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

Decorin binds fibrinogen in a Zn2+-dependent interaction.

Tracey A Dugan1, Vivian W-C Yang, David J McQuillan

  • 1Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas Medical Center, Houston 77030, USA.

The Journal of Biological Chemistry
|February 13, 2003
PubMed
Summary

Decorin, a small leucine-rich proteoglycan, binds fibrinogen and self-associates in a zinc-dependent manner. The N-terminal domain of decorin mediates these zinc-driven interactions, highlighting zinc's role in decorin's biological functions.

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

<i>Staphylococcus epidermidis</i> ST2 strains associated with bloodstream infections contain a unique mobile genetic element encoding a plasmin inhibitor.

mBio·2024
Same author

Selective refueling of CAR T cells using ADA1 and CD26 boosts antitumor immunity.

Cell reports. Medicine·2024
Same author

CRISPR-Cas9-based functional interrogation of unconventional translatome reveals human cancer dependency on cryptic non-canonical open reading frames.

Nature structural & molecular biology·2023
Same author

Antibodies to coagulase of <i>Staphylococcus aureus</i> crossreact to Efb and reveal different binding of shared fibrinogen binding repeats.

Frontiers in immunology·2023
Same author

Click display: a rapid and efficient in vitro protein display method for directed evolution.

Nucleic acids research·2023
Same author

KRAS Inhibitor that Simultaneously Inhibits Nucleotide Exchange Activity and Effector Engagement.

ACS bio & med chem Au·2023

Area of Science:

  • Biochemistry
  • Extracellular Matrix Biology
  • Proteoglycan Research

Background:

  • Decorin is a small leucine-rich proteoglycan found in the extracellular matrix.
  • Decorin functions as a zinc metalloprotein at physiological zinc concentrations.
  • Previous work established decorin's interaction with zinc ions.

Purpose of the Study:

  • To investigate the binding of decorin to fibrinogen in the presence of zinc.
  • To identify the specific domain of decorin responsible for fibrinogen binding and self-association.
  • To elucidate the role of zinc in mediating decorin's molecular interactions.

Main Methods:

  • Fluorescence polarization assays to determine binding affinity.
  • Solid-phase binding assays to study protein interactions.

Related Experiment Videos

  • Gel filtration chromatography to analyze protein oligomerization.

    • Main Results:

    • Decorin proteoglycan binds to fibrinogen in a zinc-dependent manner.
    • The N-terminal domain of decorin contains the fibrinogen-binding site.
    • Zinc promotes the self-association of decorin, mediated by its N-terminal domain, forming oligomers at low micromolar concentrations.

    Conclusions:

    • Zinc ions play a critical role in mediating decorin's interactions with fibrinogen.
    • The N-terminal domain of decorin is crucial for both fibrinogen binding and zinc-induced self-association.
    • Zinc-dependent oligomerization of decorin may be important for its biological functions in the extracellular matrix.