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Aquaporins

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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.

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Thermosensation

Thermosensation

Peripheral thermosensation is the perception of external temperature. A change in temperature (on the surface of the skin and other tissues) is detected by a family of temperature-sensitive ion channels called Transient Receptor Potential, or TRP, receptors. These receptors are located on free nerve endings. Those detecting cold temperatures are closer to the surface of the skin than the nerve endings detecting warmth. These thermoTRP channels, while temperature selective, have relatively...

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Related Experiment Video

Updated: May 29, 2026

Culturing Primary Rat Inner Medullary Collecting Duct Cells

Culturing Primary Rat Inner Medullary Collecting Duct Cells

Published on: June 21, 2013

Functional interaction between AQP2 and TRPV4 in renal cells.

Luciano Galizia¹, Alejandro Pizzoni, Juan Fernandez

¹Laboratorio de Biomembranas, Departamento de Fisiología y Biofísica, Facultad de Medicina, Universidad de Buenos Aires, Buenos Aires, Argentina.

Journal of Cellular Biochemistry

|September 23, 2011

Summary

Renal cortical collecting duct cells activate regulatory volume decrease (RVD) via calcium influx. This study reveals aquaporin-2 (AQP2) is crucial for hypotonicity-induced TRPV4 channel activation, essential for RVD.

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Published on: June 27, 2015

Area of Science:

Cell Biology
Physiology
Molecular Biology

Background:

Renal cortical collecting duct cells (RCCD(1)) exhibit regulatory volume decrease (RVD) under hypotonic stress.
This RVD requires aquaporin-2 (AQP2) and calcium influx, but the calcium entry pathway remains unclear.

Purpose of the Study:

To investigate if the calcium permeable channel TRPV4 mediates hypotonicity-induced calcium influx and RVD in RCCD(1) cells.
To determine the role of AQP2 in the activation and function of TRPV4 during osmotic stress.

Main Methods:

Evaluating TRPV4 expression and function in wild-type RCCD(1) and AQP2-transfected RCCD(1) cells.
Assessing calcium influx and RVD using pharmacological inhibitors like ruthenium red.
Analyzing TRPV4 localization via membrane translocation studies.

Main Results:

Both wild-type and AQP2-transfected RCCD(1) cells express functional TRPV4.
Hypotonicity significantly activates TRPV4 only in AQP2-expressing cells, leading to calcium influx and RVD.
TRPV4 inhibition abolishes calcium influx and RVD, highlighting its necessity.
TRPV4 translocation to the plasma membrane is essential for this process.

Conclusions:

TRPV4 is a key component of the calcium entry pathway mediating RVD in response to hypotonic stress in renal collecting duct cells.
AQP2 is critical for the hypotonicity-induced activation of TRPV4, suggesting a novel functional association.
AQP2 and TRPV4 may form a signaling complex that regulates cellular responses to osmotic challenges.