Aquaporin 2
Aquaporin 2 - Related Videos
04:21
An Assay to Detect Serum Anti-aquaporin-4 Immunoglobulin G
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2025
The video demonstrates a cell-based assay for detecting anti-aquaporin-4 immunoglobulin G using a biochip containing untransfected cells and transfected cells expressing aquaporin-4. This method has applications in diagnosing neuromyelitis optica spectrum disorders, confirmed by strong green fluorescence on the biochip.
01:25
Aquaporins
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2023
Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.
01:56
Inducing Paralysis in a Mouse Model via Transfer of Aquaporin-4-Specific Th17 Cells
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2025
This video demonstrates the procedure of inducing paralysis by transferring activated Th17 cells targeting aquaporin-4 into a mouse model. In the central nervous system, the activated Th17 cells interact with aquaporin-4-expressing astrocytes, triggering an immune response that leads to tail and limb paralysis in the mouse.
09:29
Induction of Paralysis and Visual System Injury in Mice by T Cells Specific for Neuromyelitis Optica Autoantigen Aquaporin-4
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Cited by 10 •
2017
Here, we present a protocol to induce paralysis and opticospinal inflammation by transfer of aquaporin-4 (AQP4)-specific T cells from AQP4-/- mice into WT mice. In addition, we demonstrate how to use serial optical coherence tomography to monitor visual system dysfunction.
05:45
Human Serum Anti-aquaporin-4 Immunoglobulin G Detection by Cell-based Assay
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Cited by 5 •
2019
Cell-based assay is a widely used method to detect serum anti-aquaporin-4 immunoglobulin G. This method could be applied to clinical diagnosis and scientific researches of neuromyelitis optical spectrum disorders.
FAQs
An increase in blood osmolality triggers vasopressin binding to receptors on collecting-duct cells. The resulting cAMP-dependent signaling promotes phosphorylation of AQP2, a regulatory modification associated here with its insertion into the apical membrane. This relocation increases the cell’s capacity to admit water from the tubular side, linking hormonal detection to altered epithelial water permeability.
Water entering through AQP2 at the apical surface is only the first step. Other aquaporins on the basolateral surface provide the exit route from collecting-duct cells, allowing water to move onward rather than accumulate inside the epithelium. Considering both membrane surfaces is therefore essential when interpreting how this pathway supports urinary concentration and systemic fluid regulation.
The pathway is activated when blood osmolality rises, a condition indicating a need to conserve water. Vasopressin-driven AQP2 insertion then increases water entry into collecting-duct cells, while basolateral aquaporins permit onward movement. The resulting increase in water recovery helps concentrate urine and contributes to maintaining blood volume, connecting a local epithelial response with whole-body homeostasis.
Different defects can disrupt different stages of the same regulatory pathway. Reduced AQP2 expression limits the available channel, impaired trafficking can prevent appropriate membrane insertion, and altered channel function can interfere with water movement even when the protein is present. These failures are associated with nephrogenic diabetes insipidus and help distinguish disease mechanisms.
Researchers can use AQP2 to connect molecular regulation with renal physiology and disease. A study may follow how increased osmolality, vasopressin signaling, phosphorylation, and membrane insertion relate to water movement, urine concentration, and blood volume. This framework is especially relevant when investigating nephrogenic diabetes insipidus caused by defects in AQP2 expression, trafficking, or function.
Analysis should proceed from the initiating condition to the physiological outcome: assess the rise in blood osmolality, vasopressin receptor activation, cAMP-dependent signaling, AQP2 phosphorylation and apical insertion, water entry, and basolateral exit through other aquaporins. Following this order helps identify where a defect interrupts the pathway and how that interruption affects urine concentration.