Abstract

The plasminogen activator (PA) activity of guinea pig basophil-enriched leukocyte preparations was localized to basophils, and not to contaminating lymphocytes and eosinophils, by correlating PA activity with basophil frequency and, more directly, by means of an improved cytochemical method here described. PA activity was fully expressed in living cells in the absence of immunologic stimuli and was suppressed/lost to a variable extent by different techniques of cell disruption. Conversely, killed, but not living, basophils expressed significant plasminogen-independent fibrinolytic activity, presumably reflecting access of cytoplasmic proteases of broken basophils to fibrin substrate. The PA activity of intact cells was destroyed by gentle trypsinization under conditions that did not impair cell viability. When disrupted cells were ultracentrifuged on a sucrose density gradient, PA activity was absent from purified granules and was confined to fractions containing cell membranes. The simplest explanation of these data is that guinea pig basophils have PA activity associated with their plasma membranes. This conclusion has several important implications for basophil functions in cell-mediated and other immunologic reactions in vivo.

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