Heat Shock Protein 10 Inhibits Lipopolysaccharide-induced Inflammatory Mediator Production
Heat shock protein 10 (Hsp10) and heat shock protein 60 (Hsp60) were originally described as essential mitochondrial proteins involved in protein folding. However, both proteins have also been shown to have a number of extracellular immunomodulatory activities. Here we show that purified recombinant...
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Published in | The Journal of biological chemistry Vol. 280; no. 6; pp. 4037 - 4047 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
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United States
Elsevier Inc
11.02.2005
American Society for Biochemistry and Molecular Biology |
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Abstract | Heat shock protein 10 (Hsp10) and heat shock protein 60 (Hsp60) were originally described as essential mitochondrial proteins involved in protein folding. However, both proteins have also been shown to have a number of extracellular immunomodulatory activities. Here we show that purified recombinant human Hsp10 incubated with cells in vitro reduced lipopolysaccharide (LPS)-induced nuclear factor-κB activation and secretion of several inflammatory mediators from RAW264.7 cells, murine macrophages, and human peripheral blood mononuclear cells. Induction of tolerance by contaminating LPS was formally excluded as being responsible for Hsp10 activity. Treatment of mice with Hsp10 before endotoxin challenge resulted in the reduction of serum tumor necrosis factor-α and RANTES (regulated upon activation, normal T cell expressed and secreted) levels and an elevation of serum interleukin-10 levels. Hsp10 treatment also delayed mortality in a murine graft-versus-host disease model, where gut-derived LPS contributes to pathology. We were unable to confirm previous reports that Hsp10 has tumor growth factor properties and suggest that Hsp10 exerts anti-inflammatory activity by inhibiting Toll-like receptor signaling possibly by interacting with extracellular Hsp60. |
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AbstractList | Heat shock protein 10 (Hsp10) and heat shock protein 60 (Hsp60) were originally described as essential mitochondrial proteins involved in protein folding. However, both proteins have also been shown to have a number of extracellular immunomodulatory activities. Here we show that purified recombinant human Hsp10 incubated with cells in vitro reduced lipopolysaccharide (LPS)-induced nuclear factor-κB activation and secretion of several inflammatory mediators from RAW264.7 cells, murine macrophages, and human peripheral blood mononuclear cells. Induction of tolerance by contaminating LPS was formally excluded as being responsible for Hsp10 activity. Treatment of mice with Hsp10 before endotoxin challenge resulted in the reduction of serum tumor necrosis factor-α and RANTES (regulated upon activation, normal T cell expressed and secreted) levels and an elevation of serum interleukin-10 levels. Hsp10 treatment also delayed mortality in a murine graft-versus-host disease model, where gut-derived LPS contributes to pathology. We were unable to confirm previous reports that Hsp10 has tumor growth factor properties and suggest that Hsp10 exerts anti-inflammatory activity by inhibiting Toll-like receptor signaling possibly by interacting with extracellular Hsp60. Heat shock protein 10 (Hsp10) and heat shock protein 60 (Hsp60) were originally described as essential mitochondrial proteins involved in protein folding. However, both proteins have also been shown to have a number of extracellular immunomodulatory activities. Here we show that purified recombinant human Hsp10 incubated with cells in vitro reduced lipopolysaccharide (LPS)-induced nuclear factor-κB activation and secretion of several inflammatory mediators from RAW264.7 cells, murine macrophages, and human peripheral blood mononuclear cells. Induction of tolerance by contaminating LPS was formally excluded as being responsible for Hsp10 activity. Treatment of mice with Hsp10 before endotoxin challenge resulted in the reduction of serum tumor necrosis factor-α and RANTES (regulated upon activation, normal T cell expressed and secreted) levels and an elevation of serum interleukin-10 levels. Hsp10 treatment also delayed mortality in a murine graft- versus -host disease model, where gut-derived LPS contributes to pathology. We were unable to confirm previous reports that Hsp10 has tumor growth factor properties and suggest that Hsp10 exerts anti-inflammatory activity by inhibiting Toll-like receptor signaling possibly by interacting with extracellular Hsp60. Heat shock protein 10 (Hsp10) and heat shock protein 60 (Hsp60) were originally described as essential mitochondrial proteins involved in protein folding. However, both proteins have also been shown to have a number of extracellular immunomodulatory activities. Here we show that purified recombinant human Hsp10 incubated with cells in vitro reduced lipopolysaccharide (LPS)-induced nuclear factor- Kappa B activation and secretion of several inflammatory mediators from RAW264.7 cells, murine macrophages, and human peripheral blood mononuclear cells. Induction of tolerance by contaminating LPS was formally excluded as being responsible for Hsp10 activity. Treatment of mice with Hsp10 before endotoxin challenge resulted in the reduction of serum tumor necrosis factor- alpha and RANTES (regulated upon activation, normal T cell expressed and secreted) levels and an elevation of serum interleukin-10 levels. Hsp10 treatment also delayed mortality in a murine graft-versus-host disease model, where gut-derived LPS contributes to pathology. We were unable to confirm previous reports that Hsp10 has tumor growth factor properties and suggest that Hsp10 exerts anti-inflammatory activity by inhibiting Toll-like receptor signaling possibly by interacting with extracellular Hsp60. Heat shock protein 10 (Hsp10) and heat shock protein 60 (Hsp60) were originally described as essential mitochondrial proteins involved in protein folding. However, both proteins have also been shown to have a number of extracellular immunomodulatory activities. Here we show that purified recombinant human Hsp10 incubated with cells in vitro reduced lipopolysaccharide (LPS)-induced nuclear factor-kappaB activation and secretion of several inflammatory mediators from RAW264.7 cells, murine macrophages, and human peripheral blood mononuclear cells. Induction of tolerance by contaminating LPS was formally excluded as being responsible for Hsp10 activity. Treatment of mice with Hsp10 before endotoxin challenge resulted in the reduction of serum tumor necrosis factor-alpha and RANTES (regulated upon activation, normal T cell expressed and secreted) levels and an elevation of serum interleukin-10 levels. Hsp10 treatment also delayed mortality in a murine graft-versus-host disease model, where gut-derived LPS contributes to pathology. We were unable to confirm previous reports that Hsp10 has tumor growth factor properties and suggest that Hsp10 exerts anti-inflammatory activity by inhibiting Toll-like receptor signaling possibly by interacting with extracellular Hsp60. |
Author | Dobbin, Caroline A. Banovic, Tatjana Vanags, Daina Flores, Flor de Maria Leon Johnson, Barbara J. Suhrbier, Andreas Le, Thuy T.T. Howard, Christopher B. Naylor, Dean J. Hill, Geoffrey R. |
Author_xml | – sequence: 1 givenname: Barbara J. surname: Johnson fullname: Johnson, Barbara J. email: barbara.johnson@cbio.com.au organization: CBio Limited, 17 Wakefield St., Alderley, Queensland 4051, Australia – sequence: 2 givenname: Thuy T.T. surname: Le fullname: Le, Thuy T.T. organization: Queensland Institute of Medical Research (Australian National Centre for International and Tropical Health and Nutrition and Department of Pathology, University of Queensland), 300 Herston Rd., Herston, Queensland 4029, Australia – sequence: 3 givenname: Caroline A. surname: Dobbin fullname: Dobbin, Caroline A. organization: CBio Limited, 17 Wakefield St., Alderley, Queensland 4051, Australia – sequence: 4 givenname: Tatjana surname: Banovic fullname: Banovic, Tatjana organization: Queensland Institute of Medical Research (Australian National Centre for International and Tropical Health and Nutrition and Department of Pathology, University of Queensland), 300 Herston Rd., Herston, Queensland 4029, Australia – sequence: 5 givenname: Christopher B. surname: Howard fullname: Howard, Christopher B. organization: CBio Limited, 17 Wakefield St., Alderley, Queensland 4051, Australia – sequence: 6 givenname: Flor de Maria Leon surname: Flores fullname: Flores, Flor de Maria Leon organization: CBio Limited, 17 Wakefield St., Alderley, Queensland 4051, Australia – sequence: 7 givenname: Daina surname: Vanags fullname: Vanags, Daina organization: CBio Limited, 17 Wakefield St., Alderley, Queensland 4051, Australia – sequence: 8 givenname: Dean J. surname: Naylor fullname: Naylor, Dean J. organization: CBio Limited, 17 Wakefield St., Alderley, Queensland 4051, Australia – sequence: 9 givenname: Geoffrey R. surname: Hill fullname: Hill, Geoffrey R. organization: Queensland Institute of Medical Research (Australian National Centre for International and Tropical Health and Nutrition and Department of Pathology, University of Queensland), 300 Herston Rd., Herston, Queensland 4029, Australia – sequence: 10 givenname: Andreas surname: Suhrbier fullname: Suhrbier, Andreas organization: Queensland Institute of Medical Research (Australian National Centre for International and Tropical Health and Nutrition and Department of Pathology, University of Queensland), 300 Herston Rd., Herston, Queensland 4029, Australia |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/15546885$$D View this record in MEDLINE/PubMed |
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Snippet | Heat shock protein 10 (Hsp10) and heat shock protein 60 (Hsp60) were originally described as essential mitochondrial proteins involved in protein folding.... Heat shock protein 10 (Hsp10) and heat shock protein 60 (Hsp60) were originally described as essential mitochondrial proteins involved in protein folding.... |
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SubjectTerms | Animals Antibodies, Monoclonal - chemistry Biological Assay Bone Marrow Transplantation Cell Line Cell Proliferation Chaperonin 10 - physiology Chaperonin 60 - metabolism Chemokine CCL5 - metabolism Dose-Response Relationship, Drug Endotoxins - metabolism Enzyme-Linked Immunosorbent Assay Humans Inflammation Interleukin-10 - blood Interleukin-6 - blood K562 Cells Leukocytes, Mononuclear - metabolism Lipopolysaccharides - chemistry Lipopolysaccharides - metabolism Macrophages - metabolism Mice Mice, Inbred BALB C Monocytes - metabolism Protein Binding Protein Folding Recombinant Proteins - chemistry Signal Transduction Time Factors Trypsin - pharmacology Tumor Necrosis Factor-alpha - biosynthesis U937 Cells |
Title | Heat Shock Protein 10 Inhibits Lipopolysaccharide-induced Inflammatory Mediator Production |
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