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Related Concept Videos

Tight Junctions01:29

Tight Junctions

Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...
Gap Junctions01:27

Gap Junctions

The cytoplasm of adjacent animal cells can exchange small molecules, ions, and secondary messengers via the communication channels which form the gap junctions. These junctions comprise a few hundred to thousands of molecular channels, each made of two halves, called the connexon hemichannel. A connexon is a hexamer of six transmembrane connexin proteins, which assemble radially, thus forming a pore or channel in the center. One connexon hemichannel docks with a corresponding connexon on the...
Gap Junctions01:37

Gap Junctions

Multicellular organisms employ a variety of ways for cells to communicate with each other. Gap junctions are specialized proteins that form pores between neighboring cells in animals, connecting the cytoplasm between the two, and allowing for the exchange of molecules and ions. They are found in a wide range of invertebrate and vertebrate species, mediate numerous functions including cell differentiation and development, and are associated with numerous human diseases, including cardiac and...
Adherens Junctions01:24

Adherens Junctions

Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
The endothelial cells...
Patch Clamp01:18

Patch Clamp

Many fundamental cell functions such as muscle contraction and nerve transmission rely on the electrical signals produced by the movement of positively and negatively charged ions across the cell membrane. One competent method to record current flowing across the whole cell or single ion channel is the patch-clamp technique.
In this method, a glass micropipette containing electrolyte solution is tightly sealed against a small portion of the cell membrane. As a result, a patch of the cell...
Non-gated Ion Channels01:24

Non-gated Ion Channels

Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism.

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Related Experiment Video

Updated: May 24, 2026

Functional Assessment of Intestinal Tight Junction Barrier and Ion Permeability in Native Tissue by Ussing Chamber Technique
06:43

Functional Assessment of Intestinal Tight Junction Barrier and Ion Permeability in Native Tissue by Ussing Chamber Technique

Published on: May 26, 2021

Claudin-17 forms tight junction channels with distinct anion selectivity.

Susanne M Krug1, Dorothee Günzel, Marcel P Conrad

  • 1Institute of Clinical Physiology, Campus Benjamin Franklin, Charité, Freie Universität and Humboldt Universität, Hindenburgdamm 30, 12203 Berlin, Germany.

Cellular and Molecular Life Sciences : CMLS
|March 10, 2012
PubMed
Summary

Claudin-17 protein forms anion-selective channels in the kidney

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Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands
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Last Updated: May 24, 2026

Functional Assessment of Intestinal Tight Junction Barrier and Ion Permeability in Native Tissue by Ussing Chamber Technique
06:43

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Published on: May 26, 2021

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07:47

A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters

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Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands
11:31

Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands

Published on: May 30, 2017

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Physiology

Background:

  • Tight junctions, crucial for cellular barriers, are regulated by claudin proteins.
  • While some claudins seal barriers, others form paracellular channels, but anion-selective claudins remain poorly defined.
  • Claudin-17's function and distribution were previously unknown.

Purpose of the Study:

  • To characterize the function and tissue distribution of claudin-17.
  • To determine if claudin-17 forms anion-selective paracellular channels.
  • To investigate the molecular basis of claudin-17's ion selectivity.

Main Methods:

  • Overexpression and knockdown of claudin-17 in renal cell lines (MDCK C7 and LLC-PK(1)).
  • Measurement of paracellular ion permeability and selectivity.
  • Site-directed mutagenesis to identify key residues for ion selectivity.

Main Results:

  • Overexpression of claudin-17 significantly increased paracellular anion permeability and shifted selectivity from cation- to anion-selective.
  • Knockdown experiments confirmed claudin-17's role in forming anion channels.
  • A positive charge at position 65 was critical for claudin-17's anion selectivity.
  • Claudin-17 is abundantly expressed in the kidney's proximal tubules.

Conclusions:

  • Claudin-17 forms distinct anion-selective channels within tight junctions.
  • Claudin-17 is likely involved in paracellular chloride reabsorption in the proximal nephron.
  • This study identifies claudin-17 as a key player in renal anion transport.