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Tight Junctions

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...

Overview of Cell-Cell Junctions

Overview of Cell-Cell Junctions

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 Junctions
Tight...

Overview of Cell-Cell Junctions

Overview of Cell-Cell Junctions

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 Junctions
Tight...

Anchoring Junctions

Anchoring Junctions

Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...

Membrane Domains

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...

Gap Junctions

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...

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Related Experiment Video

Updated: Jun 22, 2026

An Intravital Microscopy-Based Approach to Assess Intestinal Permeability and Epithelial Cell Shedding Performance

An Intravital Microscopy-Based Approach to Assess Intestinal Permeability and Epithelial Cell Shedding Performance

Published on: December 3, 2020

Slit diaphragms contain tight junction proteins.

Hirotaka Fukasawa¹, Scott Bornheimer, Krystyna Kudlicka

¹Department of Cellular and Molecular Medicine, University of California San Diego, 9500 Gilman Drive, La Jolla, California 92093-0651, USA.

Journal of the American Society of Nephrology : JASN

|May 30, 2009

Summary

Glomerular slit diaphragms, crucial for kidney filtration, contain tight junction proteins like JAM-A, occludin, and cingulin. These proteins are implicated in proteinuric diseases and their function in slit diaphragms requires further study.

Related Experiment Videos

Last Updated: Jun 22, 2026

An Intravital Microscopy-Based Approach to Assess Intestinal Permeability and Epithelial Cell Shedding Performance

An Intravital Microscopy-Based Approach to Assess Intestinal Permeability and Epithelial Cell Shedding Performance

Published on: December 3, 2020

Area of Science:

Nephrology
Cell Biology
Molecular Biology

Background:

Slit diaphragms are vital for kidney filtration and are altered in proteinuric diseases.
They are considered specialized adherens junctions with known unique and typical junctional proteins.
The presence of tight junction proteins in slit diaphragms was previously unknown.

Purpose of the Study:

To investigate the presence and role of tight junction proteins within the glomerular slit diaphragm.
To determine if proteins like JAM-A, occludin, and cingulin are components of the slit diaphragm.
To examine changes in these proteins during disease states like PAN nephrosis.

Main Methods:

Immunofluorescence and immunogold labeling to localize proteins.
Cell fractionation to isolate cellular components.
Cosedimentation, coimmunoprecipitation, and pull-down assays to analyze protein complexes.
Quantitative analysis of protein levels in disease models (PAN nephrosis).

Main Results:

Rat slit diaphragms were confirmed to contain tight junction proteins: junctional adhesion molecule A (JAM-A), occludin, and cingulin.
These tight junction proteins were found in complexes with known slit diaphragm proteins (nephrin, podocin, CD2AP, ZO-1, Neph1).
Protein levels of JAM-A, occludin, cingulin, and ZO-1 significantly increased in glomeruli affected by PAN nephrosis, with altered cytoskeletal attachment.

Conclusions:

Slit diaphragms contain tight junction proteins, expanding the understanding of their molecular composition.
Despite containing these proteins, slit diaphragms do not exhibit the typical morphology of tight junctions.
The findings suggest a potential role for these tight junction proteins in slit diaphragm assembly and signaling, warranting further research.