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Related Concept Videos

Aquaporins01:25

Aquaporins

4.8K
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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Reabsorption and Secretion in the DCT and Collecting Duct01:26

Reabsorption and Secretion in the DCT and Collecting Duct

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The early phase of the DCT manages the reabsorption of approximately 10-15% of filtered water, 5–10% of filtered sodium, and 5–10% of filtered chloride. This process is facilitated by Na+–Cl− symporters in apical membranes and sodium-potassium pumps, as well as Cl− leakage channels in basolateral membranes. The early DCT also stands out as a site where parathyroid hormone (PTH) stimulates calcium reabsorption, depending on the body's requirements.
The distal...
943
Pore Transport and Ion-Pair Transport01:17

Pore Transport and Ion-Pair Transport

399
Pore transport and ion-pair formation are critical mechanisms for the absorption and distribution of drugs in the body.
Pore transport, also known as convective transport, is a process where small molecules like urea, water, and sugars rapidly cross cell membranes as though there were channels or pores in the membrane. Although direct microscopic evidence is limited  but the concept of pores or channels is widely accepted based on physiological evidence. Despite the lack of direct...
399
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

8.0K
ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and...
8.0K
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

3.6K
V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
3.6K
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

2.2K
Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
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Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies
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Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies

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Aquaporin Modulation by Cations, a Review.

Robin Mom1, Vincent Mocquet1, Daniel Auguin2

  • 1Laboratoire de Biologie et Modelisation de la Cellule, Ecole Normale Superieure de Lyon, CNRS, UMR 5239, Inserm, U1293, Universite Claude Bernard Lyon 1, 46 allee d'Italie, F-69364 Lyon, France.

Current Issues in Molecular Biology
|August 28, 2024
PubMed
Summary

Aquaporins (AQPs) facilitate water transport but also interact with various solutes. This review explores how cations modulate AQP function, revealing insights into their complex regulatory network for potential therapeutic applications.

Keywords:
AQPcalciumcationmercuryregulations

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Membrane Transport

Background:

  • Aquaporins (AQPs) are critical transmembrane channels for water transport.
  • Their functions extend beyond water, involving diverse solutes and complex regulatory networks.
  • AQPs are therapeutic targets for diseases like cancer, but precise modulation remains challenging.

Purpose of the Study:

  • To review known cation modulations of aquaporin function.
  • To elucidate the molecular mechanisms underlying cation-AQP interactions.
  • To identify trends in AQP regulation by cations.

Main Methods:

  • Comprehensive literature review of aquaporin-cation interactions.
  • Analysis of molecular mechanisms and binding sites.
  • Identification of key residues involved in cation modulation.

Main Results:

  • Cations significantly modulate AQP activity, with historical links to mercury inhibition.
  • Specific molecular mechanisms and residues involved in cation binding and conformational changes were identified.
  • A preliminary overview of the cation-mediated AQP regulatory network was established.

Conclusions:

  • Cation modulation is a key aspect of aquaporin regulation.
  • Understanding these interactions is crucial for developing isoform-specific AQP modulators.
  • This review provides a foundation for future research into AQP-targeted therapies.