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Cited by 171Phagocytosis and Immune RegulationCellular Mechanics and InteractionsCellular transport and secretion

Ca(2+)-independent F-actin assembly and disassembly during Fc receptor-mediated phagocytosis in mouse macrophages.

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Greenberg, S, el Khoury, J, di Virgilio, F, Kaplan, E M, Silverstein, S C·1991·The Journal of cell biology
DOI 10.1083/jcb.113.4.757PMC PMC2288985
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Abstract

Phagocytosis of IgG-coated particles by macrophages is presumed to involve the actin-based cytoskeleton since F-actin accumulates beneath forming phagosomes, and particle engulfment is blocked by cytochalasins, drugs that inhibit actin filament assembly. However, it is unknown whether Fc receptor ligation affects the rate or extent of F-actin assembly during phagocytosis of IgG-coated particles. To examine this question we have used a quantitative spectrofluorometric method to examine F-actin dynamics during a synchronous wave of phagocytosis of IgG-coated red blood cells by inflammatory mouse macrophages. We observed a biphasic rise in macrophage F-actin content during particle engulfment, with maxima at 1 and 5 min after the initiation of phagocytosis. F-actin declined to resting levels by 30 min, by which time particle engulfment was completed. These quantitative increases in macrophage F-actin were reflected in localized changes in F-actin distribution. Previous work showed that the number of IgG-coated particles engulfed by macrophages is unaffected by buffering extracellular calcium or by clamping cytosolic free calcium concentration ([Ca2+]i) to very low levels (Di Virgilio, F., B. C. Meyer, S. Greenberg, and S. C. Silverstein. 1988. J. Cell Biol. 106: 657-666). To determine whether clamping [Ca2+]i in macrophages affects the rate of particle engulfment, or the assembly or disassembly of F-actin during phagocytosis, we examined these parameters in macrophages whose [Ca2+]i had been clamped to approximately less than 3 nM with fura 2/AM and acetoxymethyl ester of EGTA. We found that the initial rate of phagocytosis, and the quantities of F-actin assembled and disassembled were similar in Ca(2+)-replete and Ca(2+)-depleted macrophages. We conclude that Fc receptor-mediated phagocytosis in mouse macrophages is accompanied by an ordered sequence of assembly and disassembly of F-actin that is insensitive to [Ca2+]i.

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Authors
Greenberg, S., el Khoury, J., di Virgilio, F., Kaplan, E. M., & Silverstein, S. C.
Affiliations
  • Columbia University (US)
  • Rover Laboratory of Cellular Physiology, Department of Medicine, College of Physicians and Surgeons, Columbia University, New York 10032.
Venue
The Journal of cell biology
Publisher
Rockefeller University Press
Published
1991-05-15
Volume
113
Issue
4
Pages
757-767
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
DOI
10.1083/jcb.113.4.757
PMC
PMC2288985
OpenAlex
W2158352050
Cited by
171
References
51
Citations by year
2025: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 3 · 2019: 5 · 2018: 5 · 2016: 3 · 2015: 5 · 2014: 4 · 2013: 3 · 2012: 2
FWCI
5.23
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • The Journal of Cell Biology (publishedVersion)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
  • Institutional Research Information System University of Ferrara (University of Ferrara) (submittedVersion)
  • Columbia Academic Commons (Columbia University)
Funders
National Institute of Allergy and Infectious Diseases (AI20516)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
F-actin assembly, F-actin disassembly, phagocytosis, Fc receptors, macrophages, cytosolic free calcium, phagosome formation, cytoskeleton
MeSH terms
Actins, Animals, Calcium, Macrophages, Actin Cytoskeleton, Microscopy, Fluorescence, Peritoneal Cavity, Phagocytosis, Receptors, Fc, Thioglycolates, Cytochalasin D, Mice, In Vitro Techniques

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