The sea anemone Bunodosoma caissarum toxin BcIII modulates the sodium current kinetics of rat dorsal root ganglia neurons and is displaced in a voltage-dependent manner
Sea anemone toxins bind to site 3 of the sodium channels, which is partially formed by the extracellular linker connecting S3 and S4 segments of domain IV, slowing down the inactivation process. In this work we have characterized the actions of BcIII, a sea anemone polypeptide toxin isolated from Bu...
Gespeichert in:
| Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2010-03, Vol.31 (3), p.412-418 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 418 |
|---|---|
| container_issue | 3 |
| container_start_page | 412 |
| container_title | Peptides (New York, N.Y. : 1980) |
| container_volume | 31 |
| creator | Salceda, Emilio López, Omar Zaharenko, André J. Garateix, Anoland Soto, Enrique |
| description | Sea anemone toxins bind to site 3 of the sodium channels, which is partially formed by the extracellular linker connecting S3 and S4 segments of domain IV, slowing down the inactivation process. In this work we have characterized the actions of BcIII, a sea anemone polypeptide toxin isolated from
Bunodosoma caissarum, on neuronal sodium currents using the patch clamp technique. Neurons of the dorsal root ganglia of Wistar rats (P5–9) in primary culture were used for this study (
n
=
65). The main effects of BcIII were a concentration-dependent increase in the sodium current inactivation time course (IC
50
=
2.8
μM) as well as an increase in the current peak amplitude. BcIII did not modify the voltage at which 50% of the channels are activated or inactivated, nor the reversal potential of sodium current. BcIII shows a voltage-dependent action. A progressive acceleration of sodium current fast inactivation with longer conditioning pulses was observed, which was steeper as more depolarizing were the prepulses. The same was observed for other two anemone toxins (CgNa, from
Condylactis gigantea and ATX-II, from
Anemonia viridis). These results suggest that the binding affinity of sea anemone toxins may be reduced in a voltage-dependent manner, as has been described for α-scorpion toxins. |
| doi_str_mv | 10.1016/j.peptides.2009.12.005 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_745635978</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0196978109005257</els_id><sourcerecordid>745635978</sourcerecordid><originalsourceid>FETCH-LOGICAL-c447t-1c0f2b9ea0f7c66cbb4fba63e860408648f61e231787fde5fb35529bb0fdc96b3</originalsourceid><addsrcrecordid>eNqFkc1u1DAUhS0EokPhFSrvWCXYSewkO2jFz0iV2JS15djXg4fEDr5OVd6Ix8Sjadl2ZVn6zj3S-Qi54qzmjMsPx3qFNXsLWDeMjTVvasbEC7LjQ99WgsvxJdkxPspq7Ad-Qd4gHhljXTcOr8lFiXDRiXFH_t79BIqgqQ6wxAD0egvRRoyLpkZ7RJ22heb44AO9Nvv9ni7RbrPOgDSfotH6ApgtJQiZ_vIBsjdIo6NJZ2pjQj3TFGOmBx0Os9c0wJZiwNJoqUdqPa6zNlA-gWp6H-esD1BZWCHY081FhwDpLXnl9Izw7vG9JD--fL67-Vbdfv-6v_l0W5mu63PFDXPNNIJmrjdSmmnq3KRlC4NkHRtkNzjJoWl5P_TOgnBTK0QzThNz1oxyai_J-_PdNcXfG2BWi0cD81wGihuqvhOyFWXU58m2Fe3QNLyQ8kyaFBETOLUmv-j0R3GmTjrVUT3pVCedijeq6CzBq8eKbVrA_o89-SvAxzMAZZJ7D0mh8RDKmj6BycpG_1zHP_D9uIU</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>733538221</pqid></control><display><type>article</type><title>The sea anemone Bunodosoma caissarum toxin BcIII modulates the sodium current kinetics of rat dorsal root ganglia neurons and is displaced in a voltage-dependent manner</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Salceda, Emilio ; López, Omar ; Zaharenko, André J. ; Garateix, Anoland ; Soto, Enrique</creator><creatorcontrib>Salceda, Emilio ; López, Omar ; Zaharenko, André J. ; Garateix, Anoland ; Soto, Enrique</creatorcontrib><description>Sea anemone toxins bind to site 3 of the sodium channels, which is partially formed by the extracellular linker connecting S3 and S4 segments of domain IV, slowing down the inactivation process. In this work we have characterized the actions of BcIII, a sea anemone polypeptide toxin isolated from
Bunodosoma caissarum, on neuronal sodium currents using the patch clamp technique. Neurons of the dorsal root ganglia of Wistar rats (P5–9) in primary culture were used for this study (
n
=
65). The main effects of BcIII were a concentration-dependent increase in the sodium current inactivation time course (IC
50
=
2.8
μM) as well as an increase in the current peak amplitude. BcIII did not modify the voltage at which 50% of the channels are activated or inactivated, nor the reversal potential of sodium current. BcIII shows a voltage-dependent action. A progressive acceleration of sodium current fast inactivation with longer conditioning pulses was observed, which was steeper as more depolarizing were the prepulses. The same was observed for other two anemone toxins (CgNa, from
Condylactis gigantea and ATX-II, from
Anemonia viridis). These results suggest that the binding affinity of sea anemone toxins may be reduced in a voltage-dependent manner, as has been described for α-scorpion toxins.</description><identifier>ISSN: 0196-9781</identifier><identifier>EISSN: 1873-5169</identifier><identifier>DOI: 10.1016/j.peptides.2009.12.005</identifier><identifier>PMID: 20015459</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Anemonia viridis ; Animals ; ATX-II ; Bunodosoma caissarum ; Cells, Cultured ; CgNa ; Cnidarian Venoms - chemistry ; Cnidarian Venoms - pharmacology ; Condylactis gigantea ; Electrophysiology ; Fast inactivation ; Ganglia, Spinal - cytology ; Molecular Sequence Data ; Neurons - drug effects ; Neurons - metabolism ; Neurotoxins ; Rats ; Rats, Wistar ; Sequence Homology, Amino Acid ; Site-3 toxins ; Sodium - metabolism ; Sodium Channels - drug effects ; Voltage-gated sodium channels</subject><ispartof>Peptides (New York, N.Y. : 1980), 2010-03, Vol.31 (3), p.412-418</ispartof><rights>2009 Elsevier Inc.</rights><rights>(c) 2009 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c447t-1c0f2b9ea0f7c66cbb4fba63e860408648f61e231787fde5fb35529bb0fdc96b3</citedby><cites>FETCH-LOGICAL-c447t-1c0f2b9ea0f7c66cbb4fba63e860408648f61e231787fde5fb35529bb0fdc96b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0196978109005257$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20015459$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Salceda, Emilio</creatorcontrib><creatorcontrib>López, Omar</creatorcontrib><creatorcontrib>Zaharenko, André J.</creatorcontrib><creatorcontrib>Garateix, Anoland</creatorcontrib><creatorcontrib>Soto, Enrique</creatorcontrib><title>The sea anemone Bunodosoma caissarum toxin BcIII modulates the sodium current kinetics of rat dorsal root ganglia neurons and is displaced in a voltage-dependent manner</title><title>Peptides (New York, N.Y. : 1980)</title><addtitle>Peptides</addtitle><description>Sea anemone toxins bind to site 3 of the sodium channels, which is partially formed by the extracellular linker connecting S3 and S4 segments of domain IV, slowing down the inactivation process. In this work we have characterized the actions of BcIII, a sea anemone polypeptide toxin isolated from
Bunodosoma caissarum, on neuronal sodium currents using the patch clamp technique. Neurons of the dorsal root ganglia of Wistar rats (P5–9) in primary culture were used for this study (
n
=
65). The main effects of BcIII were a concentration-dependent increase in the sodium current inactivation time course (IC
50
=
2.8
μM) as well as an increase in the current peak amplitude. BcIII did not modify the voltage at which 50% of the channels are activated or inactivated, nor the reversal potential of sodium current. BcIII shows a voltage-dependent action. A progressive acceleration of sodium current fast inactivation with longer conditioning pulses was observed, which was steeper as more depolarizing were the prepulses. The same was observed for other two anemone toxins (CgNa, from
Condylactis gigantea and ATX-II, from
Anemonia viridis). These results suggest that the binding affinity of sea anemone toxins may be reduced in a voltage-dependent manner, as has been described for α-scorpion toxins.</description><subject>Amino Acid Sequence</subject><subject>Anemonia viridis</subject><subject>Animals</subject><subject>ATX-II</subject><subject>Bunodosoma caissarum</subject><subject>Cells, Cultured</subject><subject>CgNa</subject><subject>Cnidarian Venoms - chemistry</subject><subject>Cnidarian Venoms - pharmacology</subject><subject>Condylactis gigantea</subject><subject>Electrophysiology</subject><subject>Fast inactivation</subject><subject>Ganglia, Spinal - cytology</subject><subject>Molecular Sequence Data</subject><subject>Neurons - drug effects</subject><subject>Neurons - metabolism</subject><subject>Neurotoxins</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Sequence Homology, Amino Acid</subject><subject>Site-3 toxins</subject><subject>Sodium - metabolism</subject><subject>Sodium Channels - drug effects</subject><subject>Voltage-gated sodium channels</subject><issn>0196-9781</issn><issn>1873-5169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhS0EokPhFSrvWCXYSewkO2jFz0iV2JS15djXg4fEDr5OVd6Ix8Sjadl2ZVn6zj3S-Qi54qzmjMsPx3qFNXsLWDeMjTVvasbEC7LjQ99WgsvxJdkxPspq7Ad-Qd4gHhljXTcOr8lFiXDRiXFH_t79BIqgqQ6wxAD0egvRRoyLpkZ7RJ22heb44AO9Nvv9ni7RbrPOgDSfotH6ApgtJQiZ_vIBsjdIo6NJZ2pjQj3TFGOmBx0Os9c0wJZiwNJoqUdqPa6zNlA-gWp6H-esD1BZWCHY081FhwDpLXnl9Izw7vG9JD--fL67-Vbdfv-6v_l0W5mu63PFDXPNNIJmrjdSmmnq3KRlC4NkHRtkNzjJoWl5P_TOgnBTK0QzThNz1oxyai_J-_PdNcXfG2BWi0cD81wGihuqvhOyFWXU58m2Fe3QNLyQ8kyaFBETOLUmv-j0R3GmTjrVUT3pVCedijeq6CzBq8eKbVrA_o89-SvAxzMAZZJ7D0mh8RDKmj6BycpG_1zHP_D9uIU</recordid><startdate>20100301</startdate><enddate>20100301</enddate><creator>Salceda, Emilio</creator><creator>López, Omar</creator><creator>Zaharenko, André J.</creator><creator>Garateix, Anoland</creator><creator>Soto, Enrique</creator><general>Elsevier Inc</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><scope>7TK</scope><scope>7U7</scope><scope>C1K</scope></search><sort><creationdate>20100301</creationdate><title>The sea anemone Bunodosoma caissarum toxin BcIII modulates the sodium current kinetics of rat dorsal root ganglia neurons and is displaced in a voltage-dependent manner</title><author>Salceda, Emilio ; López, Omar ; Zaharenko, André J. ; Garateix, Anoland ; Soto, Enrique</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c447t-1c0f2b9ea0f7c66cbb4fba63e860408648f61e231787fde5fb35529bb0fdc96b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Sequence</topic><topic>Anemonia viridis</topic><topic>Animals</topic><topic>ATX-II</topic><topic>Bunodosoma caissarum</topic><topic>Cells, Cultured</topic><topic>CgNa</topic><topic>Cnidarian Venoms - chemistry</topic><topic>Cnidarian Venoms - pharmacology</topic><topic>Condylactis gigantea</topic><topic>Electrophysiology</topic><topic>Fast inactivation</topic><topic>Ganglia, Spinal - cytology</topic><topic>Molecular Sequence Data</topic><topic>Neurons - drug effects</topic><topic>Neurons - metabolism</topic><topic>Neurotoxins</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Sequence Homology, Amino Acid</topic><topic>Site-3 toxins</topic><topic>Sodium - metabolism</topic><topic>Sodium Channels - drug effects</topic><topic>Voltage-gated sodium channels</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Salceda, Emilio</creatorcontrib><creatorcontrib>López, Omar</creatorcontrib><creatorcontrib>Zaharenko, André J.</creatorcontrib><creatorcontrib>Garateix, Anoland</creatorcontrib><creatorcontrib>Soto, Enrique</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><collection>Neurosciences Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Peptides (New York, N.Y. : 1980)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Salceda, Emilio</au><au>López, Omar</au><au>Zaharenko, André J.</au><au>Garateix, Anoland</au><au>Soto, Enrique</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The sea anemone Bunodosoma caissarum toxin BcIII modulates the sodium current kinetics of rat dorsal root ganglia neurons and is displaced in a voltage-dependent manner</atitle><jtitle>Peptides (New York, N.Y. : 1980)</jtitle><addtitle>Peptides</addtitle><date>2010-03-01</date><risdate>2010</risdate><volume>31</volume><issue>3</issue><spage>412</spage><epage>418</epage><pages>412-418</pages><issn>0196-9781</issn><eissn>1873-5169</eissn><abstract>Sea anemone toxins bind to site 3 of the sodium channels, which is partially formed by the extracellular linker connecting S3 and S4 segments of domain IV, slowing down the inactivation process. In this work we have characterized the actions of BcIII, a sea anemone polypeptide toxin isolated from
Bunodosoma caissarum, on neuronal sodium currents using the patch clamp technique. Neurons of the dorsal root ganglia of Wistar rats (P5–9) in primary culture were used for this study (
n
=
65). The main effects of BcIII were a concentration-dependent increase in the sodium current inactivation time course (IC
50
=
2.8
μM) as well as an increase in the current peak amplitude. BcIII did not modify the voltage at which 50% of the channels are activated or inactivated, nor the reversal potential of sodium current. BcIII shows a voltage-dependent action. A progressive acceleration of sodium current fast inactivation with longer conditioning pulses was observed, which was steeper as more depolarizing were the prepulses. The same was observed for other two anemone toxins (CgNa, from
Condylactis gigantea and ATX-II, from
Anemonia viridis). These results suggest that the binding affinity of sea anemone toxins may be reduced in a voltage-dependent manner, as has been described for α-scorpion toxins.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>20015459</pmid><doi>10.1016/j.peptides.2009.12.005</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0196-9781 |
| ispartof | Peptides (New York, N.Y. : 1980), 2010-03, Vol.31 (3), p.412-418 |
| issn | 0196-9781 1873-5169 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_745635978 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Sequence Anemonia viridis Animals ATX-II Bunodosoma caissarum Cells, Cultured CgNa Cnidarian Venoms - chemistry Cnidarian Venoms - pharmacology Condylactis gigantea Electrophysiology Fast inactivation Ganglia, Spinal - cytology Molecular Sequence Data Neurons - drug effects Neurons - metabolism Neurotoxins Rats Rats, Wistar Sequence Homology, Amino Acid Site-3 toxins Sodium - metabolism Sodium Channels - drug effects Voltage-gated sodium channels |
| title | The sea anemone Bunodosoma caissarum toxin BcIII modulates the sodium current kinetics of rat dorsal root ganglia neurons and is displaced in a voltage-dependent manner |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-24T20%3A48%3A30IST&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=The%20sea%20anemone%20Bunodosoma%20caissarum%20toxin%20BcIII%20modulates%20the%20sodium%20current%20kinetics%20of%20rat%20dorsal%20root%20ganglia%20neurons%20and%20is%20displaced%20in%20a%20voltage-dependent%20manner&rft.jtitle=Peptides%20(New%20York,%20N.Y.%20:%201980)&rft.au=Salceda,%20Emilio&rft.date=2010-03-01&rft.volume=31&rft.issue=3&rft.spage=412&rft.epage=418&rft.pages=412-418&rft.issn=0196-9781&rft.eissn=1873-5169&rft_id=info:doi/10.1016/j.peptides.2009.12.005&rft_dat=%3Cproquest_cross%3E745635978%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=733538221&rft_id=info:pmid/20015459&rft_els_id=S0196978109005257&rfr_iscdi=true |