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

Hyaluronic acid-complement interactions--I. Reversible heat-induced anticomplementary activity.

N S Chang, R J Boackle, G Armand

    Molecular Immunology
    |April 1, 1985
    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

    A cascade of protein aggregation bombards mitochondria for neurodegeneration and apoptosis under WWOX deficiency.

    Cell death & disease·2015
    Same author

    WWOX suppresses autophagy for inducing apoptosis in methotrexate-treated human squamous cell carcinoma.

    Cell death & disease·2013
    Same author

    Characterization of serum adhesive proteins that block tumor necrosis factor-mediated cell death.

    Cell death and differentiation·2006
    Same author

    Biomass conversion to mixed alcohol fuels using the MixAlco process.

    Applied biochemistry and biotechnology·2004
    Same author

    Influence of maternal serum levels of vitamins C and E during the second trimester on birth weight and length.

    European journal of clinical nutrition·2004
    Same author

    Acquired activated protein C resistance, high tissue factor expression, and hyper-homocysteinemia in systemic lupus erythematosus.

    American journal of hematology·2003

    Heat treatment enhances hyaluronic acid's (HA) ability to inhibit the complement system's classical pathway. This reversible physical change in HA, stabilized by freezing and thawing, offers potent anticomplementary activity.

    Area of Science:

    • Biochemistry
    • Immunology
    • Materials Science

    Background:

    • Hyaluronic acid (HA) is a glycosaminoglycan with a known role in biological processes.
    • The interaction of HA with the complement (C) system, particularly the classical pathway, is of interest.
    • Native HA exhibits weak anticomplementary activity in vitro.

    Purpose of the Study:

    • To investigate the in vitro interaction of hyaluronic acid (HA) with complement (C) classical-pathway activity.
    • To determine if HA can be modified to exhibit enhanced anticomplementary properties.
    • To elucidate the mechanism behind HA's anticomplementary activity.

    Main Methods:

    • In vitro assays measuring complement classical pathway activity.
    • Thermal treatment of HA solutions at 100°C.

    Related Experiment Videos

  • Stabilization of treated HA via prompt freezing and thawing.
  • Assessment of anticomplementary activity before and after treatment and stabilization.
  • Analysis of HA molecular integrity post-treatment.

    • Main Results:

    • Native HA shows weak anticomplementary activity.
    • Thermal treatment (100°C) of HA, followed by prompt freezing and thawing, significantly enhances its C-inhibitory properties.
    • Heat-treated HA potently inhibits complement C1 and classical-pathway-mediated C3 conversion.
    • Anticomplementary activity is lost upon slow cooling or slow thawing and can be regenerated by re-treatment.
    • No detectable molecular degradation of HA was observed after thermal treatment.

    Conclusions:

    • A reversible physical transition of HA, likely a decoupling of intermolecular strands, is responsible for its potent anticomplementary activity.
    • Thermal treatment and prompt stabilization create a semi-stable, decoupled state of HA that effectively inhibits the classical complement pathway.
    • This heat-induced physical modification of HA offers a novel approach to modulating complement activity.