HMGB1: A signal of necrosis

Raucci, Angela; Palumbo, Roberta; Bianchi, Marco E.

doi:10.1080/08916930701356978

Cited by 159 publications

(115 citation statements)

References 44 publications

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“…Our finding that asbestos promotes necrotic cell death is in agreement with the histopathological observation that asbestos causes chronic inflammatory reaction in both humans and rodents (1,6,36). In contrast, apoptotic cell death is not associated with the release of HMGB1 from cells and with the consequent inflammation (22,27,30). Thus, apoptosis may not be nearly as relevant to the pathogenesis of asbestos-related disease as necrosis.…”

Section: Discussionsupporting

confidence: 80%

“…It was then shown that necrosis can occur as a consequence of acute ATP depletion (24)(25)(26). Recent findings indicate that necrosis can also be a regulated event, which involves the activation of PARP, depletion of intracellular ATP, and release of high-mobility group box 1 protein (HMGB1), a factor that starts and promotes inflammation (20)(21)(22)(23)(25)(26)(27)(28).…”

mentioning

confidence: 99%

“…Necrosis, unlike apoptosis, causes inflammation (20)(21)(22)(23). Necrosis was initially viewed as an uncontrolled form of cell death caused by overwhelming extrinsic injury.…”

mentioning

confidence: 99%

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Programmed necrosis induced by asbestos in human mesothelial cells causes high-mobility group box 1 protein release and resultant inflammation

Yang

Rivera

Jube

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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232

252

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Asbestos carcinogenesis has been linked to the release of cytokines and mutagenic reactive oxygen species (ROS) from inflammatory cells. Asbestos is cytotoxic to human mesothelial cells (HM), which appears counterintuitive for a carcinogen. We show that asbestos-induced HM cell death is a regulated form of necrosis that links to carcinogenesis. Asbestos-exposed HM activate poly(ADP-ribose) polymerase, secrete H 2 O 2 , deplete ATP, and translocate high-mobility group box 1 protein (HMGB1) from the nucleus to the cytoplasm, and into the extracellular space. The release of HMGB1 induces macrophages to secrete TNF-α, which protects HM from asbestos-induced cell death and triggers a chronic inflammatory response; both favor HM transformation. In both mice and hamsters injected with asbestos, HMGB1 was specifically detected in the nuclei, cytoplasm, and extracellular space of mesothelial and inflammatory cells around asbestos deposits. TNF-α was coexpressed in the same areas. HMGB1 levels in asbestos-exposed individuals were significantly higher than in nonexposed controls (P < 0.0001). Our findings identify the release of HMGB1 as a critical initial step in the pathogenesis of asbestos-related disease, and provide mechanistic links between asbestos-induced cell death, chronic inflammation, and carcinogenesis. Chemopreventive approaches aimed at inhibiting the chronic inflammatory response, and especially blocking HMGB1, may decrease the risk of malignant mesothelioma among asbestos-exposed cohorts.mesothelioma | tumor necrosis factor-alpha | carcinogenesis | biomarker | chemoprevention

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Section: Discussionsupporting

confidence: 80%

mentioning

confidence: 99%

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Programmed necrosis induced by asbestos in human mesothelial cells causes high-mobility group box 1 protein release and resultant inflammation

Yang

Rivera

Jube

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

232

252

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“…may receive Tim-3 signaling from endothelial cells to increase their proliferative potential and apoptosis-resistance, thus benefiting tumor metastasis. HMGB1 has been identified as a proinflammatory cytokine which can be secreted by different cells or released from necrotic cells (22)(23)(24). Higher HMGB1 levels have been found in tumors with greater metastatic potential (25).…”

Section: Discussionmentioning

confidence: 99%

Endothelial cell-expressed Tim-3 facilitates metastasis of melanoma cells by activating the NF-κB pathway

Yuan²,

Liu³

et al. 2010

Oncol Rep

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Abstract. T cell immunoglobulin and mucin domain-3 (Tim-3)is originally recognized as a receptor of Th1 cells. We found that Tim-3 could be expressed in endothelial cells after stimulation with tumor cell-released TLR4 ligand. Tim-3 expressed by endothelial cells does not function as the receptor of galectin-9, but mediates the interaction of endothelial cells with tumor cells. The engagement of endothelial cellexpressed Tim-3 with a non-galectin 9 putative receptor on B16 melanoma cells could trigger the NF-κB signaling pathway in B16 cells. The activated NF-κB not only promoted the proliferation of B16 cells, but also enhanced apoptosis resistance of B16 cells by up-regulating Bcl-2 and Bcl-xL and down-regulating Bax. Consistently, Tim-3 facilitated the survival of B16 cells in the blood stream, arrested in the lung and following invasion, resulted in more metastatic nodules in the lung. These findings suggest that endothelial cell-expressed Tim-3 increases tumor cell metastatic potential by facilitating tumor cell intravasation, survival in blood stream and extravasation. Thus, antiinflammation or blockade of Tim-3 may contribute to the prevention of metastasis.

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“…When stressed, some cell types are able to secrete HMGB1 and this results in an inflammatory response (for review, see Raucci et al, 2007). Moreover, HMGB1 is also passively released by necrotic cells, which has the same inflammatory consequence (Scaffidi et al, 2002).…”

Section: Chromatin and The Dna Damage Responsementioning

confidence: 99%

Chromatin structure and DNA double-strand break responses in cancer progression and therapy

Downs

2007

Oncogene

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Defects in the detection and repair of DNA double-strand breaks (DSBs) have been causatively linked to tumourigenesis. Moreover, inhibition of DNA damage responses (DDR) can increase the efficacy of cancer therapies that rely on generation of damaged DNA. DDR must occur within the context of chromatin, and there have been significant advances in recent years in understanding how the modulation and manipulation of chromatin contribute to this activity. One particular covalent modification of a histone variant-the phosphorylation of H2AX-has been investigated in great detail and has been shown to have important roles in DNA DSB responses and in preventing tumourigenesis. These studies are reviewed here in the context of their relevance to cancer therapy and diagnostics. In addition, there is emerging evidence for contributions by proteins involved in mediating higher order structure to DNA DSB responses. The contributions of a subset of these proteins-linker histones and high-mobility group box (HMGB) proteins-to DDR and their potential significance in tumourigenesis are discussed.

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HMGB1: A signal of necrosis

Cited by 159 publications

References 44 publications

Programmed necrosis induced by asbestos in human mesothelial cells causes high-mobility group box 1 protein release and resultant inflammation

Programmed necrosis induced by asbestos in human mesothelial cells causes high-mobility group box 1 protein release and resultant inflammation

Endothelial cell-expressed Tim-3 facilitates metastasis of melanoma cells by activating the NF-κB pathway

Chromatin structure and DNA double-strand break responses in cancer progression and therapy

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