Search results for "Aquaporin 2"
showing 3 items of 3 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…
Expression of Human Ubiquitous Aquaporins in Chorial Villus Samples
2011
Background/objectives: Aquaporins (AQPs) are a family of proteins (AQP0-12) ubiquitously expressed acting as cell membrane water channels. AQP 1/3/8/9 expression has been found in human placenta and fetal membranes; however, AQP4 is the only identified in first trimester fetal tissue samples. We aimed to determine AQP mRNA expression in first trimester of pregnancy and compare it to the expression in placenta at delivery. Material and Methods: 26 Chorionic villus (CV) samples and 5 placental samples were collected and analyzed by real time-PCR using Taqman assay (Applied Biosystems®) for human AQP1, 2, 3, 4, 5, 6, 7, 8, 9, 11 and 18S. Results: CV expressed high mRNA levels of AQP1, 3, 9 and…
2015
Several point mutations have been identified in human aquaporins, but their effects on the function of the respective aquaporins are mostly enigmatic. We analyzed the impact of the aquaporin 2 mutation V71M, which causes nephrogenic diabetes insipidus in humans, on aquaporin structure and activity, using the bacterial aquaglyceroporin GlpF as a model. Importantly, the sequence and structure around the V71M mutation is highly conserved between aquaporin 2 and GlpF. The V71M mutation neither impairs substrate flux nor oligomerization of the aquaglyceroporin. Therefore, the human aquaporin 2 mutant V71M is most likely active, but cellular trafficking is probably impaired.