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The Release of Granule Enzymes from Human Neutrophils Stimulated by Aggregated Immunoglobulins of Different Classes and Subclasses¹

From the Department of Experimental Pathology, Scripps Clinic and Research Foundation, 476 Prospect Street, La Jolla, California 92037

Abstract

Aggregated human myeloma proteins of subclasses IgG₁, IgG₂, IgG₃, IgG₄, IgA₁, and IgA₂ and normal IgG have been shown to react with human neutrophils in a serum-free medium and to induce release of the lysosomal enzyme glucuronidase to the exterior of the cells. In contrast, IgD, IgE and IgM macroglobulins did not stimulate this release. Incubation of neutrophils with insoluble IgG and IgA aggregates resulted in adherence of the aggregates to the neutrophils and their phagocytosis. During this process, release of granule enzymes, but not of the cytoplasmic enzyme lactic dehydrogenase, occurred, indicating a selective process rather than one of cell lysis. Soluble aggregates did not induce liberation of enzymes when incubated with the neutrophils in suspension, but when bound to micropore filters to serve as nonphagocytosable surfaces, they stimulated adherent cells to release their granule contents. This latter process has previously been shown to result from direct extrusion of neutrophil granules to the exterior.

Footnotes

¹ This is publication 545 from the Department of Experimental Pathology, Scripps Clinic and Research Foundation, La Jolla, California. The work was supported by United States Public Health Service Grant AI-07007, The National Science Foundation, The Council for Tobacco Research, U. S. A. Grant 764, American Heart Association Grant-in-Aids 69 769 and 70 710 and Special Grant 531 from The American Cancer Society.

² Dr. Henson is a recipient of a United States Public Health Service Career Development Award (5 KO4 GM42567-02).

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