Search results for " Nephrogenic"

showing 5 items of 5 documents

A female with X‐linked Nephrogenic diabetes insipidus in a family with inherited central diabetes Insipidus: Case report and review of the literature

2020

There are two forms of diabetes insipidus, central (neurohypophyseal), and nephrogenic, caused by pathogenic variants in the AVP gene and the AVPR2 or AQP2 genes, respectively. We report on a four-generation family, seven individuals had central diabetes insipidus (CDI) and the female index patient seen from age 16 to 26 years had (mild) nephrogenic diabetes insipidus. In her father with CDI, a known pathogenic heterozygous AVP variant c.232_234del p.(Glu78del) was identified, confirming the diagnosis of CDI in him and the other affected family members. In the proband, molecular analysis disclosed a novel heterozygous AVPR2 gene variant, c.962A > T p.(Asn321Ile) and an extremely skewed X-in…

AdultMaleProbandReceptors Vasopressinmedicine.medical_specialtyAdolescentVasopressinsMutation Missense610 MedizinDiabetes Insipidus NephrogenicYoung AdultGenes X-LinkedX Chromosome Inactivation610 Medical sciencesInternal medicineArginine vasopressin receptor 2Exome SequencingDiabetes MellitusGeneticsmedicineHumansMissense mutationProtein PrecursorsGenetics (clinical)Exome sequencingNeurophysinsAquaporin 2business.industryHeterozygote advantagemedicine.diseaseNephrogenic diabetes insipidusPedigreeDiabetes Insipidus NeurogenicEndocrinologyAquaporin 2Diabetes insipidusFemalebusinessAmerican Journal of Medical Genetics Part A
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Folding and stability of the aquaglyceroporin GlpF: Implications for human aqua(glycero)porin diseases

2015

AbstractAquaporins are highly selective polytopic transmembrane channel proteins that facilitate the permeation of water across cellular membranes in a large diversity of organisms. Defects in aquaporin function are associated with common diseases, such as nephrogenic diabetes insipidus, congenital cataract and certain types of cancer. In general, aquaporins have a highly conserved structure; from prokaryotes to humans. The conserved structure, together with structural dynamics and the structural framework for substrate selectivity is discussed. The folding pathway of aquaporins has been a topic of several studies in recent years. These studies revealed that a conserved protein structure ca…

Models MolecularProtein activityAmino Acid MotifsMolecular Sequence DataBiophysicsGene ExpressionPorinsAquaporinDiabetes Insipidus NephrogenicEndoplasmic-reticulum-associated protein degradationAquaporinsBiochemistryCataractProtein Structure SecondaryProtein structureNeoplasmsEscherichia coliGlpFHumansProtein foldingConserved SequenceProtein StabilityChemistryurogenital systemEscherichia coli ProteinsAquaporinWaterCell BiologyTransmembrane proteinCell biologyFolding (chemistry)Membrane proteinBiochemistryMembrane proteinPorinProtein foldingBiochimica et Biophysica Acta (BBA) - Biomembranes
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Misfolded vasopressin V2 receptors caused by extracellular point mutations entail congenital nephrogenic diabetes insipidus.

2000

Vasopressin V2 receptor mutants from three different patients with congenital nephrogenic diabetes insipidus phenotypes were investigated after expression in COS cells. The amino acid exchanges within the human V2 receptor are located in the second extracellular loop (T204N, Y205C and V206D). Confocal microscopy showed that all receptor mutants were strongly expressed but mainly located within the cell. Residual binding capacity for the antidiuretic hormone arginine vasopressin (AVP) could only be detected for the T204N mutant and was 10-fold lower than for the wild-type receptor. Stimulation of transfected cells with 1 microM AVP showed that the T204N mutant was able to activate the adenyl…

Receptors Vasopressinmedicine.medical_specialtyVasopressinVasopressinsDiabetes Insipidus NephrogenicBiologyTransfectionBiochemistryCell LineEndocrinologyInternal medicineArginine vasopressin receptor 2medicineHumansReceptorMolecular BiologyVasopressin receptorArginine vasopressin receptor 1BElucidation of the molecular defect responsible for congenital nephrogenic diabetes insipidus (NDI)Nephrogenic diabetes insipidusmedicine.diseaseEndocrinologyMutationOpheldering van het moleculaire defect dat verantwoordelijk is voor congenitale nefrogene diabetes insipidus (NDI)cAMP-dependent pathwayhormones hormone substitutes and hormone antagonistsSignal TransductionAntidiuretic
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Indomethacin treatment in amphotericin B induced nephrogenic diabetes insipidus.

1994

Nephrogenic diabetes insipidus (NDI) is a serious side effect of various drugs. Elevated renal prostaglandin E2 levels have been found in patients with lithium-induced NDI and have been implicated in the pathogenesis. We report the case of a patient who developed NDI following treatment with amphotericin B. Prostaglandin levels were elevated. Indomethacin had an antidiuretic effect and normalized prostaglandin levels.

medicine.medical_specialtySide effectVasopressinsIndomethacinProstaglandinDiabetes Insipidus NephrogenicKidneyLeukemia Myelomonocytic AcutePathogenesischemistry.chemical_compoundAmphotericin BInternal medicineAmphotericin BDrug DiscoveryMedicineHumansProstaglandin E2Genetics (clinical)business.industryGeneral MedicineMiddle Agedmedicine.diseaseNephrogenic diabetes insipidusDiuresisEndocrinologychemistryDiabetes insipidusToxicityProstaglandinsTobramycinMolecular Medicinelipids (amino acids peptides and proteins)Femalebusinessmedicine.drugThe Clinical investigator
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The AQP2 mutation V71M causesnephrogenic diabetes insipidus in humans but does not impair the function of a bacterial homolog

2015

Graphical abstract

wt wild-typeGpA glycophorin AHM half-membrane-spanningurogenital systemQH301-705.5AquaporinNephrogenic diabetes insipidusAQP ER endoplasmic reticulumGlpF glycerol facilitatorActivityProtein oligomerizationResearch articleNDI nephrogenic diabetes insipidusAVP arginine vasopressinGlpF500 Natural sciences and mathematicsAQP aquaporin500 NaturwissenschaftenBiology (General)AVPR2 V2 receptorComputingMethodologies_COMPUTERGRAPHICSTM transmembraneFEBS Open Bio
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