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Related Concept Videos

Tight Junctions01:29

Tight Junctions

6.1K
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...
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Overview of Cell-Cell Junctions01:14

Overview of Cell-Cell Junctions

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The complex three-dimensional arrangement of cells in any multicellular organism is defined and maintained by interactions of cells with each other and the extracellular matrix. Cell-cell junctions are specialized structures where the multi-protein complexes on one cell interact with the multi-protein complexes on another  cell. These cell junctions are classified  into three main types based on their function — occluding, anchoring, and gap junctions.
Occluding or Tight...
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Adherens Junctions01:24

Adherens Junctions

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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
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Patch Clamp01:18

Patch Clamp

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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...
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Overview of Cell-Matrix Interactions01:24

Overview of Cell-Matrix Interactions

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The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
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Related Experiment Video

Updated: Nov 3, 2025

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

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Chimeric Claudins: A New Tool to Study Tight Junction Structure and Function.

Abigail Taylor1, Mark Warner1, Christopher Mendoza1

  • 1Department of Physiology and Developmental Biology, College of Life Sciences, Brigham Young University, Provo, UT 84602, USA.

International Journal of Molecular Sciences
|June 2, 2021
PubMed
Summary
This summary is machine-generated.

Researchers engineered soluble chimeric claudins (CLDNs) to study their structure and function. This novel approach provides insights into cell-cell adhesion and blood-tissue barrier mechanisms.

Keywords:
E-cadherinclaudinmembrane proteinoccludintight junction

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Tight junctions (TJs) are crucial for cell-cell adhesion in epithelial and endothelial cells.
  • Claudins (CLDNs) are key transmembrane proteins forming the paracellular barrier, essential for blood-tissue integrity.
  • Existing structural data for CLDNs derived from detergent-extracted recombinant proteins lack evidence for their native quaternary structure.

Purpose of the Study:

  • To engineer and characterize detergent-independent chimeric CLDNs (MBP-CCs) to investigate their structure and function.
  • To provide biophysical evidence supporting the quaternary structure of CLDNs.
  • To establish a novel protein-engineering strategy applicable to other 4-α-helix membrane proteins.

Main Methods:

  • Protein engineering to create chimeric proteins by fusing maltose-binding protein (MBP) with the extracellular domain of human CLDN1.
  • Utilizing a soluble 4-helix bundle protein (PDB ID: 2jua) as a fusion partner.
  • Biophysical characterization of the resulting MBP-fused chimeric CLDNs (MBP-CCs).
  • Employing MBP-fused epithelial cadherin (MBP-eCAD) as a control.

Main Results:

  • Successfully generated soluble MBP-CCs that retain structural and functional characteristics of native CLDNs.
  • Provided biophysical characterization of the structure and function of these novel chimeric proteins.
  • Demonstrated the utility of this protein-engineering approach for studying membrane proteins.

Conclusions:

  • The developed chimeric CLDNs (MBP-CCs) offer a valuable tool for studying CLDN structure and function in a detergent-free system.
  • This strategy overcomes limitations of previous structural studies and provides insights into quaternary structure.
  • The synthetic approach is potentially applicable to a broader range of 4-α-helix membrane proteins, advancing their study.