Related Experiment Video
Updated: Apr 11, 2026

07:55
Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads
Published on: March 8, 2017
9.0K
Tenascin-C: Its functions as an integrin ligand
Richard P Tucker1, Ruth Chiquet-Ehrismann2
1Department of Cell Biology and Human Anatomy, University of California at Davis, 1 Shields Avenue, Davis, CA 95616, USA.
The International Journal of Biochemistry & Cell Biology
|June 10, 2015
Summary
Tenascin-C interacts with specific integrins, influencing cell behavior like proliferation and differentiation. This knowledge holds potential for stem cell therapies.
Area of Science:
- Biochemistry
- Cell Biology
- Regenerative Medicine
Background:
- Tenascin-C is a key extracellular matrix protein involved in cell adhesion and migration.
- Integrins are cell surface receptors that mediate cell-matrix and cell-cell interactions.
Purpose of the Study:
- To review experimental evidence on tenascin-C and integrin interactions.
- To identify integrin binding sites on tenascin-C.
- To understand the impact of these interactions on cell behavior.
Main Methods:
- Literature review of experimental studies on tenascin-C/integrin interactions.
- Analysis of identified integrin binding sites and motifs (IDG, RGD).
- Summary of observed cellular responses to tenascin-C/integrin binding.
Main Results:
- Four integrins (α9β1, αVβ3, α8β1, αVβ6) bind to tenascin-C's third fibronectin type III domain.
- α9β1 recognizes an IDG motif; others recognize an RGD motif.
- Tenascin-C interactions with integrins promote cell proliferation, inhibit apoptosis, and influence stem cell differentiation.
Conclusions:
- Specific tenascin-C/integrin interactions modulate critical cellular functions.
- Understanding these interactions is crucial for developing targeted therapies.
- Potential applications exist in stem cell-based therapies, particularly for neuronal differentiation.
Related Concept Videos
Integrins
6.2K
Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
6.2K
Intracellular Signaling Affects Focal Adhesions
3.8K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Some...
3.8K
Activation of Integrins
5.6K
Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
5.6K
Catenins
3.3K
Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the...
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the...
3.3K
Tension Response at Adherens Junctions
4.3K
The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...
4.3K
Fibronectins Connect Cells with ECM
3.8K
Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
3.8K

