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Research Article Free access | 10.1172/JCI117770

The purinergic P2Z receptor of human macrophage cells. Characterization and possible physiological role.

S Falzoni, M Munerati, D Ferrari, S Spisani, S Moretti, and F Di Virgilio

Institute of General Pathology, University of Ferrara, Italy.

Find articles by Falzoni, S. in: PubMed | Google Scholar

Institute of General Pathology, University of Ferrara, Italy.

Find articles by Munerati, M. in: PubMed | Google Scholar

Institute of General Pathology, University of Ferrara, Italy.

Find articles by Ferrari, D. in: PubMed | Google Scholar

Institute of General Pathology, University of Ferrara, Italy.

Find articles by Spisani, S. in: PubMed | Google Scholar

Institute of General Pathology, University of Ferrara, Italy.

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Institute of General Pathology, University of Ferrara, Italy.

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Published March 1, 1995 - More info

Published in Volume 95, Issue 3 on March 1, 1995
J Clin Invest. 1995;95(3):1207–1216. https://doi.org/10.1172/JCI117770.
© 1995 The American Society for Clinical Investigation
Published March 1, 1995 - Version history
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Abstract

We have investigated responses of human monocyte/macrophage cells to extracellular ATP (ATPe). Freshly isolated peripheral blood monocytes showed responses linked to P2Y but not P2Z purinergic receptors; however, during in vitro macrophage differentiation, these cells also exhibited responses suggestive of the presence of the membrane-permeabilizing P2Z receptor. In fact, in human macrophages a brief (15-min) exposure to ATPe, but not other nucleotides, caused (1) a rapid and long-lasting plasma membrane depolarization; (2) a large increase in intracellular Ca2+ concentration followed by efflux of the Ca2+ indicator; (3) uptake of low molecular weight hydrophilic molecules such as Lucifer yellow and ethidium bromide; and (4) cell rounding, swelling, and eventual release of the cytoplasmic enzyme lactate dehydrogenase. rIFN-gamma enhanced both membrane-permeabilizing and cytotoxic ATPe effects. Membrane permeabilization and cytotoxicity were fully blocked by pretreatment of the cells with oxidized ATP, a compound recently shown to block P2Z receptors covalently in macrophages. Blocking of the P2Z receptor by oxidized ATP also inhibited multinucleated giant cell generation stimulated by concanavalin A or rIFN-gamma without decreasing monocyte migration or membrane adhesion molecule expression. These data suggest that human macrophages express rIFN-gamma-modulated purinergic P2Z receptors in vitro and hint at a role for these plasma membrane molecules in the generation of macrophage polykarions.

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