Related Experiment Video

Updated: Jun 21, 2026

Rapid and Specific Immunomagnetic Isolation of Mouse Primary Oligodendrocytes
09:32

Rapid and Specific Immunomagnetic Isolation of Mouse Primary Oligodendrocytes

Published on: May 21, 2018

Fibronectin attenuates process outgrowth in oligodendrocytes by mislocalizing MMP-9 activity

Zuzana Sisková1, V Wee Yong, Anita Nomden

  • 1Department of Cell Biology, Section Membrane Cell Biology, University Medical Center Groningen, University of Groningen, 9713 AV Groningen, The Netherlands.

Molecular and Cellular Neurosciences
|July 18, 2009
PubMed

Insights

Fibronectin alters matrix metalloproteinase-9 (MMP-9) activity in oligodendrocytes, affecting their process extension crucial for myelination. This highlights how extracellular matrix molecules regulate oligodendrocyte differentiation.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Oligodendroglial process extension is vital for myelination, requiring extracellular matrix (ECM) remodeling by matrix metalloproteinases (MMPs).
  • The role of specific ECM components like fibronectin in modulating MMP activity and its impact on oligodendrocyte morphology remains unclear.

Purpose of the Study:

  • To investigate the correlation between fibronectin-mediated inhibition of myelin sheet formation and altered MMP activity in oligodendrocytes.
  • To determine how fibronectin influences MMP-9 activity and its spatial distribution in relation to oligodendrocyte processes.

Main Methods:

  • Oligodendrocytes were cultured and treated with fibronectin or laminin-2.
  • Matrix metalloproteinase (MMP) activity, specifically MMP-9, was assessed in conditioned media and on cell surfaces.
  • Protein kinase C (PKC) involvement was examined.
  • Oligodendroglial process outgrowth was quantified.

Main Results:

  • Fibronectin enhanced net MMP-9 activity in oligodendrocyte-conditioned medium in a PKC-dependent manner, without altering MMP-9 expression.
  • Cell-associated MMP-9 activity was localized to the cell body on fibronectin but along extending processes on laminin-2.
  • Mislocalization of MMP-9 activity on fibronectin correlated with impaired oligodendroglial process outgrowth.

Conclusions:

  • Extracellular matrix (ECM) molecules, such as fibronectin, significantly influence the net activity of secreted MMPs.
  • ECM components also dictate the spatial distribution of cell-associated MMP activity.
  • These ECM-driven modulations in MMP activity and localization are critical for regulating oligodendrocyte morphological differentiation and myelination.

More Related Videos

Visualizing Axonal Growth Cone Collapse and Early Amyloid β Effects in Cultured Mouse Neurons06:23

Visualizing Axonal Growth Cone Collapse and Early Amyloid β Effects in Cultured Mouse Neurons

Published on: October 30, 2018

Preparation of Rat Oligodendrocyte Progenitor Cultures and Quantification of Oligodendrogenesis Using Dual-infrared Fluorescence Scanning11:11

Preparation of Rat Oligodendrocyte Progenitor Cultures and Quantification of Oligodendrogenesis Using Dual-infrared Fluorescence Scanning

Published on: February 17, 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...
Cell Motility through Blebbing01:16

Cell Motility through Blebbing

Blebs are a type of membrane protrusion formed by the internal hydrostatic pressure of the cytoplasm. Blebs are observed in several cell types, including fibroblasts, immune cells, and single-celled organisms like the amoeba. The primary function of blebs is cell locomotion and apoptosis, but they are also found during necrosis and cell division. The life cycle of a bleb comprises an initiation phase followed by the expansion and retraction phases.
Blebbing Through the Matrix
In multicellular...
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult body.
A...