Cited by 41Heat shock proteins researchPhagocytosis and Immune RegulationImmune Response and Inflammation

Increase in Phagocytosis after Geldanamycin Treatment or Heat Shock: Role of Heat Shock Proteins

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Vega, Virginia L, De Maio, Antonio·2005·The Journal of Immunology

Abstract

The response to injury is activated at the systemic and cellular levels. At the systemic level, phagocytosis plays a key role in controlling infections and clearing necrotic and apoptotic cells. The expression of heat shock proteins (Hsp), which is a well-conserved process, is a major component of cellular response to stress. This study investigated the relationship between Hsps and phagocytosis. An increase in the phagocytosis of opsonized bacteria particles and latex beads was observed upon incubation of murine macrophages with geldanamycin (GA), a specific inhibitor of the Hsp90 family of proteins. The effect of GA on phagocytosis was blocked by coincubation with inhibitors of transcription (actinomycin D) or translation (cycloheximide), suggesting that gene expression was required. Because expression of Hsps has been observed after GA treatment, the effect of heat shock on phagocytosis was investigated. Similar to GA treatment, heat shock resulted in an actinomycin D-sensitive elevation of phagocytosis, which suggests that Hsps are involved. The increase in phagocytosis after GA treatment was not due to increased binding of opsonized particles to their respective receptors on the macrophage surface or to elevated oxidative stress. However, it was correlated with a rapid polymerization of actin in proximity to the plasma membrane. These results suggest that Hsps play a role in the modulation of the phagocytic process, which is part of the stress response.

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Crossref · 10.4049/jimmunol.175.8.5280

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Authors
Vega, V. L., & De Maio, A.
Affiliations
  • Johns Hopkins University (US)
  • Division of Pediatric Surgery, Johns Hopkins University School of Medicine , Baltimore, MD 21205
Venue
The Journal of Immunology
Published
2005-10
Volume
175
Issue
8
Pages
5280-5287
ISSN
  • 0022-1767 (ISSN-L)
  • 1550-6606
OpenAlex
W1584354252
Cited by
41
References
54
Citations by year
2025: 1 · 2024: 1 · 2023: 1 · 2022: 4 · 2021: 3 · 2020: 2 · 2019: 1 · 2018: 2 · 2017: 2 · 2016: 3 · 2015: 1 · 2014: 2 · 2013: 3 · 2012: 2
FWCI
1.13
Type
journal article
Language
en
Open access
Locations
  • The Journal of Immunology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health
  • National Institute of General Medical Sciences (GM50878, R01GM050878)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
  • Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Keywords
phagocytosis, heat shock proteins, geldanamycin, HSP90 inhibition, heat shock, macrophages, actin polymerization, latex beads, stress response, actinomycin D, cycloheximide, gene expression
MeSH terms
Actins, Animals, Cell Line, Gene Expression Regulation, Hot Temperature, Heat-Shock Proteins, Immunoglobulin G, Macrophages, Microspheres, Phagocytosis, Quinones, Benzoquinones, Oxidative Stress, Lactams, Macrocyclic, Mice

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