HMGB1 translocation and release mediate cigarette smoke–induced pulmonary inflammation in mice through a TLR4/MyD88-dependent signaling pathway

Cheng, Yao; Wang, Dan; Wang, Bin; Li, Huanan; Xiong, Junjie; Xu, Shuyun; Chen, Quan; Tao, Kun; Yang, Xiaoyan; Zhu, Yu; He, Sirong

doi:10.1091/mbc.e16-02-0126

Cited by 57 publications

(58 citation statements)

References 43 publications

(79 reference statements)

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“…As shown here, TLR4 signaling is associated with a specific downstream pathway that includes the JAK/STAT pathway . LPS commonly activates TLR4 and JAK signals and sequentially phosphorylates STAT1, resulting in the release of HMGB1.…”

Section: Resultsmentioning

confidence: 78%

Degradation of histone deacetylase 4 via the TLR4/JAK/STAT1 signaling pathway promotes the acetylation of high mobility group box 1 (HMGB1) in lipopolysaccharide‐activated macrophages

Park

Kim

et al. 2018

FEBS Open Bio

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High mobility group box 1 ( HMGB 1) has been proposed as crucial in the pathogenesis of many diseases including sepsis. Acetylation of HMGB 1 prevents its entry into the nucleus and leads to its secretion from the cell where it can trigger inflammation. We hypothesized that histone deacetylase 4 ( HDAC 4) controls the acetylation of HMGB 1 in lipopolysaccharide ( LPS )‐stimulated RAW 264.7 cells via the janus kinase ( JAK )/signal transducer and activator of transcription ( STAT ) pathway. The results showed that LPS treatment promoted the degradation of HDAC 4 in a proteasome‐dependent manner, which led to HMGB 1 acetylation. In LPS ‐activated RAW 264.7 cells, treatment with TAK ‐242 (a toll like receptor 4 inhibitor) and pyridone 6 (a JAK inhibitor) significantly inhibited HDAC 4 degradation and acetylation of HMGB 1, and thus prevented secretion of HMGB 1. Decreased phosphorylation of STAT 1 was also observed. Interestingly, HDAC 4 overexpression significantly prevented the acetylation and secretion of HMGB 1 in both RAW 264.7 cells and isolated murine peritoneal macrophages. We conclude that HDAC 4 might be a useful target for the treatment of sepsis.

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Section: Resultsmentioning

confidence: 78%

Degradation of histone deacetylase 4 via the TLR4/JAK/STAT1 signaling pathway promotes the acetylation of high mobility group box 1 (HMGB1) in lipopolysaccharide‐activated macrophages

Park

Kim

et al. 2018

FEBS Open Bio

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“…In line with these findings, another study demonstrated that HMGB-1 treatment increased the levels of proinflammatory markers in the lungs of wildtype mice but not in TLR4-knockout mice [57]. An in vitro study demonstrated that blocking TLR4 or MyD88 inhibited HMGB-1-induced proinflammatory cytokine production in mouse tracheal epithelial cells [58]. Furthermore, Das et al found that the interaction of HMGB-1 and TLR5 initiated NF-κB activation via MyD88, resulting in proinflammatory cytokine production in vivo [59].…”

Section: Figmentioning

confidence: 58%

“…Combined deficiency of TLR2/TLR4, or of MyD88 alone, attenuated HMGB-1-induced expression of MMP-3 and MMP-13 in chondrocytes [56]. In line with these findings, another study demonstrated that HMGB-1 treatment increased the levels of proinflammatory markers in the lungs of wildtype mice but not in TLR4-knockout mice [57]. An in vitro study demonstrated that blocking TLR4 or MyD88 inhibited HMGB-1-induced proinflammatory cytokine production in mouse tracheal epithelial cells [58].…”

Section: Figmentioning

confidence: 74%

Emerging Role of High Mobility Group Box-1 in Thrombosis-Related Diseases

Pei

et al. 2018

Cell Physiol Biochem

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High mobility group box-1 (HMGB-1), a typical damage-associated molecular pattern protein released from various cells, was first identified in 1973. It is usually stored in the nuclei of cells. Several modifications of HMGB-1 promote its translocation to the cytosol, and it is actively or passively released from cells. When outside of the cells, HMGB-1is crucial in inflammation. It exerts its biological functions via interaction with its receptors, including receptor for advanced glycation end products (RAGE) and Toll-like receptor 4(TLR4). A large number of studies showed a close link between inflammation and thrombosis. This review demonstrated the increased expression of HMGB-1 in thrombosis-related diseases, including coronary artery disease, stroke, peripheral arterial disease, disseminated intravascular coagulation, and venous thrombosis. Besides, it summarized the current understanding of the emerging link between HMGB-1 and thrombosis from three aspects: platelet, NETs, and coagulation and fibrinolysis factors. Finally, it explored the possible therapeutic strategies targeting HMGB-1 for treating thrombosis-related diseases.

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“…Another study demonstrated that HMGB1 treatment increases the levels of proinflammatory markers in the lungs of wild-type mice but not in TLR-4-/-mice. An in vitro study demonstrated that pharmacological inhibition of TLR-4 or MyD88 also inhibited HMGB1-induced proinflammatory cytokine production [39]. Furthermore, it has been demonstrated that HMGB1 induces proinflammatory cytokine production in vivo via the TLR-4-MyD88-NF-κB pathway [40] (Fig.…”

Section: Hmgb1 Signaling For the Initiation Of Different Diseasesmentioning

confidence: 97%

Sterile Inflammatory Role of High Mobility Group Box 1 Protein: Biological Functions and Involvement in Disease

et al. 2018

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High mobility group box 1 protein (HMGB1), a sterile inflammatory molecule and damage-associated molecular pattern (DAMP) released from various cells during stress has been implicated in inflammation. Several reports show that there is a direct relationship between inflammation and cardiovascular diseases (CVDs) such as thrombosis, hypertension, insulin resistance, preeclampsia, etc. Here, we intend to summarize the concept of the emerging link between HMGB1 and CVDs. Furthermore, we will discuss the possible therapeutic strategies that target HMGB1 for the treatment of different CVDs.

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HMGB1 translocation and release mediate cigarette smoke–induced pulmonary inflammation in mice through a TLR4/MyD88-dependent signaling pathway

Cited by 57 publications

References 43 publications

Degradation of histone deacetylase 4 via the TLR4/JAK/STAT1 signaling pathway promotes the acetylation of high mobility group box 1 (HMGB1) in lipopolysaccharide‐activated macrophages

Degradation of histone deacetylase 4 via the TLR4/JAK/STAT1 signaling pathway promotes the acetylation of high mobility group box 1 (HMGB1) in lipopolysaccharide‐activated macrophages

Emerging Role of High Mobility Group Box-1 in Thrombosis-Related Diseases

Sterile Inflammatory Role of High Mobility Group Box 1 Protein: Biological Functions and Involvement in Disease

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