Aquaporin-2 Translocation
Aquaporin-2 Translocation - Related Videos
04:21
An Assay to Detect Serum Anti-aquaporin-4 Immunoglobulin G
0 Views •
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
0 Views •
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
0 Views •
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.
12:27
Measuring Peptide Translocation into Large Unilamellar Vesicles
0 Views •
Cited by 9 •
2012
This protocol details a method for the quantitative measure of peptide translocation into large unilamellar lipid vesicles. This method also provides information about the rate of membrane translocation and can be used to identify peptides that efficiently and spontaneously cross lipid bilayers.
10:33
Efficient Purification and LC-MS/MS-based Assay Development for Ten-Eleven Translocation-2 5-Methylcytosine Dioxygenase
0 Views •
Cited by 5 •
2018
Here, we present a protocol for an efficient single step purification of the active untagged human ten-eleven translocation-2 (TET2) 5-methylcytosine dioxygenase using ion-exchange chromatography and its assay using a liquid chromatography-tandem mass spectrometry (LC-MS/MS)-based approach.
FAQs
When blood osmolality rises, vasopressin binds V2 receptors on kidney collecting-duct cells. This activates adenylate cyclase, raises intracellular cAMP, and stimulates protein kinase A. The kinase-dependent signal coordinates aquaporin-2 phosphorylation with movement of channel-containing intracellular vesicles toward the apical membrane, linking an osmotic stimulus to a rapid change in epithelial water permeability.
Phosphorylation serves as a regulatory step that helps promote aquaporin-2 trafficking from intracellular vesicles to the plasma membrane. Increasing the number of channels at the apical surface allows collecting-duct cells to become more permeable to water. This rapid membrane response supports urine concentration rather than relying only on slower changes in channel production.
Diabetes insipidus can result when vasopressin signaling is disrupted, aquaporin-2 trafficking fails, or the channel itself does not function properly. Each defect interferes with the normal increase in collecting-duct water permeability, limiting water conservation and impairing urine concentration. Comparing these failure points helps distinguish signaling problems from trafficking or channel-function abnormalities.
By increasing water permeability in collecting-duct cells, the pathway supports concentration of urine and conservation of body water. These effects contribute to fluid balance and also influence blood-pressure regulation. Because the response follows changes in blood osmolality, it provides a mechanism for adjusting renal water handling to the body's hydration-related needs.
The collecting duct is the renal site where regulated aquaporin-2 delivery changes epithelial water permeability. Its cells therefore connect hormonal signaling with the final handling of water before urine leaves the kidney. Studying this location clarifies how vasopressin-dependent membrane trafficking contributes to whole-body fluid regulation and why pathway defects have renal consequences.
Therapeutic research can focus on the linked stages that determine aquaporin-2 availability at the apical membrane: vasopressin binding to the V2 receptor, adenylate cyclase activation, cAMP production, protein kinase A signaling, phosphorylation, vesicle insertion, and channel function. Examining these components may help explain or address disorders in which water conservation and urine concentration are impaired.