Ca2+-dependent and Ca2+-independent phagocytosis in human neutrophils


The phagocytic function of neutrophils is a crucial element in host defence against invading microorganisms. Two main specific receptor-mediated mechanisms operate in the phagocyte plasma membrane, one recognizing the C3b/bi fragment of complement and the other the Fc domain of immunoglobulin G (ref. 1). There is evidence that phagocytosis mediated by these receptors differs in the number and nature of the intracellular signals generated2–5. However, the mechanism by which receptor binding is transduced into a signal that generates the formation of the phagocyte pseudopod is not known, although extensive biochemical evidence has allowed the postulate that calcium ion gradients in the peripheral cytoplasm, by interacting with calcium-sensitive contractile proteins, initiate the process of engulfment6. Using the high-affinity fluorescent calcium indicator quin2 both to measure and to buffer intracellular calcium ([Ca2+]i), we show here that in human neutrophils two mechanisms of phagocytosis coexist: a [Ca2+]i-dependent and modulated phagocytosis, triggered by activation of the Fc receptor, and a [Ca2+]i-independent mechanism triggered by the activation of the C3b/bi receptors.

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Lew, D., Andersson, T., Hed, J. et al. Ca2+-dependent and Ca2+-independent phagocytosis in human neutrophils. Nature 315, 509–511 (1985).

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