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Mitogenic proteinases from human leukocytes.

J D Fraser, G K Scott

    Molecular Immunology
    |April 1, 1984
    PubMed
    Summary
    This summary is machine-generated.

    Human lymphocyte membranes contain serine proteinases that stimulate lymphocyte proliferation. Antibodies against these proteinases inhibit the growth of transformed lymphocytes, highlighting their role in immune cell function.

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    Area of Science:

    • Immunology
    • Biochemistry
    • Cell Biology

    Background:

    • Serine proteinase activity is crucial for various cellular functions.
    • Understanding the role of proteinases in lymphocyte and granulocyte membranes is essential for immunology research.

    Purpose of the Study:

    • To identify and isolate serine proteinases from human lymphocyte membranes.
    • To investigate the localization and function of these enzymes in immune cells.
    • To explore their role in lymphocyte proliferation and transformed cell growth.

    Main Methods:

    • Purification of human lymphocyte membranes.
    • Isolation of enzymes using affinity chromatography.
    • Immunochemical demonstration of enzyme localization.
    • Assay of mitogenic activity on human lymphocytes.

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  • Inhibition studies using anti-proteinase antibodies.

    • Main Results:

    • Serine proteinase activity was detected in purified human lymphocyte membranes.
    • Enzymes were isolated from human leukocyte extracts and localized on lymphocyte and granulocyte membranes.
    • These proteinases exhibited mitogenic activity towards human lymphocytes.
    • Anti-proteinase antibodies inhibited the growth of transformed lymphocytes.

    Conclusions:

    • The identified serine proteinases are involved in regulating lymphocyte proliferation.
    • These enzymes play a significant role in immune cell functions, including the growth of transformed lymphocytes.
    • The findings suggest potential therapeutic targets for immune modulation.