Heat Shock Protein 10 Inhibits Lipopolysaccharide-induced Inflammatory Mediator Production

• Published in: The Journal of biological chemistry Vol. 280; no. 6; pp. 4037 - 4047
• Main Authors: Johnson, Barbara J., Le, Thuy T.T., Dobbin, Caroline A., Banovic, Tatjana, Howard, Christopher B., Flores, Flor de Maria Leon, Vanags, Daina, Naylor, Dean J., Hill, Geoffrey R., Suhrbier, Andreas
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 11.02.2005; American Society for Biochemistry and Molecular Biology
• Subjects: 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

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...