles derived from synaptosomes of rat brain have been studied using membrane-permeable and -impermeable sulfhydryl reagents, dithiol-specific reagents and oxidizing reagents. GABA transport is inhibited, reversibly, by very low concentrations of the membrane-permeable trivalent arsenical, phenylarsine oxide. Preincubation with this reagent only partially protects GABA transport from inactivation by
N-ethylmaleimide (NEM). Thorin, a negatively charged trivalent arsenical, has no influence on GABA transport at concentrations 100-fold higher than that of the inhibitory phenylarsine oxide. The impermeant oxidizing agent, potassium ferricyanide, did not inhibit transport whereas the permeant reagent, diamide, was inhibitory. These data indicate that the GABA transporter possesses an activity-linked dithiol in a hydrophobic region of the carrier not accessible to charged, polar reagents.
p-Chloromercuribenzenesulfonate (PCMBS) also inhibits but does not protect against NEM inactivation, suggesting the occurrence of an activity-linked monothiol in a polar region of the carrier.</description><subject>Animals</subject><subject>Biological Transport - drug effects</subject><subject>brain</subject><subject>Carrier Proteins</subject><subject>GABA Plasma Membrane Transport Proteins</subject><subject>GABA, γ-aminobutyric acid</subject><subject>gamma -aminobutyric acid</subject><subject>gamma-Aminobutyric Acid - metabolism</subject><subject>Kinetics</subject><subject>Male</subject><subject>Membrane Proteins</subject><subject>Membrane Transport Proteins</subject><subject>N-Ethylmaleimide</subject><subject>NEM, N-ethylmaleimide</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurotransmitter</subject><subject>Organic Anion Transporters</subject><subject>PCMBS, p-chloromercuribenzenesulfonate</subject><subject>Phenylarsine oxide</subject><subject>Rats</subject><subject>Sulfhydryl Compounds</subject><subject>Sulfhydryl reagent</subject><subject>Sulfhydryl Reagents - pharmacology</subject><subject>Synaptosomes - metabolism</subject><subject>Thorin, 4-(2-arsonophenyl)azo-3-hydroxy-2,7-naphthalenedisulfonic acid</subject><subject>γ-Aminobutyric acid</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><recordid>eNqNUctu1DAUtRBVGQp_AJJXCBahduz4sUGalk6pVKkbWFuOfS0MSTzYmVbz9zidoUtgZZ17Hr46F6E3lHykhIpzQihvOqnZeyU_KMI1adQztKJKsoZxoZ6j1ZPkBXpZyg9SsaL6FJ0yoanUYoXgc5y_xzQUbCePxzSlPzADHuL0Ezx-qBJ8vb5Y4znbqWxTnnGc8AhjXzHgeyjRDVBwCjjbGddppct-sts5lTRCeYVOgh0KvD6-Z-jb5urr5Zfm9u765nJ92ziupWpc5zhnQvngmeC91tr1HRXSMc566oKknWat7HmwOjjbeWlb2trAwesgqvUMvTvkbnP6tYMymzEWB8NQ10y7YqRUmgv5byHlqhWEsSrkB6HLqZQMwWxzHG3eG0rMcgazdGyWjo2S5vEMRlXb22P-rh_BP5mOvVd-c-Af4gD7_8o0m6uLdiGWuZKP0-WjT4cgqLXeR8imuAiTAx8zuNn4FP--6W-wBqrd</recordid><startdate>19871130</startdate><enddate>19871130</enddate><creator>Robillard, G.T.</creator><creator>Schaaf, J.M.</creator><creator>Teelken, A.W.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19871130</creationdate><title>Dithiols and monothiols are linked with GABA transport in membrane vesicles of rat brain synaptosomes</title><author>Robillard, G.T. ; Schaaf, J.M. ; Teelken, A.W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4978-c5c44368dfd364b999cb5167c343b1cf7159327b4fa9fca5d7a212af4ed9f6443</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Animals</topic><topic>Biological Transport - drug effects</topic><topic>brain</topic><topic>Carrier Proteins</topic><topic>GABA Plasma Membrane Transport Proteins</topic><topic>GABA, γ-aminobutyric acid</topic><topic>gamma -aminobutyric acid</topic><topic>gamma-Aminobutyric Acid - metabolism</topic><topic>Kinetics</topic><topic>Male</topic><topic>Membrane Proteins</topic><topic>Membrane Transport Proteins</topic><topic>N-Ethylmaleimide</topic><topic>NEM, N-ethylmaleimide</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurotransmitter</topic><topic>Organic Anion Transporters</topic><topic>PCMBS, p-chloromercuribenzenesulfonate</topic><topic>Phenylarsine oxide</topic><topic>Rats</topic><topic>Sulfhydryl Compounds</topic><topic>Sulfhydryl reagent</topic><topic>Sulfhydryl Reagents - pharmacology</topic><topic>Synaptosomes - metabolism</topic><topic>Thorin, 4-(2-arsonophenyl)azo-3-hydroxy-2,7-naphthalenedisulfonic acid</topic><topic>γ-Aminobutyric acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Robillard, G.T.</creatorcontrib><creatorcontrib>Schaaf, J.M.</creatorcontrib><creatorcontrib>Teelken, A.W.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Robillard, G.T.</au><au>Schaaf, J.M.</au><au>Teelken, A.W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dithiols and monothiols are linked with GABA transport in membrane vesicles of rat brain synaptosomes</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1987-11-30</date><risdate>1987</risdate><volume>224</volume><issue>2</issue><spage>391</spage><epage>395</epage><pages>391-395</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The properties of γ-aminobutyric acid (GABA) transport into membrane vesicles derived from synaptosomes of rat brain have been studied using membrane-permeable and -impermeable sulfhydryl reagents, dithiol-specific reagents and oxidizing reagents. GABA transport is inhibited, reversibly, by very low concentrations of the membrane-permeable trivalent arsenical, phenylarsine oxide. Preincubation with this reagent only partially protects GABA transport from inactivation by
N-ethylmaleimide (NEM). Thorin, a negatively charged trivalent arsenical, has no influence on GABA transport at concentrations 100-fold higher than that of the inhibitory phenylarsine oxide. The impermeant oxidizing agent, potassium ferricyanide, did not inhibit transport whereas the permeant reagent, diamide, was inhibitory. These data indicate that the GABA transporter possesses an activity-linked dithiol in a hydrophobic region of the carrier not accessible to charged, polar reagents.
p-Chloromercuribenzenesulfonate (PCMBS) also inhibits but does not protect against NEM inactivation, suggesting the occurrence of an activity-linked monothiol in a polar region of the carrier.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>3691796</pmid><doi>10.1016/0014-5793(87)80490-8</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Biological Transport - drug effects brain Carrier Proteins GABA Plasma Membrane Transport Proteins GABA, γ-aminobutyric acid gamma -aminobutyric acid gamma-Aminobutyric Acid - metabolism Kinetics Male Membrane Proteins Membrane Transport Proteins N-Ethylmaleimide NEM, N-ethylmaleimide Nerve Tissue Proteins - metabolism Neurotransmitter Organic Anion Transporters PCMBS, p-chloromercuribenzenesulfonate Phenylarsine oxide Rats Sulfhydryl Compounds Sulfhydryl reagent Sulfhydryl Reagents - pharmacology Synaptosomes - metabolism Thorin, 4-(2-arsonophenyl)azo-3-hydroxy-2,7-naphthalenedisulfonic acid γ-Aminobutyric acid |
title | Dithiols and monothiols are linked with GABA transport in membrane vesicles of rat brain synaptosomes |
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