Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

A model system that demonstrates interactions among extracellular matrix macromolecules.

E A Turley1, S Roth, J A Weston

  • 1Faculty of Medicine, University of Calgary, Alberta.

Connective Tissue Research
|January 1, 1989
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Receptor for hyaluronan mediated motility (RHAMM/HMMR) is a novel target for promoting subcutaneous adipogenesis.

Integrative biology : quantitative biosciences from nano to macro·2017
Same author

Hyaluronan metabolism in remodeling extracellular matrix: probes for imaging and therapy of breast cancer.

Integrative biology : quantitative biosciences from nano to macro·2011
Same author

The respiratory system of the marine bacterium Beneckea natriegens. I. Cytochrome composition.

Biochimica et biophysica acta·2009
Same author

Peptides that mimic glycosaminoglycans: high-affinity ligands for a hyaluronan binding domain.

Chemistry & biology·2001
Same author

Active erk regulates microtubule stability in H-ras-transformed cells.

Neoplasia (New York, N.Y.)·2001
Same author

Identification of sequence, protein isoforms, and distribution of the hyaluronan-binding protein RHAMM in adult and developing rat brain.

The Journal of comparative neurology·2001

Fibronectin (FN) binds to chondroitin sulfate (CS) glycosaminoglycan chains (GAG), but not hyaluronic acid (HA). Hyaluronate binding proteins (HABP) stabilize interactions between FN, CS, and HA, aiding interstitial matrix assembly.

Area of Science:

  • Biochemistry
  • Biomaterials Science
  • Extracellular Matrix Biology

Background:

  • Fibronectin (FN) is a key extracellular matrix (ECM) protein involved in cell adhesion and matrix assembly.
  • Glycosaminoglycans (GAGs), including chondroitin sulfate (CS) and hyaluronic acid (HA), are crucial ECM components.
  • Hyaluronate binding proteins (HABPs) mediate interactions within the ECM.

Purpose of the Study:

  • To investigate the binding interactions among fibronectin (FN), glycosaminoglycan chains (GAG), and hyaluronate binding proteins (HABP).
  • To characterize the self-assembly properties of ECM constituents using a bead aggregation assay.

Main Methods:

  • Utilized a bead aggregation assay to examine binding interactions.
  • Employed radiolabeled fibronectin (3H-FN) to quantify binding to GAG-coated beads.

Related Experiment Videos

  • Assessed bead agglutination in the presence and absence of divalent cations and HABP.

    • Main Results:

    • 3H-FN bound to CS-coated beads but not HA-coated beads, indicating multiple binding sites for CS.
    • FN-CS interaction reduced the association between CS-beads and HA-beads.
    • HABP bound to HA and CS, stabilizing interactions between CS-beads and HA-beads, and promoting aggregation of FN-CS-beads with HA-beads.

    Conclusions:

    • The bead aggregation assay provides a rapid method to characterize ECM component interactions.
    • FN, GAGs, and HABPs play distinct but cooperative roles in ECM assembly.
    • These interactions are critical for the spontaneous formation of the interstitial matrix.