ArticleInternational journal of molecular sciences2016
Disruption of Membranes of Extracellular Vesicles Is Necessary for ELISA Determination of Urine AQP2: Proof of Disruption and Epitopes of AQP2 Antibodies.
Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Identification and verification of exosome-related gene signature to predict the cancer status and prognosis of prostate cancer.Discover oncology · 2025Article
- Bioinformatics tools and data resources for assay development of fluid protein biomarkers.Biomarker research · 2022Review
- Circulating extracellular vesicles and rheumatoid arthritis: a proteomic analysis.Cellular and molecular life sciences : CMLS · 2021Review
- Article
- Characterization of extracellular redox enzyme concentrations in response to exercise in humans.Journal of applied physiology (Bethesda, Md. : 1985) · 2019Article
- Alteration of exosomes secreted from renal tubular epithelial cells exposed to high-concentration oxalate.Oncotarget · 2017Article
- The role of the secretin/secretin receptor axis in inflammatory cholangiocyte communication via extracellular vesicles.Scientific reports · 2017Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporin-2 (AQP2) is present in urine extracellular vesicles (EVs) and is a useful biomarker for water balance disorders. We previously found that pre-treatment of urine with alkali/detergent or storage at -25 °C is required for enzyme-linked immunosorbent assay (ELISA) measurement. We speculated that disruptions of EVs membranes are necessary to allow for the direct contact of antibodies with their epitopes. Human urine EVs were prepared using an ultracentrifugation method. Urine EV samples were stored at different temperatures for a week. Electron microscopy showed abundant EVs with diameters of 20-100 nm, consistent with those of exosomes, in normal urine, whereas samples from alkali/detergent pre-treated urine showed fewer EVs with large swollen shapes and frequent membrane disruptions. The abundance and structures of EVs were maintained during storage at -80 °C, but were severely damaged at -25 °C. Binding and competitive inhibition assays showed that epitopes of monoclonal antibody and polyclonal antibody were the hydrophilic Loop D and C-terminus of AQP2, respectively, both of which are present on the inner surface of EVs. Thus, urine storage at -25 °C or pre-treatment with alkali/detergent disrupt EVs membranes and allow AQP2 antibodies to bind to their epitopes located inside EVs.
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