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Related Concept Videos

Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

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...
Fibrous Proteins00:55

Fibrous Proteins

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...
Fibril-associated Collagen01:11

Fibril-associated Collagen

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...
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
Integrins01:10

Integrins

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,...
Introduction to Fibroblasts01:09

Introduction to Fibroblasts

Rudolph Virchow discovered spindle-shaped cells called fibroblasts in 1858. Inactive fibroblasts, called fibrocytes, become activated by various stimuli, such as growth factors and inflammatory cytokines. Activated fibroblasts play a crucial role in wound healing, inflammation, formation of new blood vessels, and cancer progression. Uncontrolled activation of fibroblasts results in fibrosis, the excess deposition of fibrous tissue, which can lead to scarring and affect normal organs. This...

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Related Experiment Video

Updated: Jul 10, 2026

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

[Fibronectin--a multifunctional glycoprotein].

S Mitrović, D Mitrović, V Todorović

    Srpski Arhiv Za Celokupno Lekarstvo
    |July 1, 1995
    PubMed
    Summary
    This summary is machine-generated.

    Fibronectin, a glycoprotein, is vital for biological processes like embryogenesis and immune defense. Its distinct cellular and plasma forms have unique roles in tissue repair and bodily defense mechanisms.

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    ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
    16:33

    ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly

    Published on: April 17, 2014

    Related Experiment Videos

    Last Updated: Jul 10, 2026

    Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
    11:13

    Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

    Published on: August 20, 2018

    ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
    16:33

    ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly

    Published on: April 17, 2014

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Context:

    • Fibronectin is a crucial glycoprotein involved in numerous biological processes.
    • It exists in distinct plasma and cellular forms with unique structural and functional characteristics.
    • Cellular fibronectin contains ED1 and ED2 domains absent in plasma fibronectin.

    Purpose:

    • To elucidate the structural and functional distinctions between plasma and cellular fibronectin.
    • To highlight the roles of fibronectin in key biological processes such as embryogenesis, wound healing, immune defense, and hemostasis.

    Summary:

    • Fibronectin is a high molecular weight glycoprotein (440-530 kD) composed of two disulfide-bridged subunits.
    • It features binding sites for cell surface integrins (e.g., RGDS, CS1) and various macromolecules like fibrin and heparin.
    • Cellular fibronectin contributes to the extracellular matrix and basal membranes, essential for tissue modeling and repair.
    • Plasma fibronectin plays a significant role in immune defense, surveillance, and hemostasis.

    Impact:

    • Provides a comprehensive overview of fibronectin's diverse biological functions.
    • Underscores the importance of fibronectin in developmental processes and tissue homeostasis.
    • Enhances understanding of fibronectin's contribution to immune responses and blood clotting mechanisms.