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Article: Characterization of a large conductance, cation-selective channel from sea urchin eggs that is sensitive to sulfhydryl reducing agents

TitleCharacterization of a large conductance, cation-selective channel from sea urchin eggs that is sensitive to sulfhydryl reducing agents
Authors
Issue Date1996
PublisherSpringer New York LLC. The Journal's web site is located at http://link.springer.de/link/service/journals/00232/
Citation
Journal Of Membrane Biology, 1996, v. 150 n. 1, p. 27-35 How to Cite?
AbstractVesicles containing large conductance cation selective channels were isolated from sea urchin (Strongylocentrotus purpuratus) eggs. Addition of the vesicles to one side of lipid bilayer led to the rapid appearance of 200 or more identical channels. These channels would then inactivate within 2 to 10 min. The inactivation could be prevented by the addition of sulfhydryl reducing agents (e.g., dithiothreitol or glutathione) to the cis side of the membrane. Only one channel type is present. The channel is cation selective, with a conductance of 572 ps in symmetrical 0.5 M KCl. The relative cation selectivity is K (1.0) > Cs (0.53) ~ Na (0.52) > Li (0.2). The permeability ratio (P(X)/P(K) is 1.37 (Li) > 1.27 (Na) > 0.57 (Cs). Most organic cations (choline, tetraethylamine, tetrabutylamine, gallamine, lysine, histidine, arginine, etc.) and multivalent cations (La+3, alkali earth family, Zn+2, Eu+3, etc.) produced a significant channel block. The highest observed affinity was for La+3 which produced a 50% decrease in conductance in 500 mM KCl at a concentration of 8 μM. The biophysical properties of this channel are similar to those of a nonselective channel found in ascidian egg plasma membrane (Dale and DeFelice, 1984). A soluble extract of the egg supernatant can also prevent the inactivation of the channels. Using deactivated channels reconstituted into a planar lipid bilayer as an assay, this factor was partially purified. It is heat and acetone stable with a molecular weight of between 10 and 20 K. One of the major bands remaining in the purest fraction cross reacted with antibodies raised against E. coli thioredoxin.
Persistent Identifierhttp://hdl.handle.net/10722/171628
ISSN
2015 Impact Factor: 1.991
2015 SCImago Journal Rankings: 0.738
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLii, Ten_US
dc.contributor.authorLee, HCen_US
dc.contributor.authorGleason, FKen_US
dc.contributor.authorLevitt, DGen_US
dc.date.accessioned2012-10-30T06:16:03Z-
dc.date.available2012-10-30T06:16:03Z-
dc.date.issued1996en_US
dc.identifier.citationJournal Of Membrane Biology, 1996, v. 150 n. 1, p. 27-35en_US
dc.identifier.issn0022-2631en_US
dc.identifier.urihttp://hdl.handle.net/10722/171628-
dc.description.abstractVesicles containing large conductance cation selective channels were isolated from sea urchin (Strongylocentrotus purpuratus) eggs. Addition of the vesicles to one side of lipid bilayer led to the rapid appearance of 200 or more identical channels. These channels would then inactivate within 2 to 10 min. The inactivation could be prevented by the addition of sulfhydryl reducing agents (e.g., dithiothreitol or glutathione) to the cis side of the membrane. Only one channel type is present. The channel is cation selective, with a conductance of 572 ps in symmetrical 0.5 M KCl. The relative cation selectivity is K (1.0) > Cs (0.53) ~ Na (0.52) > Li (0.2). The permeability ratio (P(X)/P(K) is 1.37 (Li) > 1.27 (Na) > 0.57 (Cs). Most organic cations (choline, tetraethylamine, tetrabutylamine, gallamine, lysine, histidine, arginine, etc.) and multivalent cations (La+3, alkali earth family, Zn+2, Eu+3, etc.) produced a significant channel block. The highest observed affinity was for La+3 which produced a 50% decrease in conductance in 500 mM KCl at a concentration of 8 μM. The biophysical properties of this channel are similar to those of a nonselective channel found in ascidian egg plasma membrane (Dale and DeFelice, 1984). A soluble extract of the egg supernatant can also prevent the inactivation of the channels. Using deactivated channels reconstituted into a planar lipid bilayer as an assay, this factor was partially purified. It is heat and acetone stable with a molecular weight of between 10 and 20 K. One of the major bands remaining in the purest fraction cross reacted with antibodies raised against E. coli thioredoxin.en_US
dc.languageengen_US
dc.publisherSpringer New York LLC. The Journal's web site is located at http://link.springer.de/link/service/journals/00232/en_US
dc.relation.ispartofJournal of Membrane Biologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAnions - Metabolismen_US
dc.subject.meshBiophysical Phenomenaen_US
dc.subject.meshBiophysicsen_US
dc.subject.meshBlotting, Westernen_US
dc.subject.meshCations - Metabolismen_US
dc.subject.meshChromatography, Gelen_US
dc.subject.meshChromatography, Ion Exchangeen_US
dc.subject.meshElectric Conductivityen_US
dc.subject.meshFemaleen_US
dc.subject.meshIon Channel Gatingen_US
dc.subject.meshIon Channels - Drug Effects - Isolation & Purification - Metabolismen_US
dc.subject.meshLipid Bilayers - Chemistry - Metabolismen_US
dc.subject.meshOvum - Metabolismen_US
dc.subject.meshPermeabilityen_US
dc.subject.meshSea Urchins - Metabolismen_US
dc.subject.meshSulfhydryl Reagents - Pharmacologyen_US
dc.subject.meshThioredoxins - Metabolismen_US
dc.titleCharacterization of a large conductance, cation-selective channel from sea urchin eggs that is sensitive to sulfhydryl reducing agentsen_US
dc.typeArticleen_US
dc.identifier.emailLee, HC:leehc@hku.hken_US
dc.identifier.authorityLee, HC=rp00545en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/s002329900027en_US
dc.identifier.pmid8699477-
dc.identifier.scopuseid_2-s2.0-0030007439en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0030007439&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume150en_US
dc.identifier.issue1en_US
dc.identifier.spage27en_US
dc.identifier.epage35en_US
dc.identifier.isiWOS:A1996TZ75300002-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLii, T=6602417510en_US
dc.identifier.scopusauthoridLee, HC=26642959100en_US
dc.identifier.scopusauthoridGleason, FK=7004177199en_US
dc.identifier.scopusauthoridLevitt, DG=7102923276en_US

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