Increase of high mobility group box chromosomal protein 1 in eosinophilic chronic rhinosinusitis with nasal polyps

Chen, Daishi; Mao, Mingfeng; Bellussi, Luisa; Passàli, Desiderio; Chen, Lei

doi:10.1002/alr.21294

Cited by 24 publications

(28 citation statements)

References 39 publications

(67 reference statements)

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“…Available data indicated HMGB1 expression mainly in the inflammatory infiltrates (especially eosinophilic ones), not in epithelial cells [21]. Moreover, significant differences in the HMGB1 protein level as well as the messenger RNA levels of HMGB1 were found between non-eosinophilic CRSwNP and controls [29]. This observation is consistent with our findings.…”

Section: Discussionsupporting

confidence: 92%

High motility group box 1 (HMGB1) protein and its receptor for advanced glycation end products (RAGE) expression in chronic rhinosinusitis without nasal polyps

Dżaman

Zagor

Molińska-Glura

et al. 2015

Folia Histochem Cytobiol.

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Introduction. Chronic rhinosinusitis (CRS) affects 14% of the world population. The high motility group box 1 (HMGB1) protein triggers inflammation, cell proliferation and cell survival through its receptor for advanced glycation end products (RAGE) upon release from stressed or necrotic cells. The aim of the study was to analyze the expression and function of HMGB1 and RAGE in CRS, providing more information about HMGB1 signaling pathway in CRS, to determine its potential clinical significance. Material and methods. Thirty-seven patients with CRS and 26 normal controls (NC) were enrolled in this study. Classification of disease severity using the SNOT-20 questionnaire, nasal endoscopy, CT scan, assessment of allergy status, microbiological and cytological analysis was performed in patients. Fresh sinus mucosa samples were obtained and analyzed by immunohistochemistry for HMGB1 and RAGE expression in epithelial cells. ELISA assay was performed to evaluate the concentration of HMGB1 in the patients' sera. Results. No differences were found in HMGB1 immunoexpression between CRS patients and NC, however there was a highly significant difference in RAGE immunoexpression between both groups. There was a correlation between RAGE expression and number of tissue-infiltrating lymphocytes. Further, RAGE expression positively correlated with disease severity and a positive history for allergies. Conclusions. Interaction of HMGB1 and RAGE might be relevant to CRS pathomechanisms leading to sinus mucosa hyperproliferation. CRS pathogenesis might be especially related to the RAGE overexpression correlated with disease severity and allergy.

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Section: Discussionsupporting

confidence: 92%

High motility group box 1 (HMGB1) protein and its receptor for advanced glycation end products (RAGE) expression in chronic rhinosinusitis without nasal polyps

Dżaman

Zagor

Molińska-Glura

et al. 2015

Folia Histochem Cytobiol.

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“…Another study [18] by our research group has recently confirmed the hypothesis that up-regulation of HMGB1 could be a significant marker of eosinophilic CRSwNP and contribute to the pathogenesis of CRSwNP along with IL-5, IL-8 and TNF-α (fig. 2).…”

Section: Hmgb1 and Rhinosinusitissupporting

confidence: 59%

Rhinosinusal Inflammation and High Mobility Group Box 1 Protein: A New Target for Therapy

Bellussi¹,

Cocca²,

Chen³

et al. 2016

ORL

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Background/Aims: High mobility group box 1 (HMGB1) is a protein belonging to the class of damage-associated molecular pattern molecules, which activates innate immunity and powerful inflammatory factors. The aim of this review is to show the importance of HMGB1 in the pathogenesis of nasal inflammatory diseases and to suggest that inhibition of HMGB1 may be an innovative therapeutic target. Methods: We used immunohistochemistry to study whether HMGB1 increases in chronic rhinosinusitis with nasal polyps and whether its expression is associated with eosinophils and inflammatory cytokines. Using primary cultures of human nasal epithelial cells, we localised lipopolysaccharide-induced active translocation and release of HMGB1 by immunofluorescence assay and Western blot. Results: Patients with severe symptoms have the highest HMGB1 serum levels. Glycyrrhetic acid inhibits the chemotactic and mitogenic function of HMGB1, binding to the hydrophobic residues that delimit the pockets in box A and B. Conclusions: Chronic inflammatory diseases of the nose and paranasal sinuses are increasingly prevalent and are a financial burden for society. HMGB1 has been shown to play a role in several inflammatory diseases of otolaryngological interest. The inhibition of HMGB1 may be an innovative therapeutic target for patients with chronic upper airway inflammatory diseases having nasal obstruction as a major symptom.

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“…RAGE may be required for HMGB1-mediated eosinophil activation (Curran and Bertics, 2011; Lotfi et al, 2009). Upregulation of HMGB1 contributes to the pathogenesis of eosinophilic chronic rhinosinusitis with nasal polyps (Chen et al, 2014b). …”

Section: Hmgb1 Functionmentioning

confidence: 99%

HMGB1 in health and disease

Kang

Chen

Zhang

et al. 2014

Molecular Aspects of Medicine

801

828

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Complex genetic and physiological variations as well as environmental factors that drive emergence of chromosomal instability, development of unscheduled cell death, skewed differentiation, and altered metabolism are central to the pathogenesis of human diseases and disorders. Understanding the molecular bases for these processes is important for the development of new diagnostic biomarkers, and for identifying new therapeutic targets. In 1973, a group of non-histone nuclear proteins with high electrophoretic mobility was discovered and termed High-Mobility Group (HMG) proteins. The HMG proteins include three superfamilies termed HMGB, HMGN, and HMGA. High-mobility group box 1 (HMGB1), the most abundant and well-studied HMG protein, senses and coordinates the cellular stress response and plays a critical role not only inside of the cell as a DNA chaperone, chromosome guardian, autophagy sustainer, and protector from apoptotic cell death, but also outside the cell as the prototypic damage associated molecular pattern molecule (DAMP). This DAMP, in conjunction with other factors, thus has cytokine, chemokine, and growth factor activity, orchestrating the inflammatory and immune response. All of these characteristics make HMGB1 a critical molecular target in multiple human diseases including infectious diseases, ischemia, immune disorders, neurodegenerative diseases, metabolic disorders, and cancer. Indeed, a number of emergent strategies have been used to inhibit HMGB1 expression, release, and activity in vitro and in vivo. These include antibodies, peptide inhbitiors, RNAi, anti-coagulants, endogenous hormones, various chemical compounds, HMGB1-receptor and signaling pathway inhibition, artificial DNAs, physical strategies including vagus nerve stimulation and other surgical approaches. Future work further investigating the details of HMGB1 localizationtion, structure, post-translational modification, and identifccation of additional partners will undoubtedly uncover additional secrets regarding HMGB1’s multiple functions.

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Increase of high mobility group box chromosomal protein 1 in eosinophilic chronic rhinosinusitis with nasal polyps

Abstract: Upregulation of HMGB1 could be a significant marker typically in eosinophilic CRSwNP and it may also contribute to the pathogenesis of CRSwNP along with IL-5, IL-8, and TNF-α.

Cited by 24 publications

References 39 publications

High motility group box 1 (HMGB1) protein and its receptor for advanced glycation end products (RAGE) expression in chronic rhinosinusitis without nasal polyps

High motility group box 1 (HMGB1) protein and its receptor for advanced glycation end products (RAGE) expression in chronic rhinosinusitis without nasal polyps

Rhinosinusal Inflammation and High Mobility Group Box 1 Protein: A New Target for Therapy

HMGB1 in health and disease

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