Effects of latrunculin A on immunological phagocytosis and macrophage spreading-associated changes in the F-actin/G-actin content of the cells
Abstract
Latrunculin A, a toxin from a Red Sea sponge, was shown to be a very potent inhibitor of immunological phagocytosis by normal and activated macrophages (obtained from mice injected i.p. with LPS), as well as by polymorphonuclear leukocytes. This toxin blocks the interiorization of the immune complexes but does not interfere with their binding to the phagocyte (recognition phase); activated macrophages were more susceptible to this inhibition than normal macrophages and polymorphonuclear leukocytes. The effect of the toxin on cellular spreading of macrophages was also studied using two kinds of substrate: glass, and glass covered with IgG immune complexes. Latrunculin A was able to impair the spreading of normal macrophages on glass covered with immune complexes, and could also completely reverse the spreading after it had occurred. Contrarily, in activated macrophages, this toxin could neither impede the spreading nor reverse it, a difference that might be a distinctive property of the activated state. We have also found that latrunculin A can reduce the percentage of F-actin in both normal and activated macrophages, the activated cells being more susceptible to this effect. Since latrunculin A is a blocking agent of actin polymerization in vitro, these results indicate that actin polymerization and assembly must be an essential component of the primary, active event of the engulfment phase of phagocytosis.
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Uptake of Aβ in BV2 cells occurs primarily through endocytosis (receptor-mediated endocytosis), as latrunculin A prevents zymosan internalization but has no effect on dextran or Aβ.
“Inhibition of actin polymerization and phagocytosis using latrunculin A (de Oliveira and Mantovani, 1988; Oliveira et al., 1996), prevented the internalization of the phagocytic substrate zymosan but had no effect on either the endocytic substrate dextran or Aβ (Fig. 2C), suggesting that uptake of Aβ in our model occurs primarily through endocytosis (RME).”
From LC3-Associated Endocytosis Facilitates β-Amyloid Clearance and Mitigates Neurodegeneration in Murine Alzheimer’s Disease (2019) · cites this paper as Oliveira et al., 1996
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“Inhibition of actin polymerization and phagocytosis using latrunculin A (de Oliveira and Mantovani, 1988; Oliveira et al., 1996), prevented the internalization of the phagocytic substrate zymosan but had no effect on either the endocytic substrate dextran or Aβ (Fig.”
- Authors
- Oliveira, C. A., Kashman, Y., & Mantovani, B.
- Affiliations
- Universidade de São Paulo (BR)
- Tel Aviv University (IL)
- Corresponding author
- Mantovani, Bernardo
- ORCID
- Oliveira, Carlos A.
- Venue
- Chemico-Biological Interactions
- Publisher
- Elsevier BV
- Published
- 1996-03
- Volume
- 100
- Issue
- 2
- Pages
- 141-153
- ISSN
- 0009-2797 (ISSN-L)
- OpenAlex
- W2028101883
- Cited by
- 43
- References
- 36
- Citations by year
- 2026: 1 · 2024: 1 · 2023: 1 · 2022: 3 · 2021: 2 · 2020: 2 · 2019: 7 · 2018: 2 · 2017: 2 · 2016: 2 · 2014: 2 · 2013: 2
- FWCI
- 0.56
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Chemico-Biological Interactions (publishedVersion)
- PubMed (publishedVersion)
- 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 › Biotechnology › Marine Sponges and Natural Products
- Keywords
- latrunculin A, phagocytosis, macrophages, polymorphonuclear leukocytes, immune complexes, actin polymerization, F-actin, macrophage spreading, macrophage activation, LPS, engulfment
- MeSH terms
- Actins, Animals, Antigen-Antibody Complex, Cell Movement, Cytoskeleton, Erythrocytes, Macrophage Activation, Macrophages, Marine Toxins, Phagocytosis, Porifera, Thiazoles, Rats, Wistar, Bridged Bicyclo Compounds, Heterocyclic, Cell Size, Mice, Rats, Thiazolidines
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