Oxidative stress and high-mobility group box 1 (HMGB1) protein release in vitiligo

2017 ◽  
Vol 176 (6) ◽  
pp. 1436-1437 ◽  
Author(s):  
M. Becatti
Keyword(s):  
Oxidative Stress ◽  
High Mobility ◽  
Protein Release ◽  
High Mobility Group ◽  
Hmgb1 Protein

High Mobility Group Box-1 (HMGB1): A Potential Target in Therapeutics

2019 ◽  
Vol 20 (14) ◽  
pp. 1474-1485 ◽  
Author(s):  
Eyaldeva C. Vijayakumar ◽  
Lokesh Kumar Bhatt ◽  
Kedar S. Prabhavalkar
Keyword(s):  
Myocardial Infarction ◽  
Vagus Nerve Stimulation ◽  
Nuclear Protein ◽  
Therapeutic Potential ◽  
High Mobility ◽  
Dna Binding Protein ◽  
High Mobility Group ◽  
Eukaryotic Cells ◽  
Hmgb1 Protein

High mobility group box-1 (HMGB1) mainly belongs to the non-histone DNA-binding protein. It has been studied as a nuclear protein that is present in eukaryotic cells. From the HMG family, HMGB1 protein has been focused particularly for its pivotal role in several pathologies. HMGB-1 is considered as an essential facilitator in diseases such as sepsis, collagen disease, atherosclerosis, cancers, arthritis, acute lung injury, epilepsy, myocardial infarction, and local and systemic inflammation. Modulation of HMGB1 levels in the human body provides a way in the management of these diseases. Various strategies, such as HMGB1-receptor antagonists, inhibitors of its signalling pathway, antibodies, RNA inhibitors, vagus nerve stimulation etc. have been used to inhibit expression, release or activity of HMGB1. This review encompasses the role of HMGB1 in various pathologies and discusses its therapeutic potential in these pathologies.

scholarly journals Identification and Characterization of the Direct Interaction between Methotrexate (MTX) and High-Mobility Group Box 1 (HMGB1) Protein

PLoS ONE ◽  
2013 ◽  
Vol 8 (5) ◽  
pp. e63073 ◽  
Author(s):  
Yuki Kuroiwa ◽  
Yoichi Takakusagi ◽  
Tomoe Kusayanagi ◽  
Kouji Kuramochi ◽  
Takahiko Imai ◽  
...  
Keyword(s):  
High Mobility ◽  
Direct Interaction ◽  
High Mobility Group ◽  
Hmgb1 Protein ◽  
Identification And Characterization

The Role of High Mobility Group Box 1 (HMGB1) in Neurodegeneration: A Systematic Review

2022 ◽  
Vol 20 ◽  
Author(s):  
Fathimath Zaha Ikram ◽  
Alina Arulsamy ◽  
Thaarvena Retinasamy ◽  
Mohd. Farooq Shaikh
Keyword(s):  
Systematic Review ◽  
Tissue Injury ◽  
High Mobility ◽  
High Mobility Group ◽  
Hmgb1 Protein ◽  
Toll Like Receptor 4 ◽  
Neuroinflammatory Response ◽  
Molecular Pattern ◽  
Glycation End Products

Background: High mobility group box 1 (HMGB1) protein is a damage-associated molecular pattern (DAMP) molecule that plays an important role in the repair and regeneration of tissue injury. It also acts as a pro-inflammatory cytokine through the activation of toll-like receptor 4 (TLR4) and receptor for advanced glycation end products (RAGE), to elicit the neuroinflammatory response. HMGB1 may aggravate several cellular responses which may lead to pathological inflammation and cellular death. Thus, there have been a considerable amount of research into the pathological role of HMGB1 in diseases. However, whether the mechanism of action of HMGB1 is similar in all neurodegenerative disease pathology remains to be determined. Objective: Therefore, this systematic review aimed to critically evaluate and elucidate the role of HMGB1 in the pathology of neurodegeneration based on the available literature. Methods: A comprehensive literature search was performed on four databases; EMBASE, PubMed, Scopus, and CINAHL Plus. Results: A total of 85 articles were selected for critical appraisal, after subjecting to the inclusion and exclusion criteria in this study. The selected articles revealed that HMGB1 levels were found elevated in most neurodegeneration except in Huntington’s disease and Spinocerebellar ataxia, where the levels were found decreased. This review also showcased that HMGB1 may act on distinctive pathways to elicit its pathological response leading to the various neurodegeneration processes/diseases. Conclusion: While there have been promising findings in HMGB1 intervention research, further studies may still be required before any HMGB1 intervention may be recommended as a therapeutic target for neurodegenerative diseases.

High-mobility group box 1 (HMGB1) protein regulates tumor-associated cell migration through the interaction with BTB domain

2014 ◽  
Vol 26 (4) ◽  
pp. 777-783 ◽  
Author(s):  
Young Bok Ko ◽  
Boh-Ram Kim ◽  
Sang Lyun Nam ◽  
Jung Bo Yang ◽  
Sang-Yoon Park ◽  
...  
Keyword(s):  
Cell Migration ◽  
High Mobility ◽  
High Mobility Group ◽  
Hmgb1 Protein ◽  
Btb Domain

scholarly journals High-mobility group box-1 protein from CC10+ club cells promotes type 2 response in the later stage of respiratory syncytial virus infection

2019 ◽  
Vol 316 (1) ◽  
pp. L280-L290 ◽  
Author(s):  
Sisi Chen ◽  
Guangyuan Yu ◽  
Jun Xie ◽  
Wei Tang ◽  
Leiqiong Gao ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
High Mobility ◽  
Clinical Severity ◽  
High Mobility Group ◽  
Hmgb1 Protein ◽  
Club Cells ◽  
Hmgb1 Expression ◽  
Syncytial Virus ◽  
Tract Infections

The type 2 immune response, induced by infection of respiratory syncytial virus (RSV), has been linked to asthma development, but it remains unclear how the response is initiated. Here, we reported that the high-mobility group box-1 (HMGB1) protein promotes the type 2 response in the later stage of RSV infection. In mice, we found that type 2 cytokines were elevated in the later stages, which were strongly diminished after administration of anti-HMGB1 antibodies. Further investigation revealed that HMGB1 expression was localized to CC10+ club cells in the lung. In the clinic, levels of HMGB1 in nasopharyngeal aspirates in hospitalized infants with RSV bronchiolitis [median (interquartile range) 161.20 ng/ml (68.06–221.30)] were significantly higher than those without lower respiratory tract infections [21.94 ng/ml (12.12–59.82); P < 0.001]. Moreover, higher levels of HMGB1 correlated with clinical severity. These results reveal a link between viral infection and the asthma-like type 2 responses that are associated with long-term consequences.

scholarly journals High Mobility Group Box 1 (HMGB1) Activates an Autophagic Response to Oxidative Stress

2011 ◽  
Vol 15 (8) ◽  
pp. 2185-2195 ◽  
Author(s):  
Daolin Tang ◽  
Rui Kang ◽  
Kristen M. Livesey ◽  
Herbert J. Zeh ◽  
Michael T. Lotze
Keyword(s):  
Oxidative Stress ◽  
High Mobility ◽  
High Mobility Group

scholarly journals The Proinflammatory Cytokine High-Mobility Group Box-1 Mediates Retinal Neuropathy Induced by Diabetes

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Ahmed M. Abu El-Asrar ◽  
Mohammad Mairaj Siddiquei ◽  
Mohd Imtiaz Nawaz ◽  
Karel Geboes ◽  
Ghulam Mohammad
Keyword(s):  
Tyrosine Hydroxylase ◽  
Proinflammatory Cytokine ◽  
Caspase 3 ◽  
High Mobility ◽  
Diabetic Rats ◽  
High Mobility Group ◽  
Hmgb1 Protein ◽  
Epiretinal Membranes ◽  
Glyoxalase 1 ◽  
Extracellular Signal

To test the hypothesis that increased expression of proinflammatory cytokine high-mobility group box-1 (HMGB1) in epiretinal membranes and vitreous fluid from patients with proliferative diabetic retinopathy and in retinas of diabetic rats plays a pathogenetic role in mediating diabetes-induced retinal neuropathy. Retinas of 1-month diabetic rats and HMGB1 intravitreally injected normal rats were studied using Western blot analysis, RT-PCR and glutamate assay. In addition, we studied the effect of the HMGB1 inhibitor glycyrrhizin on diabetes-induced biochemical changes in the retina. Diabetes and intravitreal injection of HMGB1 in normal rats induced significant upregulation of HMGB1 protein and mRNA, activated extracellular signal-regulated kinase 1 and 2 (ERK1/2), cleaved caspase-3 and glutamate; and significant downregulation of synaptophysin, tyrosine hydroxylase, glutamine synthetase, and glyoxalase 1. Constant glycyrrhizin intake from the onset of diabetes did not affect the metabolic status of the diabetic rats, but it significantly attenuated diabetes-induced upregulation of HMGB1 protein and mRNA, activated ERK1/2, cleaved caspase-3, and glutamate. In the glycyrrhizin-fed diabetic rats, the decrease in synaptophysin, tyrosine hydroxylase, and glyoxalase 1 caused by diabetes was significantly attenuated. These findings suggest that early retinal neuropathy of diabetes involves upregulated expression of HMGB1 and can be ameliorated by inhibition of HMGB1.

C-reactive protein induces high-mobility group box-1 protein release through activation of p38MAPK in macrophage RAW264.7 cells

2008 ◽  
Vol 17 (3) ◽  
pp. 129-138 ◽  
Author(s):  
Ko-ichi Kawahara ◽  
Kamal Krishna Biswas ◽  
Masako Unoshima ◽  
Takashi Ito ◽  
Kiyoshi Kikuchi ◽  
...  
Keyword(s):  
High Mobility ◽  
Protein Release ◽  
High Mobility Group ◽  
Raw264.7 Cells ◽  
C Reactive Protein ◽  
Reactive Protein

scholarly journals Anabolic Properties of High Mobility Group Box Protein-1 in Human Periodontal Ligament CellsIn Vitro

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
Michael Wolf ◽  
Stefan Lossdörfer ◽  
Piero Römer ◽  
Rogerio Bastos Craveiro ◽  
James Deschner ◽  
...  
Keyword(s):  
Periodontal Ligament ◽  
Tooth Movement ◽  
Therapeutic Potential ◽  
Marker Gene ◽  
Orthodontic Tooth Movement ◽  
High Mobility ◽  
High Mobility Group ◽  
Nodule Formation ◽  
Hmgb1 Protein ◽  
Pdl Cells

High mobility group box protein-1 (HMGB1) is mainly recognized as a chemoattractant for macrophages in the initial phase of host response to pathogenic stimuli. However, recent findings provide evidence for anabolic properties in terms of enhanced proliferation, migration, and support of wound healing capacity of mesenchymal cells suggesting a dual role of the cytokine in the regulation of immune response and subsequent regenerative processes. Here, we examined potential anabolic effects of HMGB1 on human periodontal ligament (PDL) cells in the regulation of periodontal remodelling, for example, during orthodontic tooth movement. Preconfluent human PDL cells (hPDL) were exposed to HMGB1 protein and the influence on proliferation, migration, osteogenic differentiation, and biomineralization was determined by MTS assay, real time PCR, immunofluorescence cytochemistry, ELISA, and von Kossa staining. HMGB1 protein increased hPDL cell proliferation, migration, osteoblastic marker gene expression, and protein production as well as mineralized nodule formation significantly. The present findings support the dual character of HMGB1 with anabolic therapeutic potential that might support the reestablishment of the structural and functional integrity of the periodontium following periodontal trauma such as orthodontic tooth movement.

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