Related Experiment Video

Updated: Oct 6, 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 is a binding partner for the myelin-associated glycoprotein (siglec-4a)

K Strenge1, R Brossmer, P Ihrig

  • 1Institute of Biochemistry, University of Kiel, Germany. kstrenge@biochem.uni-kiel.de

FEBS Letters
|June 26, 2001
PubMed

Insights

Researchers identified fibronectin as a binding partner for the myelin-associated glycoprotein (MAG). This interaction, crucial for cell communication in the nervous system, changes during development.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • The myelin-associated glycoprotein (MAG) is vital for cell-cell interactions between neurons and myelinating glial cells.
  • Understanding MAG's molecular interactions is key to deciphering neural development and function.

Purpose of the Study:

  • To identify novel binding partners of the myelin-associated glycoprotein (MAG).
  • To investigate the role of fibronectin in MAG-mediated cellular interactions.

Main Methods:

  • Affinity precipitation using MAG-Fc from NG108-15 cells.
  • Protein microsequencing to identify MAG-binding proteins.
  • Western blot analysis to confirm fibronectin presence in various neural tissues.
  • Isolation of fibronectin isoforms from rat brains at different developmental stages.

Main Results:

  • Fibronectin was identified as a direct binding partner of MAG.
  • Fibronectin was confirmed to be present in MAG-binding complexes from neuronal and glial cell lines, as well as brain and spinal cord tissues.
  • Distinct fibronectin isoforms were found in young and adult rat brains, suggesting developmental regulation.

Conclusions:

  • Fibronectin is a novel extracellular matrix binding partner of MAG.
  • The interaction between MAG and fibronectin may play a significant role in neural development and function.
  • Developmental changes in fibronectin expression highlight its dynamic role in the nervous system.

More Related Videos

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study11:10

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study

Published on: June 29, 2016

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...
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...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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...
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,...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...