Location of a ligand recognition site of FMRFamide‐gated Na+ channels
The second FMRFamide‐gated Na+ channel (HtFaNaC), from Helisoma trivolvis, has been cloned. HtFaNaC has some different pharmacological properties to HaFaNaC, from Helix aspersa, which has enabled a rational approach to be made to start to identify the FMRFamide recognition site. Several chimeras wer...
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| Veröffentlicht in: | FEBS letters 2001-01, Vol.489 (1), p.71-74 |
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| creator | Cottrell, G.A. Jeziorski, M.C. Green, K.A. |
| description | The second FMRFamide‐gated Na+ channel (HtFaNaC), from Helisoma trivolvis, has been cloned. HtFaNaC has some different pharmacological properties to HaFaNaC, from Helix aspersa, which has enabled a rational approach to be made to start to identify the FMRFamide recognition site. Several chimeras were made by switching sections between the channels. The differences in sensitivity to FMRFamide, and amiloride, were assessed after expression in Xenopus oocytes. The data suggest that a recognition site for FMRFamide, and the potentiating action of amiloride, resides in a sequence of about 120 amino acids in the extracellular loop proximal to the first transmembrane segment. |
| doi_str_mv | 10.1016/S0014-5793(01)02081-6 |
| format | Article |
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HtFaNaC has some different pharmacological properties to HaFaNaC, from Helix aspersa, which has enabled a rational approach to be made to start to identify the FMRFamide recognition site. Several chimeras were made by switching sections between the channels. The differences in sensitivity to FMRFamide, and amiloride, were assessed after expression in Xenopus oocytes. 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HtFaNaC has some different pharmacological properties to HaFaNaC, from Helix aspersa, which has enabled a rational approach to be made to start to identify the FMRFamide recognition site. Several chimeras were made by switching sections between the channels. The differences in sensitivity to FMRFamide, and amiloride, were assessed after expression in Xenopus oocytes. The data suggest that a recognition site for FMRFamide, and the potentiating action of amiloride, resides in a sequence of about 120 amino acids in the extracellular loop proximal to the first transmembrane segment.</description><subject>Amiloride</subject><subject>Amiloride - pharmacology</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>ASIC, acid-sensing ion channel</subject><subject>Binding Sites</subject><subject>Diuretics - pharmacology</subject><subject>Electrophysiology</subject><subject>ENaC, epithelial sodium channel</subject><subject>FaNaC</subject><subject>FMRFamide - pharmacology</subject><subject>FMRFamide recognition</subject><subject>FMRFamide, Phe-Met-Arg-Phe-NH2</subject><subject>Molecular Sequence Data</subject><subject>Mollusca - metabolism</subject><subject>Na+ channel</subject><subject>Na+, sodium ion</subject><subject>Oocytes</subject><subject>PCR, polymerase chain reaction</subject><subject>Recombinant Fusion Proteins - drug effects</subject><subject>Recombinant Fusion Proteins - physiology</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sodium Channels - drug effects</subject><subject>Sodium Channels - genetics</subject><subject>Sodium Channels - physiology</subject><subject>TM, transmembrane</subject><subject>Transfection</subject><subject>Xenopus laevis</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1OwzAQhS0EoqVwBFBWCIQC4zgZO0uomhapgMTP2nIdpxjlp8StUHccgTNyEpK0gi2r0cz75tnzCDmmcEmB4tUTAA39iMfsDOg5BCCojzukTwVnPgtR7JL-L9IjB869QdMLGu-THqUBa136ZDyttFraqvSqzFNebueqTL3a6Gpe2m7u7NK0YnL3mKjCpub782uulib17tWFp19VWZrcHZK9TOXOHG3rgLwko-fhxJ8-jG-H11NfhwzR50JnGk0UQMSDKBa8aQ1iGKpIBykXAkTzZ5ayGeWUgUY-45ChzoBhqgPBBuR047uoq_eVcUtZWKdNnqvSVCsnOcaIKFow2oC6rpyrTSYXtS1UvZYUZHu77BKUbTwSqOwSlNjsnWwfWM0Kk_5tbSNrgMkG-LC5Wf_PVSajm6BTWgFoN0b2A_SJfnk</recordid><startdate>20010126</startdate><enddate>20010126</enddate><creator>Cottrell, G.A.</creator><creator>Jeziorski, M.C.</creator><creator>Green, K.A.</creator><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>20010126</creationdate><title>Location of a ligand recognition site of FMRFamide‐gated Na+ channels</title><author>Cottrell, G.A. ; Jeziorski, M.C. ; Green, K.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4366-78cfc6e5205725987cfce6644a5c2d788080143d3b17130c67b70f6cf036dc283</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amiloride</topic><topic>Amiloride - pharmacology</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>ASIC, acid-sensing ion channel</topic><topic>Binding Sites</topic><topic>Diuretics - pharmacology</topic><topic>Electrophysiology</topic><topic>ENaC, epithelial sodium channel</topic><topic>FaNaC</topic><topic>FMRFamide - pharmacology</topic><topic>FMRFamide recognition</topic><topic>FMRFamide, Phe-Met-Arg-Phe-NH2</topic><topic>Molecular Sequence Data</topic><topic>Mollusca - metabolism</topic><topic>Na+ channel</topic><topic>Na+, sodium ion</topic><topic>Oocytes</topic><topic>PCR, polymerase chain reaction</topic><topic>Recombinant Fusion Proteins - drug effects</topic><topic>Recombinant Fusion Proteins - physiology</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sodium Channels - drug effects</topic><topic>Sodium Channels - genetics</topic><topic>Sodium Channels - physiology</topic><topic>TM, transmembrane</topic><topic>Transfection</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cottrell, G.A.</creatorcontrib><creatorcontrib>Jeziorski, M.C.</creatorcontrib><creatorcontrib>Green, K.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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cottrell, G.A.</au><au>Jeziorski, M.C.</au><au>Green, K.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Location of a ligand recognition site of FMRFamide‐gated Na+ channels</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2001-01-26</date><risdate>2001</risdate><volume>489</volume><issue>1</issue><spage>71</spage><epage>74</epage><pages>71-74</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The second FMRFamide‐gated Na+ channel (HtFaNaC), from Helisoma trivolvis, has been cloned. HtFaNaC has some different pharmacological properties to HaFaNaC, from Helix aspersa, which has enabled a rational approach to be made to start to identify the FMRFamide recognition site. Several chimeras were made by switching sections between the channels. The differences in sensitivity to FMRFamide, and amiloride, were assessed after expression in Xenopus oocytes. The data suggest that a recognition site for FMRFamide, and the potentiating action of amiloride, resides in a sequence of about 120 amino acids in the extracellular loop proximal to the first transmembrane segment.</abstract><cop>England</cop><pmid>11231016</pmid><doi>10.1016/S0014-5793(01)02081-6</doi><tpages>4</tpages></addata></record> |
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| ispartof | FEBS letters, 2001-01, Vol.489 (1), p.71-74 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | Wiley Free Content; MEDLINE; Elsevier ScienceDirect Journals Complete; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amiloride Amiloride - pharmacology Amino Acid Sequence Animals ASIC, acid-sensing ion channel Binding Sites Diuretics - pharmacology Electrophysiology ENaC, epithelial sodium channel FaNaC FMRFamide - pharmacology FMRFamide recognition FMRFamide, Phe-Met-Arg-Phe-NH2 Molecular Sequence Data Mollusca - metabolism Na+ channel Na+, sodium ion Oocytes PCR, polymerase chain reaction Recombinant Fusion Proteins - drug effects Recombinant Fusion Proteins - physiology Sequence Homology, Amino Acid Sodium Channels - drug effects Sodium Channels - genetics Sodium Channels - physiology TM, transmembrane Transfection Xenopus laevis |
| title | Location of a ligand recognition site of FMRFamide‐gated Na+ channels |
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