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

Complement-induced decrease in membrane mobility: introducing a more sensitive index of spin-label motion.

R P Mason, E B Giavedoni, A P Dalmasso

    Biochemistry
    |March 22, 1977
    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

    [Oxygen and the liberation of glucose in the perfused toad liver].

    Comptes rendus des seances de la Societe de biologie et de ses filiales·2014
    Same author

    Interleukin-4 induces lipogenesis in porcine endothelial cells, which in turn is critical for induction of protection against complement-mediated injury.

    Transplantation proceedings·2008
    Same author

    Potential of anticomplement therapy in clinical transplantation.

    BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy·2007
    Same author

    Dyspepsia is associated with CagA-positive Helicobacter pylori.

    The American journal of gastroenterology·2001
    Same author

    Endotoxin (lipopolysaccharide)-induced nitric oxide production in 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated Fischer rats: detection of nitrosyl hemoproteins by EPR spectroscopy.

    Chemical research in toxicology·2000
    Same author

    In vivo metabolism of tert-butyl hydroperoxide to methyl radicals. EPR spin-trapping and DNA methylation studies.

    Chemical research in toxicology·2000

    Complement activation alters erythrocyte membrane fluidity. Spin-labeling electron spin resonance (ESR) revealed reduced fluidity in complement-lysed membranes, indicating changes in lipid organization due to complement-induced damage.

    Area of Science:

    • Biochemistry
    • Membrane Biophysics
    • Immunology

    Background:

    • Antibody-sensitized erythrocytes are targets for complement system activation.
    • Understanding complement-mediated membrane damage is crucial for immunology and cell biology.
    • Spin-labeling electron spin resonance (ESR) is a technique to probe membrane dynamics.

    Purpose of the Study:

    • To investigate complement-induced alterations in the lipid organization of sheep erythrocyte membranes.
    • To compare membrane fluidity between complement-lysed and osmotically-lysed erythrocytes.
    • To evaluate the sensitivity of ESR spectral parameters to changes in membrane fluidity.

    Main Methods:

    • Utilized spin-labeling with methyl 5-doxylstearate to study sheep erythrocyte membranes.

    Related Experiment Videos

  • Incorporated the spin label into the lipid component of the erythrocyte membranes.
  • Analyzed ESR spectra to determine membrane fluidity parameters, specifically T' and hyperfine extrema widths.

    • Main Results:

    • The ESR spectrum of methyl 5-doxylstearate in erythrocyte membranes indicated a typical bilayer structure.
    • Complement-lysed erythrocyte membranes exhibited a statistically significant reduction in fluidity (increase in T') compared to osmotically-lysed controls.
    • The half-width at half-height of the outer hyperfine extrema showed a greater percentage change than T', suggesting higher sensitivity to motion.

    Conclusions:

    • Complement activation induces measurable changes in erythrocyte membrane lipid organization and fluidity.
    • ESR spectral parameters, particularly hyperfine extrema widths, are sensitive indicators of complement-induced membrane alterations.
    • Motional corrections to existing spin-labeling formalisms may be necessary to accurately interpret ESR spectra of complex membrane systems.