Related Experiment Video
Updated: May 3, 2026
16:33
ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
Published on: April 17, 2014
11.7K
Molecular interactions of fibronectin
Progress in Clinical and Biological Research
|January 1, 1980
Summary
Fibronectin is crucial for cell attachment, interacting with collagen, fibrinogen, and cell surface receptors. Its binding sites are distinct, influencing extracellular matrix formation and potentially cancer cell matrix disturbances.
Area of Science:
- Biochemistry
- Cell Biology
- Extracellular Matrix Research
Background:
- Fibronectin mediates cell attachment in vitro and in vivo.
- It interacts with collagen, fibrinogen, glycosaminoglycans, and cell surface receptors.
- Fibronectin's role in the extracellular matrix is significant, especially in relation to malignant cells.
Purpose of the Study:
- To investigate the molecular interactions of fibronectin.
- To identify the binding sites of fibronectin for various macromolecules.
- To understand the implications of fibronectin's interactions in extracellular matrix formation.
Main Methods:
- Analysis of fibronectin's binding activities with collagen, fibrinogen, and glycosaminoglycans.
- Characterization of fibronectin fragments to localize binding sites.
- Comparison of binding affinities for native and denatured collagens.
Main Results:
- Fibronectin binds to collagen, fibrinogen, glycosaminoglycans, and cell/bacterial surface receptors.
- Collagen and fibrinogen share overlapping binding sites on fibronectin.
- A 30,000 MW fragment of fibronectin binds collagen, while other fragments bind cells and Staphylococci.
- Glycosaminoglycans stabilize collagen-fibronectin complexes.
Conclusions:
- Fibronectin's distinct binding sites mediate interactions with multiple macromolecules.
- These interactions are critical for extracellular matrix formation.
- Further research is needed to understand fibronectin's role in matrix disturbances by malignant cells.
Related Concept Videos
01:56Structural Protein Function
28.9K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
28.9K
01:11Fibril-associated Collagen
2.7K
Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
2.7K
01:25Fibronectins Connect Cells with ECM
2.9K
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...
2.9K
01:24Overview of Cell-Matrix Interactions
8.0K
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...
8.0K
01:17Intracellular Signaling Affects Focal Adhesions
2.8K
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...
2.8K
00:55Fibrous Proteins
3.9K
Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
3.9K