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• W1992854118 abstract "AVPR2 variants and V2 vasopressin receptor function in nephrogenic diabetes insipidus.BackgroundThe AVPR2 gene encodes the type 2 vasopressin receptor, a member of the vasopressin/oxytocin receptor subfamily of G protein-coupled receptors. Disruption of AVPR2 causes X-linked congenital nephrogenic diabetes insipidus (NDI), yet the functional significance of most gene sequence variations found in association with NDI has not been proven. The large number of naturally occurring AVPR2 mutations constitutes a model system for studying the structure-function relationship of G protein-coupled receptors. This analysis can be aided by examining amino acid sequence variation and conservation among evolutionarily disparate members of the subfamily.MethodsTwenty-five new NDI patients were evaluated by DNA sequencing for mutations in AVPR2. Receptors encoded by eighteen NDI alleles were tested for physiologic signaling activity in response to varying concentrations of arginine vasopressin (AVP) in a sensitive cell culture assay. Seventeen amino acid sequences from the vasopressin/oxytocin receptor subfamily were aligned and conserved residues were identified and correlated with the locations of NDI associated variations.ResultsTwenty-four variant alleles were found among the 25 new patients. Thirteen had no prior family history of expressed NDI. All 18 of the NDI-associated AVPR2 alleles tested for function demonstrated diminished response to stimulation with AVP. Twelve failed to respond at all, whereas six signaled only at high AVP concentrations. Evolutionarily conserved residues clustered in the transmembrane domains and in the first and second extracellular loops, and NDI-associated missense mutations appeared mostly in the conserved domains.ConclusionsSporadic cases are frequent and they usually represent the X-linked rather than the autosomal form of NDI. Genetic and functional testing can confirm this in individual cases. Mutations in this study affecting ligand binding domains tend to retain partial signaling in vitro, whereas those that introduce a charged residue in a transmembrane domain are inactive. The minimal partial signaling observed in cultured cells is unlikely to correlate with clinically significant urine concentrating ability. Other AVPR2 mutations with milder effects on receptor function probably exist, but may not be expressed clinically as typical NDI. AVPR2 variants and V2 vasopressin receptor function in nephrogenic diabetes insipidus. The AVPR2 gene encodes the type 2 vasopressin receptor, a member of the vasopressin/oxytocin receptor subfamily of G protein-coupled receptors. Disruption of AVPR2 causes X-linked congenital nephrogenic diabetes insipidus (NDI), yet the functional significance of most gene sequence variations found in association with NDI has not been proven. The large number of naturally occurring AVPR2 mutations constitutes a model system for studying the structure-function relationship of G protein-coupled receptors. This analysis can be aided by examining amino acid sequence variation and conservation among evolutionarily disparate members of the subfamily. Twenty-five new NDI patients were evaluated by DNA sequencing for mutations in AVPR2. Receptors encoded by eighteen NDI alleles were tested for physiologic signaling activity in response to varying concentrations of arginine vasopressin (AVP) in a sensitive cell culture assay. Seventeen amino acid sequences from the vasopressin/oxytocin receptor subfamily were aligned and conserved residues were identified and correlated with the locations of NDI associated variations. Twenty-four variant alleles were found among the 25 new patients. Thirteen had no prior family history of expressed NDI. All 18 of the NDI-associated AVPR2 alleles tested for function demonstrated diminished response to stimulation with AVP. Twelve failed to respond at all, whereas six signaled only at high AVP concentrations. Evolutionarily conserved residues clustered in the transmembrane domains and in the first and second extracellular loops, and NDI-associated missense mutations appeared mostly in the conserved domains. Sporadic cases are frequent and they usually represent the X-linked rather than the autosomal form of NDI. Genetic and functional testing can confirm this in individual cases. Mutations in this study affecting ligand binding domains tend to retain partial signaling in vitro, whereas those that introduce a charged residue in a transmembrane domain are inactive. The minimal partial signaling observed in cultured cells is unlikely to correlate with clinically significant urine concentrating ability. Other AVPR2 mutations with milder effects on receptor function probably exist, but may not be expressed clinically as typical NDI." @default.
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• W1992854118 date "1998-01-01" @default.
• W1992854118 modified "2023-09-26" @default.
• W1992854118 title "AVPR2 variants and V2 vasopressin receptor function in nephrogenic diabetes insipidus" @default.
• W1992854118 cites W1495947004 @default.
• W1992854118 cites W1600839161 @default.
• W1992854118 cites W1974370292 @default.
• W1992854118 cites W1986662318 @default.
• W1992854118 cites W1993005963 @default.
• W1992854118 cites W2005825986 @default.
• W1992854118 cites W2006793024 @default.
• W1992854118 cites W2010838245 @default.
• W1992854118 cites W2011067926 @default.
• W1992854118 cites W2017641415 @default.
• W1992854118 cites W2023166473 @default.
• W1992854118 cites W2023254642 @default.
• W1992854118 cites W2031495245 @default.
• W1992854118 cites W2042173717 @default.
• W1992854118 cites W2044098020 @default.
• W1992854118 cites W2054212035 @default.
• W1992854118 cites W2055120442 @default.
• W1992854118 cites W2058948801 @default.
• W1992854118 cites W2060920066 @default.
• W1992854118 cites W2062250423 @default.
• W1992854118 cites W2064546838 @default.
• W1992854118 cites W2071226874 @default.
• W1992854118 cites W2079126167 @default.
• W1992854118 cites W2082802847 @default.
• W1992854118 cites W2091614241 @default.
• W1992854118 cites W2103844900 @default.
• W1992854118 cites W2109030204 @default.
• W1992854118 cites W2111052083 @default.
• W1992854118 cites W2114935719 @default.
• W1992854118 cites W2124009791 @default.
• W1992854118 cites W2131706912 @default.
• W1992854118 cites W2133981789 @default.
• W1992854118 cites W2145382725 @default.
• W1992854118 cites W2152954179 @default.
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• W1992854118 cites W2337080608 @default.
• W1992854118 cites W263812101 @default.
• W1992854118 cites W4249572021 @default.
• W1992854118 doi "https://doi.org/10.1046/j.1523-1755.1998.00214.x" @default.
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