195 217

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 FieldValueLanguage
dc.contributor.author민경태-
dc.contributor.author구본녀-
dc.date.accessioned2015-04-24T16:22:01Z-
dc.date.available2015-04-24T16:22:01Z-
dc.date.issued2009-
dc.identifier.issn2005-6419-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/103394-
dc.description.abstractBACKGROUND: 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.statementOfResponsibilityopen-
dc.format.extent66~73-
dc.relation.isPartOfKOREAN JOURNAL OF ANESTHESIOLOGY-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.titleAmino acid residues involved in agonist binding and its linking to channel gating, proximal to transmembrane domain of 5-HT3A receptor for halothane modulation-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine (의과대학)-
dc.contributor.departmentDept. of Anesthesiology (마취통증의학)-
dc.contributor.googleauthorMi Kyeong Kim-
dc.contributor.googleauthorKyeong Tae Min-
dc.contributor.googleauthorBon Nyeo Koo-
dc.admin.authorfalse-
dc.admin.mappingfalse-
dc.contributor.localIdA01400-
dc.contributor.localIdA00193-
dc.relation.journalcodeJ01963-
dc.identifier.eissn2005-7563-
dc.subject.keywordTransitional cell carcinoma-
dc.subject.keywordIn situ hybridization-
dc.subject.keywordfluorescence-
dc.subject.keywordNuclear matrix protein 22-
dc.contributor.alternativeNameMin, Kyeong Tae-
dc.contributor.alternativeNameKu, Bon Nyo-
dc.contributor.affiliatedAuthorMin, Kyeong Tae-
dc.contributor.affiliatedAuthorKu, Bon Nyo-
dc.citation.volume56-
dc.citation.number1-
dc.citation.startPage66-
dc.citation.endPage73-
dc.identifier.bibliographicCitationKOREAN JOURNAL OF ANESTHESIOLOGY, Vol.56(1) : 66-73, 2009-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Anesthesiology and Pain Medicine (마취통증의학교실) > 1. Journal Papers

qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.