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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1984 Sep;81(17):5430–5434. doi: 10.1073/pnas.81.17.5430

The increase in intracellular free calcium associated with IgG gamma 2b/gamma 1 Fc receptor-ligand interactions: role in phagocytosis.

J D Young, S S Ko, Z A Cohn
PMCID: PMC391718  PMID: 6236462

Abstract

The concentration of cytosolic free calcium, [Ca2+]i, was measured in J774 mouse macrophages by use of the fluorescent indicator quin-2. Resting [Ca2+]i was 87 nM. Addition of a number of specific ligands to the immunoglobulin gamma 2b/gamma 1 Fc receptor resulted in a transient increase in [Ca2+]i, the magnitude of which depended on the extent of receptor aggregation. Monovalent ligands gave only a small Ca2+ signal but blocked cell response to subsequent addition of multivalent ligands. Incubation with antibody-coated erythrocytes raised macrophage [Ca2+]i to micromolar levels. [Ca2+]i changes were only partially inhibited by the absence of external Ca2+, suggesting the release of Ca2+ from internal stores in addition to an influx of external Ca2+. These internal stores were not limited to mitochondria. An optimal range of [Ca2+]i was required for phagocytosis. Buffering [Ca2+]i with quin-2 and treating cells with quinine in the absence of external Ca2+ resulted in inhibition of phagocytosis. Increasing [Ca2+]i to micromolar levels with the calcium ionophore A23187 also resulted in similar inhibitory effects. We suggest the involvement of localized cytosolic Ca2+ gradients in generating the signals necessary for phagocytosis.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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