Matches in SemOpenAlex for { <https://semopenalex.org/work/W1998996859> ?p ?o ?g. }
Showing items 1 to 85 of
85
with 100 items per page.
- W1998996859 endingPage "775" @default.
- W1998996859 startingPage "767" @default.
- W1998996859 abstract "Sequence alignment shows that there is a highly conserved aspartate in the second transmembrane helix of virtually all G protein-coupled receptors. A previous study on the alpha 2-adrenergic receptor demonstrated that substitution of this acidic residue for the corresponding amide slightly decreases the affinity of the receptor for agonists and completely abolishes the effect of Na+ on the affinity for agonists. Since we have previously shown that Na+ modulates the binding affinity of the LH/CG receptor for ovine LH (oLH) [but not for human CG (hCG)], the experiments described here were designed to determine if the corresponding residue (D383) of the rat LH/CG receptor also mediates this Na+ effect. We used site-directed mutagenesis to create an LH/CG receptor mutant in which D383 was substituted by N. The wild type and mutant receptor [designated rLHR(D383N)] were expressed in human embryonic kidney 293 cells, and the transfected cells were tested for their ability to bind hCG and oLH in medium containing Na+ or an isoosmolar concentration of an appropriate sodium substitute. The results presented here show that this single point mutation of the LH/CG receptor leads to a slight reduction in affinity for hCG and oLH but completely abolishes the effects of Na+ removal on the affinity for oLH. Thus, regardless of the presence or absence of Na+, cells expressing rLHR(D383N) bind oLH with a low affinity comparable to that of the wild type receptor assayed in the presence of Na+. We also measured the ability of hCG and oLH to increase cAMP accumulation in cells expressing the wild type and mutant receptors.(ABSTRACT TRUNCATED AT 250 WORDS)" @default.
- W1998996859 created "2016-06-24" @default.
- W1998996859 creator A5001077804 @default.
- W1998996859 creator A5053376200 @default.
- W1998996859 creator A5089145622 @default.
- W1998996859 date "1993-06-01" @default.
- W1998996859 modified "2023-09-24" @default.
- W1998996859 title "The regulation of the binding affinity of the luteinizing hormone/choriogonadotropin receptor by sodium ions is mediated by a highly conserved aspartate located in the second transmembrane domain of G protein-coupled receptors." @default.
- W1998996859 cites W1489947307 @default.
- W1998996859 cites W1503203225 @default.
- W1998996859 cites W1503983718 @default.
- W1998996859 cites W1539774089 @default.
- W1998996859 cites W1577261117 @default.
- W1998996859 cites W1601441394 @default.
- W1998996859 cites W1806182887 @default.
- W1998996859 cites W1936333617 @default.
- W1998996859 cites W1954929088 @default.
- W1998996859 cites W1984918402 @default.
- W1998996859 cites W1985896961 @default.
- W1998996859 cites W1998591058 @default.
- W1998996859 cites W2007033259 @default.
- W1998996859 cites W2043813981 @default.
- W1998996859 cites W2057129205 @default.
- W1998996859 cites W2058850101 @default.
- W1998996859 cites W2059665365 @default.
- W1998996859 cites W2060913542 @default.
- W1998996859 cites W2093909923 @default.
- W1998996859 cites W2109245267 @default.
- W1998996859 cites W2133002630 @default.
- W1998996859 cites W2138270253 @default.
- W1998996859 cites W2143572454 @default.
- W1998996859 doi "https://doi.org/10.1210/mend.7.6.8395653" @default.
- W1998996859 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8395653" @default.
- W1998996859 hasPublicationYear "1993" @default.
- W1998996859 type Work @default.
- W1998996859 sameAs 1998996859 @default.
- W1998996859 citedByCount "15" @default.
- W1998996859 countsByYear W19989968592016 @default.
- W1998996859 countsByYear W19989968592019 @default.
- W1998996859 countsByYear W19989968592020 @default.
- W1998996859 crossrefType "journal-article" @default.
- W1998996859 hasAuthorship W1998996859A5001077804 @default.
- W1998996859 hasAuthorship W1998996859A5053376200 @default.
- W1998996859 hasAuthorship W1998996859A5089145622 @default.
- W1998996859 hasBestOaLocation W19989968591 @default.
- W1998996859 hasConcept C104317684 @default.
- W1998996859 hasConcept C118892022 @default.
- W1998996859 hasConcept C143065580 @default.
- W1998996859 hasConcept C153911025 @default.
- W1998996859 hasConcept C16318435 @default.
- W1998996859 hasConcept C170493617 @default.
- W1998996859 hasConcept C54009773 @default.
- W1998996859 hasConcept C55493867 @default.
- W1998996859 hasConcept C86803240 @default.
- W1998996859 hasConceptScore W1998996859C104317684 @default.
- W1998996859 hasConceptScore W1998996859C118892022 @default.
- W1998996859 hasConceptScore W1998996859C143065580 @default.
- W1998996859 hasConceptScore W1998996859C153911025 @default.
- W1998996859 hasConceptScore W1998996859C16318435 @default.
- W1998996859 hasConceptScore W1998996859C170493617 @default.
- W1998996859 hasConceptScore W1998996859C54009773 @default.
- W1998996859 hasConceptScore W1998996859C55493867 @default.
- W1998996859 hasConceptScore W1998996859C86803240 @default.
- W1998996859 hasIssue "6" @default.
- W1998996859 hasLocation W19989968591 @default.
- W1998996859 hasLocation W19989968592 @default.
- W1998996859 hasOpenAccess W1998996859 @default.
- W1998996859 hasPrimaryLocation W19989968591 @default.
- W1998996859 hasRelatedWork W1994346428 @default.
- W1998996859 hasRelatedWork W2009464217 @default.
- W1998996859 hasRelatedWork W2015762961 @default.
- W1998996859 hasRelatedWork W2078113843 @default.
- W1998996859 hasRelatedWork W2092726819 @default.
- W1998996859 hasRelatedWork W2271695270 @default.
- W1998996859 hasRelatedWork W2386230503 @default.
- W1998996859 hasRelatedWork W2428581689 @default.
- W1998996859 hasRelatedWork W2911149935 @default.
- W1998996859 hasRelatedWork W4255328563 @default.
- W1998996859 hasVolume "7" @default.
- W1998996859 isParatext "false" @default.
- W1998996859 isRetracted "false" @default.
- W1998996859 magId "1998996859" @default.
- W1998996859 workType "article" @default.