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

Reabsorption and Secretion in the DCT and Collecting Duct

938
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...
938
Membrane Proteins01:30

Membrane Proteins

18.4K
Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
18.4K
Pore Transport and Ion-Pair Transport01:17

Pore Transport and Ion-Pair Transport

389
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...
389
Facilitated Transport01:19

Facilitated Transport

11.3K
The chemical and physical properties of plasma membranes cause them to be selectively permeable. Since plasma membranes have both hydrophobic and hydrophilic regions, substances need to be able to transverse both regions. The hydrophobic area of membranes repels substances such as charged ions. Therefore, such substances need special membrane proteins to cross a membrane successfully. In  facilitated transport, also known as facilitated diffusion, molecules and ions travel across a...
11.3K
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

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Related Experiment Video

Updated: Jun 11, 2025

Measuring the Osmotic Water Permeability Coefficient Pf of Spherical Cells: Isolated Plant Protoplasts as an Example
14:20

Measuring the Osmotic Water Permeability Coefficient Pf of Spherical Cells: Isolated Plant Protoplasts as an Example

Published on: October 8, 2014

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Heme-based aquareceptors

Savani Anbalagan1

  • 1Instytut Biologii Molekularnej i Biotechnologii, Wydział Biologii, Uniwersytet im. Adama Mickiewicza w Poznaniu.

Postepy Biochemii
|October 4, 2024
PubMed
Summary

Cells may sense water using protein aquareceptors, similar to gasoreceptors. These aquareceptors could be widespread, functioning in various cellular locations and potentially including hemoglobin.

Area of Science:

  • Cell biology
  • Biochemistry
  • Physiology

Background:

  • Cellular water sensing (hygrosensation) is crucial for life, yet mechanisms remain unclear.
  • Existing osmosensors detect solute concentration, not water directly.
  • Water-sensing evolved to aid survival and multicellularity.

Purpose of the Study:

  • To propose a novel mechanism for cellular water sensing.
  • To identify potential protein structures involved in water detection.

Main Methods:

  • Hypothesizing a role for gasoreceptors as aquareceptors based on structural similarities.
  • Extending the proposed function to various cellular compartments.

Main Results:

  • Suggests gas-binding sites in heme-based gasoreceptors could bind water molecules.

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Culturing Primary Rat Inner Medullary Collecting Duct Cells
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Culturing Primary Rat Inner Medullary Collecting Duct Cells

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Human Serum Anti-aquaporin-4 Immunoglobulin G Detection by Cell-based Assay
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Human Serum Anti-aquaporin-4 Immunoglobulin G Detection by Cell-based Assay

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Related Experiment Videos

Last Updated: Jun 11, 2025

Measuring the Osmotic Water Permeability Coefficient Pf of Spherical Cells: Isolated Plant Protoplasts as an Example
14:20

Measuring the Osmotic Water Permeability Coefficient Pf of Spherical Cells: Isolated Plant Protoplasts as an Example

Published on: October 8, 2014

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Culturing Primary Rat Inner Medullary Collecting Duct Cells
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Culturing Primary Rat Inner Medullary Collecting Duct Cells

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Human Serum Anti-aquaporin-4 Immunoglobulin G Detection by Cell-based Assay
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Human Serum Anti-aquaporin-4 Immunoglobulin G Detection by Cell-based Assay

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  • Proposes that these proteins function as aquareceptors in nearly all cells.
  • Hypothesizes aquareceptors are located in membranes, cytoplasm, and organelles.

    • Conclusions:

    • Gasoreceptors may possess a dual function as aquareceptors.
    • A wide distribution of aquareceptors is predicted across cellular structures.
    • Hemoglobin is considered a potential aquareceptor candidate.