Interestingly, we show in this report that upon heteromer formation with SCTR, R137H, a NDI-causing AVPR2 mutant that is defective in trafficking to cell surface, can functionally be rescued.
In addition to the functional significance of the conserved cysteine residues, we have also analyzed the defects of two mutant V2 receptors which cause X-linked nephrogenic diabetes insipidus (NDI) by the introduction of additional cysteine residues into the second extracellular loop (mutants G185C, R202C).
In addition to the functional significance of the conserved cysteine residues, we have also analyzed the defects of two mutant V2 receptors which cause X-linked nephrogenic diabetes insipidus (NDI) by the introduction of additional cysteine residues into the second extracellular loop (mutants G185C, R202C).
To date, only three AVPR2 mutations (P322S, D85N, and G201D) have been associated with a mild NDI phenotype, and intrafamilial phenotype variability has not been reported in affected males.
To date, only three AVPR2 mutations (P322S, D85N, and G201D) have been associated with a mild NDI phenotype, and intrafamilial phenotype variability has not been reported in affected males.
Genetic testing for the nephronophthisis came back negative but was positive for a missense mutation in the AVPR2 gene (p.Arg104Cys) associated with partial nephrogenic diabetes insipidus.He was started on daily desmopressin.
Genetic testing for the nephronophthisis came back negative but was positive for a missense mutation in the AVPR2 gene (p.Arg104Cys) associated with partial nephrogenic diabetes insipidus.He was started on daily desmopressin.
Mother and child were found to have the previously characterised activating mutation (p.Arg137Cys) of the arginine vasopressin receptor type 2 gene (AVPR2), but had measurable levels of AVP when hyponatraemic.
In addition to the functional significance of the conserved cysteine residues, we have also analyzed the defects of two mutant V2 receptors which cause X-linked nephrogenic diabetes insipidus (NDI) by the introduction of additional cysteine residues into the second extracellular loop (mutants G185C, R202C).