HMGB1 Protein

Publication Title: 
Medical Hypotheses

Despite recent advances in antibiotic therapy and intensive care, sepsis remains widespread problems in critically ill patients. The high mortality of sepsis is in part mediated by bacterial endotoxin, which stimulates macrophages/monocytes to sequentially release early (e.g., TNF, IL-1, and IFN-gamma) and late (e.g., HMGB1) pro-inflammatory cytokines.

Author(s): 
Chen, Xiaotian
Li, Wei
Wang, Haichao
Publication Title: 
The Journal of Nutrition

Despite recent advances in antibiotic therapy and intensive care, sepsis remains a widespread problem in critically ill patients. The high mortality from sepsis is in part mediated by bacterial endotoxin, which stimulates macrophages/monocytes to sequentially release early (e.g., tumor necrosis factor, interleukin-1, and interferon-gamma) and late [e.g., high mobility group box 1 protein (HMGB1)] proinflammatory cytokines. Our discovery of HMGB1 as a late mediator of lethal systemic inflammation has initiated a new field of investigation for the development of experimental therapeutics.

Author(s): 
Wang, Haichao
Li, Wei
Li, Jianhua
Rendon-Mitchell, Beatriz
Ochani, Mahendar
Ashok, Mala
Yang, Lihong
Yang, Huan
Tracey, Kevin J.
Wang, Ping
Sama, Andrew E.
Publication Title: 
Current Opinion in Pharmacology

A nuclear protein, high mobility group box 1 (HMGB1), is released passively by necrotic cells, and actively by macrophages/monocytes in response to exogenous and endogenous inflammatory stimuli. After binding to the receptor for advanced glycation end products (RAGE) or toll-like receptor 4 (TLR4), HMGB1 activates vascular endothelial cells and macrophages/monocytes to express proinflammatory cytokines, chemokines and adhesion molecules.

Author(s): 
Li, Wei
Sama, Andrew E.
Wang, Haichao
Publication Title: 
Viral Immunology

A nuclear protein, high mobility group box 1 (HMGB1), is released passively by necrotic cells and actively by macrophages/monocytes in response to exogenous and endogenous inflammatory stimuli. After binding to the receptor for advanced glycation end products (RAGE), or Toll-like receptor 4 (TLR4), HMGB1 activates macrophages/monocytes to express proinflammatory cytokines, chemokines, and adhesion molecules. Pharmacological suppression of its activities or release is protective against lethal endotoxemia and sepsis, establishing HMGB1 as a critical mediator of lethal systemic inflammation.

Author(s): 
Wang, Haichao
Ward, Mary F.
Fan, Xue-Gong
Sama, Andrew E.
Li, Wei
Publication Title: 
Journal of Leukocyte Biology

High mobility group box 1 (HMGB1) can be actively secreted by macrophages/monocytes in response to exogenous and endogenous inflammatory stimuli (such as bacterial endotoxin, TNF-alpha, IL-1, and IFN-gamma) or passively released by necrotic cells and mediates innate and adaptive inflammatory responses to infection and injury. Here, we demonstrated that a reactive oxygen species, hydrogen peroxide (H(2)O(2)), induces active and passive HMGB1 release from macrophage and monocyte cultures in a time- and dose-dependent manner.

Author(s): 
Tang, Daolin
Shi, Yongzhong
Kang, Rui
Li, Tong
Xiao, Weimin
Wang, Haichao
Xiao, Xianzhong
Publication Title: 
Journal of Immunology (Baltimore, Md.: 1950)

The pathogenesis of sepsis is mediated in part by bacterial endotoxin, which stimulates macrophages/monocytes to sequentially release early (e.g., TNF, IL-1, and IFN-gamma) and late (e.g., high mobility group box 1 (HMGB1) protein) proinflammatory cytokines. The recent discovery of HMGB1 as a late mediator of lethal sepsis has prompted investigation for development of new experimental therapeutics.

Author(s): 
Li, Wei
Li, Jianhua
Ashok, Mala
Wu, Rongqian
Chen, Dazhi
Yang, Lihong
Yang, Huan
Tracey, Kevin J.
Wang, Ping
Sama, Andrew E.
Wang, Haichao
Publication Title: 
Journal of Immunology (Baltimore, Md.: 1950)

In response to inflammatory stimuli (e.g., endotoxin, proinflammatory cytokines) or oxidative stress, macrophages actively release a ubiquitous nuclear protein, high-mobility group box 1 (HMGB1), to sustain an inflammatory response to infection or injury. In this study, we demonstrated mild heat shock (e.g., 42.5 degrees C, 1 h), or enhanced expression of heat shock protein (Hsp) 72 (by gene transfection) similarly rendered macrophages resistant to oxidative stress-induced HMGB1 cytoplasmic translocation and release.

Author(s): 
Tang, Daolin
Kang, Rui
Xiao, Weimin
Jiang, Lei
Liu, Meidong
Shi, Yongzhong
Wang, Kangkai
Wang, Haichao
Xiao, Xianzhong
Publication Title: 
Journal of Immunology (Baltimore, Md.: 1950)

High-mobility-group box 1 (HMGB1), a nuclear protein, has recently been identified as an important mediator of local and systemic inflammatory diseases when released into the extracellular milieu. Anti-inflammatory regulation by the stress response is an effective autoprotective mechanism when the host encounters harmful stimuli, but the mechanism of action remains incompletely delineated.

Author(s): 
Tang, Daolin
Kang, Rui
Xiao, Weimin
Wang, Haichao
Calderwood, Stuart K.
Xiao, Xianzhong
Publication Title: 
Expert Reviews in Molecular Medicine

Sepsis refers to a systemic inflammatory response syndrome resulting from a microbial infection. The inflammatory response is partly mediated by innate immune cells (such as macrophages, monocytes and neutrophils), which not only ingest and eliminate invading pathogens but also initiate an inflammatory response upon recognition of pathogen-associated molecular patterns (PAMPs).

Author(s): 
Wang, Haichao
Zhu, Shu
Zhou, Rongrong
Li, Wei
Sama, Andrew E.
Publication Title: 
Shock (Augusta, Ga.)

Sepsis refers to a systemic inflammatory response syndrome resulting from a microbial infection. The inflammatory response is partly mediated by innate immune cells (such as macrophages, monocytes, and neutrophils), which not only ingest and eliminate invading pathogens but also initiate an inflammatory response by producing early (e.g., TNF and IFN-gamma) and late (e.g., high-mobility group box [HMGB1]) proinflammatory cytokines.

Author(s): 
Wang, Haichao
Ward, Mary F.
Sama, Andrew E.

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