Abstract
The ability of C5a to stimulate lysosomal enzyme release and 45Ca 2+ efflux from rabbit neutrophils was studied. C5a stimulated β-glucuronidase release from cytochalasin B-treated neutrophils either in the presence or absence of extracellular calcium. Depletion of cell calcium by pretreatment with the calcium ionophore A23187 blocked both the ability of C5a to elicit enzyme release in the absence of extracellular calcium and its ability to stimulate 45Ca 2+ efflux. Both actions were dose-dependent over the same concentration range (10 −8–10 −6 M ionophore A23187). In contrast, ionophore pretreatment had no effect on C5a-stimulated enzyme release in the presence of extracellular calcium. These results suggest that (a) release of cell calcium is required for enzyme secretion in the absence of extracellular calcium, and (b) C5a can trigger near-maximal enzyme release by using calcium from either of two sources: the extracellular space or an intracellular site.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
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