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Previous studies have been shown that IgA paraproteins suppress human neutrophil chemotaxis. This investigation was undertaken to determine the effect of isolated IgA myeloma component (IgA-MC) on eosinophil chemotaxis. The data presented here indicate that IgA myeloma sera inhibit eosinophil chemotaxis, and demonstrate that the IgA-MC is responsible for this chemotactic inhibitory activity (CIA). Chemotactic inhibition was cell directed and was lost following pepsin digestion or dithiothreitol reduction alkylation of the IgA-MC. Polymeric IgA was shown to be the most effective inhibitor of eosinophil chemotaxis as determined by Sephadex G-200 gel filtration chromatography and sucrose density gradient centrifugation. Both isolated IgA-MC and normal secretory IgA were shown to inhibit eosinophil chemotaxis, while nonpolymeric forms of IgA failed to suppress either neutrophil or eosinophil chemotaxis. It is postulated that the observed CIA may be a function of the interaction of IgA-MC with a cell surface IgA receptor.



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UNM Biology Department

First Committee Member (Chair)

Dennis Van Epps

Second Committee Member

Robert Berner Loftfield

Third Committee Member

Sei Tokuda

Fourth Committee Member

Leroy Clarence McLaren

Fifth Committee Member

Arthur Dale Bankhurst

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