HMGB1 in the pathogenesis of ultraviolet-induced ocular surface inflammation

Han, S-J.; Hj, Min; Sc, Yoon; Ko, Eun A.; Park, Sung Jin; Jh, Yoon; Shin, Jeon Soo; Seo, Kyoung Yul

doi:10.1038/cddis.2015.199

Cited by 26 publications

(12 citation statements)

References 51 publications

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“…Oxidation of HMGB1 attenuates its proinflammatory activity (55), particularly during apoptosis (56), when induction of immunological tolerance by apoptotic cells requires caspase-dependent oxidation of the protein (57) to eliminate danger signaling (58). UV exposure (which likely induces photo-oxidative damage by UV-induced ROS and not necrosis) seems to stimulate HMGB1 release by keratinocytes (59) or conjunctival epithelial cells as a stressorin (60). In addition, it was also reported that UV irradiation induces a TLR4/MYD88-driven neutrophilic skin inflammatory response in animal models initiated by HMGB1 release from damaged keratinocytes (61).…”

Section: Stressorins Respond To Stressmentioning

confidence: 99%

Alarmins: Feel the Stress

Rider

Voronov

Dinarello

et al. 2017

The Journal of Immunology

157

117

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Over the last decade, danger-associated molecular pattern molecules, or alarmins, have been recognized as signaling mediators of sterile inflammatory responses after trauma and injury. In contrast with the accepted passive release models suggested by the "danger hypothesis," it was recently shown that alarmins can also directly sense and report damage by signaling to the environment when released from live cells undergoing physiological stress, even without loss of subcellular compartmentalization. In this article, we review the involvement of alarmins such as IL-1α, IL-33, IL-16, and high-mobility group box 1 in cellular and physiological stress, and suggest a novel activity of these molecules as central initiators of sterile inflammation in response to nonlethal stress, a function we denote "stressorins." We highlight the role of posttranslational modifications of stressorins as key regulators of their activity and propose that targeted inhibition of stressorins or their modifiers could serve as attractive new anti-inflammatory treatments for a broad range of diseases.

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Section: Stressorins Respond To Stressmentioning

confidence: 99%

Alarmins: Feel the Stress

Rider

Voronov

Dinarello

et al. 2017

The Journal of Immunology

157

117

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“…1,2,9 In our previous study, we proved that reactive oxygen species (ROS) was important in translocation of HMGB1. 10 Hypoxia is defined as a low level of oxygen in the environment and oxygen concentrations of o5% are usually considered to be hypoxic. 11,12 In the nasal cavity, many pathologic diseases are related to tissue hypoxia.…”

Section: Introductionmentioning

confidence: 99%

ROS-dependent HMGB1 secretion upregulates IL-8 in upper airway epithelial cells under hypoxic condition

et al. 2017

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High-mobility group box 1 (HMGB1) mediates various functions according to the location. We tried to investigate the role of HMGB1 in upper airway under hypoxic conditions. We cultured primary normal human nasal epithelium (NHNE) cells under hypoxic conditions and evaluated the movement of HMGB1 by western blotting, immunofluorescence, and enzyme-linked immunosorbent assay (ELISA). Reactive oxygen species (ROS) level was evaluated to estimate the translocation mechanism of HMGB1. The role of secreted HMGB1 was evaluated by ELISA assay. Furthermore, we collected human nasal mucosa samples and nasal lavage fluids from patients conditioned under hypoxic and non-hypoxic environment, and compared the expression of HMGB1 in human nasal mucosa samples by immunohistochemistry and the levels of HMGB1 in lavage fluids using ELISA assay. Hypoxia induced translocation of HMGB1 into the extracellular area and it was dependent on ROS produced by dual oxidase 2. Secreted HMGB1 was involved in the upregulation of interleukin (IL)-8. In human samples, HMGB1 was translocated from nucleus to the cytoplasm in hypoxic-conditioned nasal mucosa. HMGB1 was increased in nasal lavage samples of chronic rhinosinusitis patients, whose sinus mucosa was supposed to be hypoxic as compared with controls. We suggest that HMGB1 is secreted in hypoxic condition via ROS-dependent mechanism and secreted HMGB1 participates in IL-8 upregulation mediating inflammatory response.

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“…Extracellular HMGB1 binds to receptors for advanced glycation end products on cell surfaces to induce cellular signalling in inflammation, cell differentiation and cell migration . Many external stresses, which include reactive oxygen species (ROS) from ultraviolet (UV) irradiation and intracellular enzymatic reactions, are known to trigger release of HMGB1 from various cells, such as macrophages, monocytes and neutrophils . Release of HMGB1 from keratinocytes is similarly induced by UVB irradiation, potentially linking HMGB1 with certain pathological conditions of the skin …”

mentioning

confidence: 99%

“…15,16 Many external stresses, which include reactive oxygen species (ROS) from ultraviolet (UV) irradiation and intracellular enzymatic reactions, are known to trigger release of HMGB1 from various cells, such as macrophages, monocytes and neutrophils. [17][18][19][20] Release of HMGB1 from keratinocytes is similarly induced by UVB irradiation, potentially linking HMGB1 with certain pathological conditions of the skin. 21 Released HMGB1 may act as a damage-associated molecular pattern (DAMP) molecule, inducing immune responses through proinflammatory molecular production.…”

mentioning

confidence: 99%