Cells migrating to sites of tissue damage in response to the danger signal HMGB1 require NF-κB activation

Palumbo, Roberta; Gálvez, Beatriz G.; Pusterla, Tobias; Marchis, Francesco De; Cossu, Giulio; Marcu, Kenneth B.; Bianchi, Marco E.

doi:10.1083/jcb.200704015

Cited by 235 publications

(102 citation statements)

References 28 publications

(44 reference statements)

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“…A number of studies have indicated that HMGB1 acts as a potential host cell-derived, chemotactic factor to promote migration of several cell types (Degryse and de Virgilio, 2003). These cells include neurites (Fages et al, 2000), smooth muscle cells (Degryse et al, 2001), myoblast cells (Fages et al, 2000), tumor cells (Fages et al, 2000; Huttunen et al, 2002; Palumbo and Bianchi, 2004; Palumbo et al, 2004), hepatic stellate cells (Wang et al, 2013b), stem cells (Palumbo et al, 2009; Palumbo et al, 2007; Palumbo et al, 2004), endothelial cells (Furlani et al, 2012), keratinocytes (Ranzato et al, 2009), monocytes (Pedrazzi et al, 2007; Rouhiainen et al, 2004), dendritic cells (Dumitriu et al, 2007; Yang et al, 2007), and neutrophils (Orlova et al, 2007; Palumbo et al, 2009; van Zoelen et al, 2009). The potential mechanisms include HMGB1-mediated signaling transduction (e.g., ERK (Degryse et al, 2001; Ranzato et al, 2009), Cdc42 (Fages et al, 2000), Rac (Fages et al, 2000), JNK (Wang et al, 2013b), PI3K/AKT (Wang et al, 2013b) and Src (Palumbo et al, 2009)), transcriptional factor activation (NF-κB), and chemokine production.…”

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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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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“…These results suggested that RAGE signaling plays an important role in microglia migration and that factors in the culture medium might stimulate basal microglia migration in a RAGE-mediated manner. One candidate RAGE agonist with the ability to stimulate basal microglia transmigration is high mobility group protein 1 (HMGB1), an established RAGE ligand (51-53) released by activated macrophages (54) and implicated in RAGE-dependent migration of several cell types (55)(56)(57)(58). Indeed, the microglia culture medium contained HMGB1 (Fig.…”

Section: S100b Stimulates Microglia Transmigration In a Rage-dependentmentioning

confidence: 99%

S100B Protein Stimulates Microglia Migration via RAGE-dependent Up-regulation of Chemokine Expression and Release

Bianchi

Kastrisianaki

Giambanco

et al. 2011

Journal of Biological Chemistry

205

173

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The Ca 2؉ -binding protein of the EF-hand type, S100B, is abundantly expressed in and secreted by astrocytes, and release of S100B from damaged astrocytes occurs during the course of acute and chronic brain disorders. Thus, the concept has emerged that S100B might act an unconventional cytokine or a damage-associated molecular pattern protein playing a role in the pathophysiology of neurodegenerative disorders and inflammatory brain diseases. S100B proinflammatory effects require relatively high concentrations of the protein, whereas at physiological concentrations S100B exerts trophic effects on neurons. Most if not all of the extracellular (trophic and toxic) effects of S100B in the brain are mediated by the engagement of RAGE (receptor for advanced glycation end products). We show here that high S100B stimulates murine microglia migration in Boyden chambers via RAGE-dependent activation of Src kinase, Ras, PI3K, MEK/ERK1/2, RhoA/ROCK, Rac1/JNK/AP-1, Rac1/ NF-B, and, to a lesser extent, p38 MAPK. Recruitment of the adaptor protein, diaphanous-1, a member of the formin protein family, is also required for S100B/RAGE-induced migration of microglia. The S100B/RAGE-dependent activation of diaphanous-1/Rac1/JNK/AP-1, Ras/Rac1/NF-B and Src/Ras/PI3K/ RhoA/diaphanous-1 results in the up-regulation of expression of the chemokines, CCL3, CCL5, and CXCL12, whose release and activity are required for S100B to stimulate microglia migration. Lastly, RAGE engagement by S100B in microglia results in up-regulation of the chemokine receptors, CCR1 and CCR5. These results suggests that S100B might participate in the pathophysiology of brain inflammatory disorders via RAGEdependent regulation of several inflammation-related events including activation and migration of microglia. S100B is a Ca 2ϩ -binding protein of the EF-hand type abundantly expressed in astrocytes (1). S100B has been implicated in the regulation of astrocyte shape, migration, proliferation and differentiation via activation of the Src/PI3K module and PI3K-dependent stimulation of Akt and RhoA activities and hence of the supramolecular organization of F-actin (2). S100B also regulates the state of assembly of microtubules and type III intermediate filaments (3) and the cytosolic Ca 2ϩ concentration (4). In addition to having intracellular regulatory activities, S100B also exerts extracellular effects. Indeed, astrocytes secrete the protein constitutively and to a larger extent under the action of several stimuli including the proinflammatory cytokine, TNF-␣ (see for review Ref. 1). Moreover, levels of brain S100B are elevated in the aging brain and in several pathological conditions such as Alzheimer disease, brain infarct, epilepsy, and infectious diseases, as well as in Down syndrome (5, 6) in consequence of S100B human gene mapping to chromosome 21q22.3 (7). For example, hypertrophic astrocytes in peri-infarct areas and in neuritic plaques in Alzheimer disease and Down syndrome show elevated expression levels of S100B, and S100B can be detected outside hypert...

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“…In addition, activation of NF-B and ERK1/2 is required for initiation of pro-inflammatory responses (Marui et al 1993;Lockyer et al 1998;Rose et al 2010). HMGB1 is known to activate NF-B and ERK1/2 in vascular inflammatory responses (Park et al 2006;Palumbo et al 2007;Yang and Tracey 2010). Therefore, we evaluated the effects of VCN and SCL on the activation of NF-B and ERK1/2 by HMGB1.…”

Section: Effects Of Vcn and Scl On Hmgb1-stimulated Production Of Tnfmentioning

confidence: 98%

Antiseptic effect of vicenin-2 and scolymoside from Cyclopia subternata (honeybush) in response to HMGB1 as a late sepsis mediator in vitro and in vivo

Lee

Yoon

Kim

et al. 2015

Can. J. Physiol. Pharmacol.

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Cyclopia subternata is a medicinal plant commonly used in traditional medicine to relieve pain. In this study, we investigated the antiseptic effects and underlying mechanisms of vicenin-2 and scolymoside, which are 2 active compounds from C. subternata that act against high mobility group box 1 (HMGB1)-mediated septic responses in human umbilical vein endothelial cells (HUVECs) and mice. The antiseptic activities of vicenin-2 and scolymoside were determined by measuring permeability, neutrophil adhesion and migration, and activation of proinflammatory proteins in HMGB1-activated HUVECs and mice. According to the results, vicenin-2 and scolymoside effectively inhibited lipopolysaccharide-induced release of HMGB1, and suppressed HMGB1-mediated septic responses such as hyperpermeability, the adhesion and migration of leukocytes, and the expression of cell adhesion molecules. In addition, vicenin-2 and scolymoside suppressed the production of tumor necrosis factor-α and interleukin 6, and activation of nuclear factor-κB and extracellular regulated kinases 1/2 by HMGB1. Collectively, these results indicate that vicenin-2 and scolymoside could be a potential therapeutic agents for the treatment of various severe vascular inflammatory diseases via inhibition of the HMGB1 signaling pathway.

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Cells migrating to sites of tissue damage in response to the danger signal HMGB1 require NF-κB activation

Cited by 235 publications

References 28 publications

HMGB1 in health and disease

HMGB1 in health and disease

S100B Protein Stimulates Microglia Migration via RAGE-dependent Up-regulation of Chemokine Expression and Release

Antiseptic effect of vicenin-2 and scolymoside from Cyclopia subternata (honeybush) in response to HMGB1 as a late sepsis mediator in vitro and in vivo

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