High Mobility Group B1 Protein Research Articles

Antibody–drug conjugates harboring a kinesin spindle protein inhibitor with immunostimulatory properties

ABSTRACT Antibody–drug conjugates (ADCs) are used to target cancer cells by means of antibodies directed to tumor-associated antigens, causing the incorporation of a cytotoxic payload into target cells. Here, we characterized the mode of action of ADC costing of a TWEAKR-specific monoclonal antibody conjugated to a small molecule kinesin spindle protein (KSP) inhibitor (KSPi). These TWEAKR-KSPi-ADCs showed strong efficacy in a TWEAKR expressing CT26 colon cancer model in mice. TWEAKR-KSPi-ADCs controlled the growth of CT26 colon cancers in immunodeficient as well as in immunocompetent mice. However, when treated with suboptimal doses, TWEAKR-KSPi-ADCs were still active in immunocompetent but not in immunodeficient mice, indicating that TWEAKR-KSPi-ADCs act – in addition to the cytotoxic mode of action – through an immunological mechanism. Indeed, in vitro experiments performed with a cell-permeable small molecule KSPi closely related to the active payload released from the TWEAKR-KSPi-ADCs revealed that KSPi was capable of stimulating several hallmarks of immunogenic cell death (ICD) on three different human cancer cell lines: cellular release of adenosine triphosphate (ATP) and high mobility group B1 protein (HMGB1), exposure of calreticulin on the cell surface as well as a transcriptional type-I interferon response. Further, in vivo experiments confirmed that treatment with TWEAKR-KSPi-ADCs activated immune responses via enhancing the infiltration of CD4+ and CD8+ T lymphocytes in tumors and the local production of interferon-γ, interleukin-2, and tumor necrosis factor-α. In conclusion, the antineoplastic effects of TWEAKR-KSPi-ADCs can partly be attributed to its ICD-stimulatory properties.

Role of HMGB1 in Post-traumatic Endoplasmic Reticulum Stress in Rat Lung Tissues.

To explore the role of high mobility group B1 （HMGB1） protein in the post-traumatic endoplasmic reticulum stress （ERS） in rat lung tissues. The rat model of acute lung injury was established by crushing the hind limbs of rats with standard weight. The first experiment was to divide rats into postural control group and crush groups （6 h, 18 h and 30 h after crushing）. The second experiment was to divide rats into postural control group, 18 h crush group, HMGB1 inhibitor sodium butyrate （SB） group and 18 h crush+SB group. The protein expression changes of HMGB1 and ERS- related proteins （GRP78, caspase-12, CHOP and IRE1α） in rat lung tissues were detected with Western blotting. Meanwhile, the pathological changes of rat lungs were observed by HE stain. Compared with the postural control group, the expression levels of ERS-related proteins （GRP78, caspase-12, CHOP and IRE1α） and HMGB1 protein in rat lung tissues by crushing the hind limbs of rats were obviously increased. The protein levels reduced at 30 h after crushing but were still higher than those of postural control group and obvious pathological changes of acute lung injury were observed simultaneously in rats. Compared with the 18 h crush group, the expression levels of the ERS-related proteins and HMGB1 protein in rat lung tissues were attenuated in 18 h crush+SB group, and the pathological changes of rat lung injury began to alleviate. HMGB1-ERS pathway activated by traumatic stress can lead to acute lung injury in rats.

Chronic saline exposures interfere with basal and induced immunity in striped catfish (Pangasianodon hypophthalmus, sauvage) exposed to virulent strain of Edwardsiella ictaluri

Hyperosmotic stress has often been investigated from osmoregulation perspectives while the effects of such stress on the immune capacity remain largely unexplored. In this study, stenohaline striped catfish Pangasianodon hypophthalmus were submitted to gradual hyperosmotic stress during 20 days up to 10 and 20 ppt. Hyperosmotic stress was followed by an infection with a highly virulent strain of an intracellular gram negative bacteria, Edwardsiella ictaluri, responsible for Enteric Septicemia of Catfish (ESC). Osmoregulatory (i.e. plasma osmolarity and NaK ATPase activity), immune (i.e. lysozyme, complement, respiratory burst, white blood cells, heat shock protein and high-mobility group B1 protein) parameters and mortality rates were monitored. Moreover, a label free quantitative proteomics workflow was performed to study how salinity affects the proteome of kidney in healthy and infected catfish. The flow consisted in initial global profiling of relative peptide abundances (by LC/MS, peak area quantification based on extracted ion currents) followed by MS/MS identification. In total, 496 differentially expressed proteins were analyzed in DAVID interface to isolate functional pathways and categories involved in the response to bacterial infection and which were influenced by salinity changes. Pathways and functional categories, particularly those related to stress, immunity and ion homeostasis, are discussed. We hypothesized that prolonged exposure to mild and high hyperosmotic stress may induce chronic sterile inflammation and disruption of immune homeostasis that may lead to excessive inflammatory response and serious ESC disease.

An acetylome peptide microarray reveals specificities and deacetylation substrates for all human sirtuin isoforms

Sirtuin enzymes regulate metabolism and aging processes through deacetylation of acetyl-lysines in target proteins. More than 6,800 mammalian acetylation sites are known, but few targets have been assigned to most sirtuin isoforms, hampering our understanding of sirtuin function. Here we describe a peptide microarray system displaying 6,802 human acetylation sites for the parallel characterisation of their modification by deacetylases. Deacetylation data for all seven human sirtuins obtained with this system reveal isoform-specific substrate preferences and deacetylation substrate candidates for all sirtuin isoforms, including Sirt4. We confirm malate dehydrogenase protein as a Sirt3 substrate and show that peroxiredoxin 1 and high-mobility group B1 protein are deacetylated by Sirt5 and Sirt1, respectively, at the identified sites, rendering them likely new in vivo substrates. Our microarray platform enables parallel studies on physiological acetylation sites and the deacetylation data presented provide an exciting resource for the identification of novel substrates for all human sirtuins.

Pharmacologic Suppression of Inflammation by a Diphenyldifluoroketone, EF24, in a Rat Model of Fixed-Volume Hemorrhage Improves Survival

An exaggerated release of proinflammatory cytokines and accompanying inflammation contributes to the development of multiple organ failure after hemorrhagic shock. Here, we tested the nuclear factor (NF) κ-light-chain-enhancer of activated B cell (NF-κB)-mediated transcriptional control of inflammatory pathways as a target in the management of hemorrhage-induced inflammation. We performed a study in a rat model of fixed-volume hemorrhage to investigate the anti-inflammatory effects of the diphenyldifluoroketone EF24 [3,5-bis(2-fluorobenzylidene)piperidin-4-one], an NF-κB inhibitor, in lung tissue. EF24 treatment (0.4 mg/kg) significantly prevented the upregulation of inflammatory biomarkers in rats subjected to 50% hemorrhage and preserved the pulmonary histology in hemorrhaged rats. The lung tissue from treated rats showed marked suppression of the hemorrhage-mediated induction of Toll-like receptor 4, phospho-p65 NF-κB, inducible nitric-oxide synthase, heme oxygenase-1, and cyclooxygenase-2 (COX-2). The hemorrhage-induced COX-2 activity was also significantly inhibited by the EF24 treatment. At the same time, EF24 induced nuclear factor (erythroid-derived 2)-like 2-mediated protective mechanisms against oxidative stress. EF24 also reduced hemorrhage-induced lung myeloperoxidase activity. The plasma levels of proinflammatory tumor necrosis factor-α, interleukin (IL)-6, IL-1α, and IL-1β were lower in EF24-treated rats than in untreated rats. Moreover, there was a significant reduction in the pulmonary expression of high-mobility group B1 protein. These biochemical effects were accompanied by a significant improvement in the survival of rats administered with EF24 as compared with the rats receiving vehicle control (P < 0.05). Overall, the results suggest that EF24 attenuates hemorrhage-induced inflammation and could serve as a salutary anti-inflammatory agent in resuscitation strategies.

Insulin infusion suppresses while glucose infusion induces Toll-like receptors and high-mobility group-B1 protein expression in mononuclear cells of type 1 diabetes patients

The purpose of this study was to determine whether an insulin infusion exerts an anti-inflammatory effect and whether the infusion of small amounts of glucose results in oxidative and inflammatory stress in patients with type 1 diabetes. Ten patients with type 1 diabetes were infused with either 2 U/h of insulin with 100 ml 5% dextrose/h to or just dextrose (100 ml/h) or physiological saline (100 ml/h) for 4 h after an overnight fast on three separate days. Blood samples were collected at 0, 2, 4, and 6 h. Insulin with glucose infusion led to the maintenance of euglycemia and a significant suppression of reactive oxygen species (ROS) generation, p47(phox) expression, Toll-like receptor (TLR)-4, TLR-2, TLR-1, CD14, high-mobility group-B1 (HMGB1), p38 mitogen-activated protein (MAP) kinase, c-Jun NH2-terminal kinase (JNK)-1, and platelet/endothelial cell adhesion molecule expression and a fall in serum concentrations of C-reactive protein, HMGB1, and rapid upon activation T cell expressed and secreted. Glucose infusion led to an increase in plasma glucose concentration from 115 (fasting) to 215 (at 4 and 6 h) mg/dl and to an increase in ROS generation, the expression of TLR-4, TLR-2, TLR-1, HMGB1, p38 MAP kinase, and JNK-1, and plasma concentrations of HMGB1. While insulin reduces indexes of oxidative and inflammatory stress in patients with type 1 diabetes, even small amounts of glucose (20 g over 4 h) induce oxidative and inflammatory stress. These effects are reflected in TLR, p38 MAP kinase, and HMGB1 expression. The induction of significant oxidative and inflammatory stress by small amounts of glucose in patients with type 1 diabetes may have important pathophysiological and therapeutic implications.

High mobility group B1 protein interacts with its receptor RAGE in tumor cells but not in normal tissues

The high mobility group box 1 (HMGB1) protein is an abundant non-histone component of chromatin well known for its two DNA binding domains, HMG box A and HMG box B. The main characteristics of the HMGB1 protein as an 'architectural' factor are its ability to recognize and bind with high affinity to distorted DNA and its ability to induce kinks in linear DNA fragments. The HMGB1 protein has been correlated to cancer progression. An elevated expression of HMGB1 occurred in certain types of primary tumor, including melanoma and colon, prostate, pancreatic and breast cancers, and in the majority of cases HMGB1 is associated with invasion and metastasis. The main signaling pathway is activated through the interaction of HMGB1 with its Receptor for Advanced Glycation End products (RAGE). Certain data indicate that an elevated expression of RAGE and HMGB1 is not always a prerequisite of poor prognosis of tumor development. The cellular localization of the ligand/receptor pair also requires consideration. The data concerning the expression of HMGB1 protein and its receptor RAGE in various tissues and tumor cells reflect the overall production of the proteins. However, they do not refer to their cellular localization and there is no direct evidence for the formation of a stable complex between them. In the present study, we investigated the subcellular distribution of HMGB1 and its receptor RAGE in various rat organs compared to Guerin ascites tumor cells. In the normal tissues the proteins exist in their soluble form, whereas in the tumor cells they are insoluble and membrane-bound. HMGB1 forms a stable complex with RAGE only in the protein extract derived from the cancer cells predominantly in the membrane fraction.

Molecular Mechanism Underlying RAG1/RAG2 Synaptic Complex Formation

Two lymphoid cell-specific proteins, RAG1 and RAG2 (RAG), initiate V(D)J recombination by assembling a synaptic complex with recombination signal sequences (RSSs) abutting two different antigen receptor gene coding segments, and then introducing a DNA double strand break at the end of each RSS. Despite the biological importance of this system, the structure of the synaptic complex, and the RAG protein stoichiometry and arrangement of DNA within the synaptosome, remains poorly understood. Here we applied atomic force microscopy to directly visualize and characterize RAG synaptic complexes. We report that the pre-cleavage RAG synaptic complex contains about twice the protein content as a RAG complex bound to a single RSS, with a calculated mass consistent with a pair of RAG heterotetramers. In the synaptic complex, the RSSs are predominantly oriented in a side-by-side configuration with no DNA strand crossover. The mass of the synaptic complex, and the conditions under which it is formed in vitro, favors an association model of assembly in which isolated RAG-RSS complexes undergo synapsis mediated by RAG protein-protein interactions. The replacement of Mg2+ cations with Ca2+ leads to a dramatic change in protein stoichiometry for all RAG-RSS complexes, suggesting that the cation composition profoundly influences the type of complex assembled.

Role of high mobility group protein B1 in cancer

As a nonhistone chromosomal protein,high mobility group B1 ( HMGB1 ) is involed in a va-riety of biological processes, including transcription, DNA repair, V (D) J recombination, differentiation, develop-ment,and extracellular signaling. Increased expression of HMGB1 is associated with the proliferation, invasion and metastasis of many tumor types. Furthermore, HMGB1 overexpression inhibits apoptosis of cancer cells and tumor suppressor genes,resuhing in the genesis and development of tumor. HMGB1 plays roles in activation of plasminogen and matrix metalloproteases,reorganization of cytoskeleton. HMGB1 can also be involved in DNA damage repair,preventing cell carcinogenesis. HMGB1 can increase the sensitivity of breast cancer cells to γ-ray radiation. Key words: HMGB1 protein; Neoplasm metastasis; Radiobiology

Redox properties of the A-domain of the HMGB1 protein

The High Mobility Group B1 (HMGB1) protein plays important roles in both intracellular (reductive) and extracellular (oxidative) environments. We have carried out quantitative investigations of the redox chemistry involving Cys22 and Cys44 of the HMGB1 A-domain, which form an intramolecular disulfide bond. Using NMR spectroscopy, we analyzed the real-time kinetics of the redox reactions for the A-domain in glutathione and thioredoxin systems, and also determined the standard redox potential. Thermodynamic experiments showed that the Cys22–Cys44 disulfide bond stabilizes the folded state of the protein. These data suggest that the oxidized HMGB1 may accumulate even in cells under oxidative stress. Structured summary MINT- 6795963: txn (uniprotkb: P10599) and HMGB1 (uniprotkb: P09429) bind (MI: 0408) by nuclear magnetic resonance (MI: 0077)

High Mobility Group B1 Protein Suppresses the Human Plasmacytoid Dendritic Cell Response to TLR9 Agonists

Plasmacytoid dendritic cells (PDC) are innate immune effector cells that are recruited to sites of chronic inflammation, where they modify the quality and nature of the adaptive immune response. PDCs modulate adaptive immunity in response to signals delivered within the local inflammatory milieu by pathogen- or damage-associated molecular pattern, molecules, and activated immune cells (including NK, T, and myeloid dendritic cells). High mobility group B1 (HMGB1) is a recently identified damage-associated molecular pattern that is released during necrotic cell death and also secreted from activated macrophages, NK cells, and mature myeloid dendritic cells. We have investigated the effect of HMGB1 on the function of PDCs. In this study, we demonstrate that HMGB1 suppresses PDC cytokine secretion and maturation in response to TLR9 agonists including the hypomethylated oligodeoxynucleotide CpG- and DNA-containing viruses. HMGB1-inhibited secretion of several proinflammatory cytokines including IFN-alpha, IL-6, TNF-alpha, inducible protein-10, and IL-12. In addition, HMGB1 prevented the CpG induced up-regulation of costimulatory molecules on the surface of PDC and potently suppressed their ability to drive generation of IFN-gamma-secreting T cells. Our observations suggest that HMGB1 may play a critical role in regulating the immune response during chronic inflammation and tissue damage through modulation of PDC function.

Cloning and characterization of the canine receptor for advanced glycation end products

Metastasis is one of the major problems when dealing with malignant neoplasias. Accordingly, the finding of molecular targets, which can be addressed to reduce tumour metastasising, will have significant impact on the development of new therapeutic approaches. Recently, the receptor for advanced glycation end products (RAGE)–high mobility group B1 (HMGB1) protein complex has been shown to have significant influence on invasiveness, growth and motility of tumour cells, which are essential characteristics required for metastatic behaviour. A set of in vitro and in vivo approaches showed that blocking of this complex resulted in drastic suppression of tumour cell growth. Due to the similarities of human and canine cancer the dog has joined the common rodent animal model for therapeutic and preclinical studies. However, complete characterisation of the protein complex is a precondition to a therapeutic approach based on the blocking of the RAGE–HMGB1 complex to spontaneously occurring tumours in dogs. We recently characterised the canine HMGB1 gene and protein completely. Here we present the complete characterisation of the canine RAGE gene including its 1384 bp mRNA, the 1215 bp protein coding sequence, the 2835 bp genomic structure, chromosomal localisation, gene expression pattern, and its 404 amino acid protein. Furthermore we compared the CDS of six different canine breeds and screened them for single nucleotide polymorphisms.

The Enhanced Tumor Selectivity of an Oncolytic Vaccinia Lacking the Host Range and Antiapoptosis Genes SPI-1 and SPI-2

The ability of cancer cells to evade apoptosis may permit survival of a recombinant vaccinia lacking antiapoptotic genes in cancer cells compared with normal cells. We have explored the deletion of two vaccinia virus host range/antiapoptosis genes, SPI-1 and SPI-2, for their effects on the viral replication and their ability to induce cell death in infected normal and transformed cells in vitro. Indeed, in three paired normal and transformed cell types, the SPI-1 and SPI-2 gene-deleted virus (vSP) preferentially replicates in transformed cells or p53-null cells when compared with their normal counterparts. This selectivity may be derived from the fact that vSP-infected normal cells died faster than infected cancer cells. A fraction of infected cells died with evidence of necrosis as shown by both flow cytometry and detection of high-mobility group B1 protein released from necrotic cells into the culture supernatant. When administered to animals, vSP retains full ability to replicate in tumor tissues, whereas replication in normal tissues is greatly diminished. In a model of viral pathogenesis, mice treated with vSP survived substantially longer when compared with mice treated with the wild-type virus. The mutant virus vSP displayed significant antitumoral effects in an MC38 s.c. tumor model in both nude (P < 0.001) and immunocompetent mice (P < 0.05). We conclude that this recombinant vaccinia vSP shows promise for oncolytic virus therapy. Given its enhanced tumor selectivity, improved safety profile, and substantial oncolytic effects following systemic delivery in murine models, it should also serve as a useful vector for tumor-directed gene therapy.

The N-terminal domain of thrombomodulin sequesters high-mobility group-B1 protein, a novel antiinflammatory mechanism

Thrombomodulin (TM) is an endothelial anticoagulant cofactor that promotes thrombin-mediated formation of activated protein C (APC). We have found that the N-terminal lectin-like domain (D1) of TM has unique antiinflammatory properties. TM, via D1, binds high-mobility group-B1 DNA-binding protein (HMGB1), a factor closely associated with necrotic cell damage following its release from the nucleus, thereby preventing in vitro leukocyte activation, in vivo UV irradiation-induced cutaneous inflammation, and in vivo lipopolysaccharide-induced lethality. Our data also demonstrate antiinflammatory properties of a peptide spanning D1 of TM and suggest its therapeutic potential. These findings highlight a novel mechanism, i.e., sequestration of mediators, through which an endothelial cofactor, TM, suppresses inflammation quite distinctly from its anticoagulant cofactor activity, thereby preventing the interaction of these mediators with cell surface receptors on effector cells in the vasculature.

The N-terminal domain of thrombomodulin sequesters high-mobility group-B1 protein, a novel antiinflammatory mechanism

The N-terminal domain of thrombomodulin sequesters high-mobility group-B1 protein, a novel antiinflammatory mechanism

HMGB1 is an endogenous immune adjuvant released by necrotic cells.

Immune responses against pathogens require that microbial components promote the activation of antigen-presenting cells (APCs). Autoimmune diseases and graft rejections occur in the absence of pathogens; in these conditions, endogenous molecules, the so-called 'innate adjuvants', activate APCs. Necrotic cells contain and release innate adjuvants; necrotic cells also release high-mobility group B1 protein (HMGB1), an abundant and conserved constituent of vertebrate nuclei. Here, we show that necrotic HMGB1(-/-) cells have a reduced ability to activate APCs, and HMGB1 blockade reduces the activation induced by necrotic wild-type cell supernatants. In vivo, HMGB1 enhances the primary antibody responses to soluble antigens and transforms poorly immunogenic apoptotic lymphoma cells into efficient vaccines.

Intracellular high mobility group B1 protein (HMGB1) represses HIV-1 LTR-directed transcription in a promoter- and cell-specific manner

We investigated whether the high mobility group B 1 (HMGB1), an abundant nuclear protein in all mammalian cells, affects HIV-1 transcription. Intracellular expression of human HMGB1 repressed HIV-1 gene expression in epithelial cells. This inhibitory effect of HMGB1 was caused by repression of long terminal repeat (LTR)-mediated transcription. Other viral promoters/enhancers, including simian virus 40 or cytomegalovirus, were not inhibited by HMGB1. In addition, HMGB1 inhibition of HIV-1 subtype C expression was dependent on the number of NFκB sites in the LTR region. The inhibitory effect of HMGB1 on viral gene expression observed in HeLa cells was confirmed by an upregulation of viral replication in the presence of antisense HMGB1 in monocytic cells. In contrast to what was found in HeLa cells and monocytic cells, endogenous HMGB1 expression did not affect HIV-1 replication in unstimulated Jurkat cells. Thus, intracellular HMGB1 affects HIV-1 LTR-directed transcription in a promoter- and cell-specific manner.

DNA sequence of the long terminal repeat of human immunodeficiency virus type 1 subtype A through G.

AIDS Research and Human RetrovirusesVol. 15, No. 5 DNA Sequence of the Long Terminal Repeat of Human Immunodeficiency Virus Type 1 Subtype A through GMojgan H. Naghavi, Mika O. Salminen, Anders Sonnerborg, and Anders VahlneMojgan H. NaghaviSearch for more papers by this author, Mika O. SalminenSearch for more papers by this author, Anders SonnerborgSearch for more papers by this author, and Anders VahlneSearch for more papers by this authorPublished Online:5 Jul 2004https://doi.org/10.1089/088922299311240AboutSectionsPDF/EPUB Permissions & CitationsPermissionsDownload CitationsTrack CitationsAdd to favorites Back To Publication ShareShare onFacebookTwitterLinked InRedditEmail FiguresReferencesRelatedDetailsCited byAn emerging and variant viral promoter of HIV-1 subtype C exhibits low-level gene expression noise19 September 2021 | Retrovirology, Vol. 18, No. 1BK polyomavirus diversity—Why viral variation matters3 March 2020 | Reviews in Medical Virology, Vol. 30, No. 4Transcription: Insights From the HIV-1 PromoterFunctional Incompatibility between the Generic NF-κB Motif and a Subtype-Specific Sp1III Element Drives the Formation of the HIV-1 Subtype C Viral PromoterJournal of Virology, Vol. 90, No. 16Multiple NF-κB Sites in HIV-1 Subtype C Long Terminal Repeat Confer Superior Magnitude of Transcription and Thereby the Enhanced Viral PredominanceJournal of Biological Chemistry, Vol. 287, No. 53Sequence Insertions in the HIV Type 1 Subtype C Viral Promoter Predominantly Generate an Additional NF-κB Binding Site Mahesh Bachu, Anil Babu Mukthey, Rajesh V. 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McCutchan5 July 2004 | AIDS Research and Human Retroviruses, Vol. 19, No. 12Intracellular high mobility group B1 protein (HMGB1) represses HIV-1 LTR-directed transcription in a promoter- and cell-specific mannerVirology, Vol. 314, No. 1Protein Tyrosyl Phosphatases in T Cell Activation: Implication for Human Immunodeficiency Virus Transcriptional ActivityCharacterization of the South African HIV Type 1 Subtype C Complete 5′ Long Terminal Repeat, nef, and Regulatory Genes Thomas J. Scriba, Tania de Villiers, Florette K. Treurnicht, Jan zur Megede, Susan W. 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Hunt and C. T. Tiemessen5 July 2004 | AIDS Research and Human Retroviruses, Vol. 16, No. 3Long Terminal Repeat Promoter/Enhancer Activity of Different Subtypes of HIV Type 1 Mojgan H. Naghavi, Stefan Schwartz, Anders Sonnerborg, and Anders Vahlne5 July 2004 | AIDS Research and Human Retroviruses, Vol. 15, No. 14 Volume 15Issue 5Mar 1999 To cite this article:Mojgan H. Naghavi, Mika O. Salminen, Anders Sonnerborg, and Anders Vahlne.DNA Sequence of the Long Terminal Repeat of Human Immunodeficiency Virus Type 1 Subtype A through G.AIDS Research and Human Retroviruses.Mar 1999.485-488.http://doi.org/10.1089/088922299311240Published in Volume: 15 Issue 5: July 5, 2004PDF download