Acetylcholine receptor conformational transition on excitation masks disulphide bonds against reduction
KARLIN and Bartels 1 found that dithiothreitol (DTT) inhibits the responses induced by acetylcholine (ACh) in the Electrophorus electricus electroplax preparation and that 5,5′-dithio- bis -(2-nitrobenzoic acid) completely restored the membrane sensitivity to ACh. These results illustrate the import...
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| Veröffentlicht in: | Nature (London) 1977-11, Vol.270 (5632), p.71-73 |
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| container_title | Nature (London) |
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| creator | BREGESTOVSKI, P. D. ILJIN, V. I. JURCHENKO, OLGA P. VEPRINTSEV, B. N. VULFIUS, CATHERINE A. |
| description | KARLIN and Bartels
1
found that dithiothreitol (DTT) inhibits the responses induced by acetylcholine (ACh) in the
Electrophorus electricus
electroplax preparation and that 5,5′-dithio-
bis
-(2-nitrobenzoic acid) completely restored the membrane sensitivity to ACh. These results illustrate the importance of disulphide bonds for acetylcholine receptor (AChR) function, and work on other preparations with nicotinic AChRs gave similar results
2–9
. Several facts suggest that DTT affects AChRs specifically; (1), the significance of the quaternary ammonium group in the molecules of alkylating and acylating agents for the rate of their reaction with the AChR reduced by DTT
10
; (2) changes in pharmacological specificity seen in the modified receptor
5,7,10
;(3) the decrease in the slope of the dose–response curve to carbamylcholine expressed as the Hillplot
11
; and (4) the increase in
d
-tubocurarine affinity to the AChR active site
5
. If we could protect the receptor against chemical modification by an agonist or antagonist, this would be the most reliable proof of the specificity of modifying agent action
12
. We present here a detailed study of the action of DTT on nicotinic AChRs of completely isolated
Limnaea stagnalis
neurones in order to clarify the ability of various cholinergic ligands to protect the receptor disulphide bonds against reduction by DTT. |
| doi_str_mv | 10.1038/270071a0 |
| format | Article |
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1
found that dithiothreitol (DTT) inhibits the responses induced by acetylcholine (ACh) in the
Electrophorus electricus
electroplax preparation and that 5,5′-dithio-
bis
-(2-nitrobenzoic acid) completely restored the membrane sensitivity to ACh. These results illustrate the importance of disulphide bonds for acetylcholine receptor (AChR) function, and work on other preparations with nicotinic AChRs gave similar results
2–9
. Several facts suggest that DTT affects AChRs specifically; (1), the significance of the quaternary ammonium group in the molecules of alkylating and acylating agents for the rate of their reaction with the AChR reduced by DTT
10
; (2) changes in pharmacological specificity seen in the modified receptor
5,7,10
;(3) the decrease in the slope of the dose–response curve to carbamylcholine expressed as the Hillplot
11
; and (4) the increase in
d
-tubocurarine affinity to the AChR active site
5
. If we could protect the receptor against chemical modification by an agonist or antagonist, this would be the most reliable proof of the specificity of modifying agent action
12
. We present here a detailed study of the action of DTT on nicotinic AChRs of completely isolated
Limnaea stagnalis
neurones in order to clarify the ability of various cholinergic ligands to protect the receptor disulphide bonds against reduction by DTT.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/270071a0</identifier><identifier>PMID: 927521</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Animals ; Binding Sites ; Disulfides ; Dithiothreitol ; Humanities and Social Sciences ; In Vitro Techniques ; letter ; Ligands ; Membrane Potentials - drug effects ; Mollusca ; multidisciplinary ; Neurilemma - physiology ; Oxidation-Reduction ; Parasympathomimetics - pharmacology ; Protein Conformation - drug effects ; Receptors, Cholinergic - drug effects ; Receptors, Nicotinic - drug effects ; Science ; Science (multidisciplinary)</subject><ispartof>Nature (London), 1977-11, Vol.270 (5632), p.71-73</ispartof><rights>Springer Nature Limited 1977</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2260-bb09f41069bc1a5c5709d1c5a26ed07b8f8b32698934f3998fe173d206ad1eb23</citedby><cites>FETCH-LOGICAL-c2260-bb09f41069bc1a5c5709d1c5a26ed07b8f8b32698934f3998fe173d206ad1eb23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/270071a0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/270071a0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/927521$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>BREGESTOVSKI, P. D.</creatorcontrib><creatorcontrib>ILJIN, V. I.</creatorcontrib><creatorcontrib>JURCHENKO, OLGA P.</creatorcontrib><creatorcontrib>VEPRINTSEV, B. N.</creatorcontrib><creatorcontrib>VULFIUS, CATHERINE A.</creatorcontrib><title>Acetylcholine receptor conformational transition on excitation masks disulphide bonds against reduction</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>KARLIN and Bartels
1
found that dithiothreitol (DTT) inhibits the responses induced by acetylcholine (ACh) in the
Electrophorus electricus
electroplax preparation and that 5,5′-dithio-
bis
-(2-nitrobenzoic acid) completely restored the membrane sensitivity to ACh. These results illustrate the importance of disulphide bonds for acetylcholine receptor (AChR) function, and work on other preparations with nicotinic AChRs gave similar results
2–9
. Several facts suggest that DTT affects AChRs specifically; (1), the significance of the quaternary ammonium group in the molecules of alkylating and acylating agents for the rate of their reaction with the AChR reduced by DTT
10
; (2) changes in pharmacological specificity seen in the modified receptor
5,7,10
;(3) the decrease in the slope of the dose–response curve to carbamylcholine expressed as the Hillplot
11
; and (4) the increase in
d
-tubocurarine affinity to the AChR active site
5
. If we could protect the receptor against chemical modification by an agonist or antagonist, this would be the most reliable proof of the specificity of modifying agent action
12
. We present here a detailed study of the action of DTT on nicotinic AChRs of completely isolated
Limnaea stagnalis
neurones in order to clarify the ability of various cholinergic ligands to protect the receptor disulphide bonds against reduction by DTT.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>Disulfides</subject><subject>Dithiothreitol</subject><subject>Humanities and Social Sciences</subject><subject>In Vitro Techniques</subject><subject>letter</subject><subject>Ligands</subject><subject>Membrane Potentials - drug effects</subject><subject>Mollusca</subject><subject>multidisciplinary</subject><subject>Neurilemma - physiology</subject><subject>Oxidation-Reduction</subject><subject>Parasympathomimetics - pharmacology</subject><subject>Protein Conformation - drug effects</subject><subject>Receptors, Cholinergic - drug effects</subject><subject>Receptors, Nicotinic - drug effects</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1977</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNplkE1LxDAQhoP4ta6CP8BDTqKH6iRtk-a4LH7Bghc9lzRJd7O2TU1acP-9rV29CAPD8Dy8MC9ClwTuCMTZPeUAnEg4QDOScBYlLOOHaAZAswiymJ2isxC2AJASnpygY0F5SskMrRfKdLtKbVxlG4O9UabtnMfKNaXzteysa2SFOy-bYMcDD2O-lO1-EK5l-AhY29BX7cZqgwvX6IDlWtomdEOe7tUonqOjUlbBXOz3HL0_Prwtn6PV69PLcrGKFKUMoqIAUSYEmCgUkalKOQhNVCopMxp4kZVZEVMmMhEnZSxEVhrCY02BSU1MQeM5up5yW-8-exO6vLZBmaqSjXF9yHk8_s1G8WYSlXcheFPmrbe19LucQD5Wmv9WOqhX-8y-qI3-E6cOB3w74TCAZm18vnW9H1oL_6O-AXvZf9Y</recordid><startdate>19771103</startdate><enddate>19771103</enddate><creator>BREGESTOVSKI, P. D.</creator><creator>ILJIN, V. I.</creator><creator>JURCHENKO, OLGA P.</creator><creator>VEPRINTSEV, B. N.</creator><creator>VULFIUS, CATHERINE A.</creator><general>Nature Publishing Group UK</general><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>19771103</creationdate><title>Acetylcholine receptor conformational transition on excitation masks disulphide bonds against reduction</title><author>BREGESTOVSKI, P. D. ; ILJIN, V. I. ; JURCHENKO, OLGA P. ; VEPRINTSEV, B. N. ; VULFIUS, CATHERINE A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2260-bb09f41069bc1a5c5709d1c5a26ed07b8f8b32698934f3998fe173d206ad1eb23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1977</creationdate><topic>Animals</topic><topic>Binding Sites</topic><topic>Disulfides</topic><topic>Dithiothreitol</topic><topic>Humanities and Social Sciences</topic><topic>In Vitro Techniques</topic><topic>letter</topic><topic>Ligands</topic><topic>Membrane Potentials - drug effects</topic><topic>Mollusca</topic><topic>multidisciplinary</topic><topic>Neurilemma - physiology</topic><topic>Oxidation-Reduction</topic><topic>Parasympathomimetics - pharmacology</topic><topic>Protein Conformation - drug effects</topic><topic>Receptors, Cholinergic - drug effects</topic><topic>Receptors, Nicotinic - drug effects</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BREGESTOVSKI, P. D.</creatorcontrib><creatorcontrib>ILJIN, V. I.</creatorcontrib><creatorcontrib>JURCHENKO, OLGA P.</creatorcontrib><creatorcontrib>VEPRINTSEV, B. N.</creatorcontrib><creatorcontrib>VULFIUS, CATHERINE A.</creatorcontrib><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>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>BREGESTOVSKI, P. D.</au><au>ILJIN, V. I.</au><au>JURCHENKO, OLGA P.</au><au>VEPRINTSEV, B. N.</au><au>VULFIUS, CATHERINE A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Acetylcholine receptor conformational transition on excitation masks disulphide bonds against reduction</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1977-11-03</date><risdate>1977</risdate><volume>270</volume><issue>5632</issue><spage>71</spage><epage>73</epage><pages>71-73</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><abstract>KARLIN and Bartels
1
found that dithiothreitol (DTT) inhibits the responses induced by acetylcholine (ACh) in the
Electrophorus electricus
electroplax preparation and that 5,5′-dithio-
bis
-(2-nitrobenzoic acid) completely restored the membrane sensitivity to ACh. These results illustrate the importance of disulphide bonds for acetylcholine receptor (AChR) function, and work on other preparations with nicotinic AChRs gave similar results
2–9
. Several facts suggest that DTT affects AChRs specifically; (1), the significance of the quaternary ammonium group in the molecules of alkylating and acylating agents for the rate of their reaction with the AChR reduced by DTT
10
; (2) changes in pharmacological specificity seen in the modified receptor
5,7,10
;(3) the decrease in the slope of the dose–response curve to carbamylcholine expressed as the Hillplot
11
; and (4) the increase in
d
-tubocurarine affinity to the AChR active site
5
. If we could protect the receptor against chemical modification by an agonist or antagonist, this would be the most reliable proof of the specificity of modifying agent action
12
. We present here a detailed study of the action of DTT on nicotinic AChRs of completely isolated
Limnaea stagnalis
neurones in order to clarify the ability of various cholinergic ligands to protect the receptor disulphide bonds against reduction by DTT.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>927521</pmid><doi>10.1038/270071a0</doi><tpages>3</tpages></addata></record> |
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| source | MEDLINE; SpringerLink Journals; Nature Journals Online |
| subjects | Animals Binding Sites Disulfides Dithiothreitol Humanities and Social Sciences In Vitro Techniques letter Ligands Membrane Potentials - drug effects Mollusca multidisciplinary Neurilemma - physiology Oxidation-Reduction Parasympathomimetics - pharmacology Protein Conformation - drug effects Receptors, Cholinergic - drug effects Receptors, Nicotinic - drug effects Science Science (multidisciplinary) |
| title | Acetylcholine receptor conformational transition on excitation masks disulphide bonds against reduction |
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