Cited 0 times in
Amino acid residues involved in agonist binding and its linking to channel gating, proximal to transmembrane domain of 5-HT3A receptor for halothane modulation
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 민경태 | - |
dc.contributor.author | 구본녀 | - |
dc.date.accessioned | 2015-04-24T16:22:01Z | - |
dc.date.available | 2015-04-24T16:22:01Z | - |
dc.date.issued | 2009 | - |
dc.identifier.issn | 2005-6419 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/103394 | - |
dc.description.abstract | BACKGROUND: The 5-hydroxytryptamine type 3 (5-HT3) receptor is a member of the Cys-loop superfamily of ligand-gated ion channels (LGICs) and modulated by pharmacologic relevant concentrations of volatile anesthetics or n-alcohols like most receptors of LGICs. The goal of this study was to reveal whether the site-directed single mutations of E-106, F-107 and R-222 in 5-HT3 receptor may affect the anesthetic modulation of halothane known as positive modulator. METHODS: The wild-type and mutant receptors, E106D, F107Y, R222F, R222V, were expressed in Xenopus Laevis oocytes and receptor function was assessed using two electrode voltage clamp techniques. RESULTS: E106D, F107Y, R222F, R222V mutant 5-HT3A receptors were functionally expressed. F107Y mutant 5-HT3A receptors displayed decreased sensitivity to 5-HT compared to the wild type 5-HT3A receptor (P < 0.05). Halothane showed positive modulation in both wild and F107Y mutant 5-HT3A receptors but F107Y mutant 5-HT3 receptor showed greater enhancing modulation comparing to wild-type receptor. Meanwhile, R222F and R222V mutant 5-HT3 receptor lost positive modulation with 1 and 2 MAC of halothane. Most interestingly, positive modulation by halothane was converted into negative modulation in E106D mutant 5-HT3A receptor. CONCLUSIONS: The present study implicate the amino acid residues known for agonist binding and linking agonist binding to channel gating might also have important role for anesthetic modulation in 5-HT3A receptor | - |
dc.description.statementOfResponsibility | open | - |
dc.format.extent | 66~73 | - |
dc.relation.isPartOf | KOREAN JOURNAL OF ANESTHESIOLOGY | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/2.0/kr/ | - |
dc.title | Amino acid residues involved in agonist binding and its linking to channel gating, proximal to transmembrane domain of 5-HT3A receptor for halothane modulation | - |
dc.type | Article | - |
dc.contributor.college | College of Medicine (의과대학) | - |
dc.contributor.department | Dept. of Anesthesiology (마취통증의학) | - |
dc.contributor.googleauthor | Mi Kyeong Kim | - |
dc.contributor.googleauthor | Kyeong Tae Min | - |
dc.contributor.googleauthor | Bon Nyeo Koo | - |
dc.admin.author | false | - |
dc.admin.mapping | false | - |
dc.contributor.localId | A01400 | - |
dc.contributor.localId | A00193 | - |
dc.relation.journalcode | J01963 | - |
dc.identifier.eissn | 2005-7563 | - |
dc.subject.keyword | Transitional cell carcinoma | - |
dc.subject.keyword | In situ hybridization | - |
dc.subject.keyword | fluorescence | - |
dc.subject.keyword | Nuclear matrix protein 22 | - |
dc.contributor.alternativeName | Min, Kyeong Tae | - |
dc.contributor.alternativeName | Ku, Bon Nyo | - |
dc.contributor.affiliatedAuthor | Min, Kyeong Tae | - |
dc.contributor.affiliatedAuthor | Ku, Bon Nyo | - |
dc.citation.volume | 56 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 66 | - |
dc.citation.endPage | 73 | - |
dc.identifier.bibliographicCitation | KOREAN JOURNAL OF ANESTHESIOLOGY, Vol.56(1) : 66-73, 2009 | - |
dc.identifier.rimsid | 37313 | - |
dc.type.rims | ART | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.