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

Superoxide dismutase activity in leukocytes.

L R DeChatelet, C E McCall, L C McPhail

    The Journal of Clinical Investigation
    |April 1, 1974
    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

    Endotoxin-adapted septic shock leukocytes selectively alter production of sIL-1RA and IL-1beta.

    Shock (Augusta, Ga.)·2002
    Same author

    The phosphatidylinositol 3-kinase pathway selectively controls sIL-1RA not interleukin-1beta production in the septic leukocytes.

    The Journal of biological chemistry·2001
    Same author

    Phosphatidic acid regulates tyrosine phosphorylating activity in human neutrophils: enhancement of Fgr activity.

    The Journal of biological chemistry·2000
    Same author

    Phosphatidic acid and diacylglycerol directly activate NADPH oxidase by interacting with enzyme components.

    The Journal of biological chemistry·2000
    Same author

    Phosphorylation of p22phox is mediated by phospholipase D-dependent and -independent mechanisms. Correlation of NADPH oxidase activity and p22phox phosphorylation.

    The Journal of biological chemistry·2000
    Same author

    Characterization of interleukin-1 receptor-associated kinase in normal and endotoxin-tolerant cells.

    The Journal of biological chemistry·2000

    Superoxide dismutase enzyme activity was found in human neutrophils and rabbit macrophages. This enzyme protects phagocytic cells from superoxide generated during bacterial killing.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Immunology

    Background:

    • Phagocytic cells, such as neutrophils and macrophages, play a crucial role in the innate immune system.
    • The generation of superoxide anion is a key component of the microbicidal activity of these cells.
    • Understanding the cellular mechanisms that regulate superoxide levels is important for comprehending host defense.

    Purpose of the Study:

    • To identify and characterize superoxide dismutase activity in human neutrophils and rabbit alveolar macrophages.
    • To investigate the cellular localization and properties of this enzyme.
    • To assess the potential role of superoxide dismutase in protecting phagocytic cells during the inflammatory response.

    Main Methods:

    • Enzyme assays were performed using two distinct procedures to measure superoxide dismutase activity.

    Related Experiment Videos

  • Cellular fractions were analyzed to determine the subcellular localization of the enzyme.
  • The enzyme's sensitivity to inhibitors like cyanide and azide was tested.
  • Main Results:

    • Superoxide dismutase activity was successfully identified in both human neutrophils and rabbit alveolar macrophages.
    • The enzyme was found to be located in the cytosol of these phagocytic cells.
    • The identified superoxide dismutase was insensitive to inhibition by cyanide and azide.

    Conclusions:

    • The presence of superoxide dismutase in phagocytic cells supports the hypothesis that superoxide anion is involved in cellular bactericidal activity.
    • This enzyme likely functions as a protective mechanism, mitigating oxidative stress caused by superoxide generation during phagocytosis.
    • Further research into superoxide dismutase activity can elucidate its role in immune cell function and host defense against pathogens.