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Isolation of human eosinophil phospholipase D.

L A Kater, E J Goetzl, K F Austen

    The Journal of Clinical Investigation
    |May 1, 1976
    PubMed
    Summary

    Human eosinophils contain a unique phospholipase D enzyme that inactivates platelet-activating factor (PAF). This enzyme may regulate immediate hypersensitivity reactions by breaking down PAF.

    Area of Science:

    • Biochemistry
    • Immunology

    Background:

    • Eosinophils play a role in immediate hypersensitivity reactions.
    • Platelet-activating factor (PAF) is implicated in these reactions.

    Purpose of the Study:

    • To isolate and characterize phospholipase D from human eosinophils.
    • To investigate the enzyme's role in PAF inactivation.

    Main Methods:

    • Sequential chromatography (asion, cation exchange) and gel filtration for enzyme isolation.
    • Enzyme activity assays using phosphatidyl choline and platelet-activating factor (PAF).
    • Isoelectric focusing for pI determination and molecular weight estimation.

    Main Results:

    • Phospholipase D was purified from human eosinophil polymorphonuclear leukocytes.

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  • The enzyme exhibits optimal activity at pH 4.5-6.0 with a pI of 5.8-6.2.
  • Eosinophil phospholipase D inactivated rat platelet-activating factor (PAF) in a time- and dose-dependent manner.
  • The enzyme's molecular weight (60,000) is half that of plant phospholipase D.

    • Conclusions:

    • Human eosinophil phospholipase D can inactivate platelet-activating factor (PAF).
    • This enzymatic activity suggests a regulatory role for eosinophils in immediate hypersensitivity.
    • Eosinophils may modulate hypersensitivity by degrading both PAF and slow-reacting substance of anaphylaxis (via arylsulfatase B).