ArticleJournal of leukocyte biology2017
Involvement of cell surface 90 kDa heat shock protein (HSP90) in pattern recognition by human monocyte-derived macrophages.
Article in Journal of leukocyte biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Upregulation of HSP90α in the lungs and circulation in sarcoidosis.Frontiers in medicine · 2025Article
- All-Trans Retinoic Acid-Induced Cell Surface Heat Shock Protein 90 Mediates Tau Protein Internalization and Degradation in Human Microglia.Molecular neurobiology · 2025Article
- Cytoskeleton Remodeling-Related Proteins Represent a Specific Salivary Signature in PSC Patients.Molecules (Basel, Switzerland) · 2024Article
- Heat shock protein 90 inhibition attenuates inflammation in models of atopic dermatitis: a novel mechanism of action.Frontiers in immunology · 2023Article
- HSP90α induces immunosuppressive myeloid cells in melanoma via TLR4 signaling.Journal for immunotherapy of cancer · 2022Article
- Targeting extracellular Hsp90: A unique frontier against cancer.Frontiers in molecular biosciences · 2022Review
- Untangling Local Pro-Inflammatory, Reparative, and Regulatory Damage-Associated Molecular-Patterns (DAMPs) Pathways to Improve Transplant Outcomes.Frontiers in immunology · 2021Review
- mTORC1 Is Not Principally Involved in the Induction of Human Endotoxin Tolerance.Frontiers in immunology · 2020Article
- Substance P Improves Renal Ischemia Reperfusion Injury Through Modulating Immune Response.Frontiers in immunology · 2020Article
- Diversity and environmental adaptation of phagocytic cell metabolism.Journal of leukocyte biology · 2019Review
- 17-DMAG regulates p21 expression to induce chondrogenesisDisease models & mechanisms · 2018Article
- Exposure of Monocytic Cells to Lipopolysaccharide Induces Coordinated Endotoxin Tolerance, Mitochondrial Biogenesis, Mitophagy, and Antioxidant Defenses.Frontiers in immunology · 2018Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat shock proteins (HSPs) are typical intracellular chaperones which also appear on the cell surface and in extracellular milieu. HSP90, which chaperones many proteins involved in signal transduction, is also a regular component of LPS-signaling complexes on Mϕ. As LPS is a prototypical PAMP, we speculated that HSP90 is engaged in pattern recognition by professional phagocytes. In this report, we provide the first evidence, to our knowledge, of the geldanamycin (Ge)-inhibitable HSP90 on the surface of live monocyte-derived Mϕs (hMDMs). Using cytometry and specific Abs, we showed both HSP90 isoforms (α and β) on the surface of human monocytes and hMDMs. The cell-surface HSP90 pool was also labeled with cell-impermeable Ge derivatives. Confocal analysis of hMDMs revealed that HSP90-inhibitor complexes were rapidly clustered on the cell surface and recycled through the endosomal compartment. This finding suggests that the N-terminal (ATPase) domain of HSP90 is exposed and accessible from the extracellular space. To study the role of cell-surface HSP90 in pattern recognition, we used pathogen (PAMPs)- or apoptotic cell-associated molecular patterns (ACAMPs). We showed that blocking the cell-surface HSP90 pool leads to a dramatic decrease in TNF production by monocytes and hMDMs exposed to soluble (TLRs-specific ligands) and particulate [bacteria
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