High levels of HMG1‐2 protein expression in the cytoplasm and nucleus of hydrocortisone sensitive amphibian thymocytes

Guillet, F; Tournefier, Annick; Denoulet, Philippe; Capony, Jean‐Paul; Kerfourn, Fabienne; Charlemagne, Jacques

doi:10.1016/0248-4900(90)90341-y

Cited by 11 publications

(5 citation statements)

References 43 publications

(41 reference statements)

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“…Subsequent studies investigated the levels and distribution of HMGB1 between the nucleus and cytoplasm in different cells and tissues. Localization of HMGB1 in the cytoplasm has been confirmed in living fibroblasts (Einck et al, 1984), thymocytes (Guillet et al, 1990) and several different tissues (e.g., liver, kidney, heart, and lung) (Kuehl et al, 1984). The normal ratio of nuclear to cytoplasmic HMGB1 is about 30:1 (Kuehl et al, 1984).…”

Section: Hmgb1 Functionmentioning

confidence: 92%

HMGB1 in health and disease

Kang

Chen

Zhang

et al. 2014

Molecular Aspects of Medicine

803

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: 92%

HMGB1 in health and disease

Kang

Chen

Zhang

et al. 2014

Molecular Aspects of Medicine

803

828

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“…One of the top 20 proteins (ranked 14th) was identified as a High Mobility Group1/2-like protein (HMG1/2-like). HMG proteins are known as abundant nonhistone components of chromatin involved in the organization of chromatin structure. − Immunofluorescence staining using anti-HMG1 antibody showed that the HMG proteins are predominantly associated with heterochromatin, including the centromeres of human and mouse chromosomes . In addition, HMG proteins were predicted to play a role in positioning of the centromere DNA .…”

Section: Resultsmentioning

confidence: 99%

Isolation and Proteomics Analysis of Barley Centromeric Chromatin Using PICh

Zeng

Jiang

2016

J. Proteome Res.

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Identification of proteins that are directly or indirectly associated with a specific DNA sequence is often an important goal in molecular biology research. Proteomics of isolated chromatin fragments (PICh) is a technique used to isolate chromatin that contains homologous DNA sequence to a specific nucleic acid probe. All proteins directly and indirectly associated with the DNA sequences that hybridize to the probe are then identified by proteomics.1 We used the PICh technique to isolate chromatin associated with the centromeres of barley (Hordeum vulgare) by using a 2'-deoxy-2'fluoro-ribonucleotides (2'-F RNA) probe that is homologous to the AGGGAG satellite DNA specific to barley centromeres. Proteins associated with the barley centromeric chromatin were then isolated and identified by mass spectrometry. Both alpha-cenH3 and beta-cenH3, the two centromeric histone H3 variants associated with barley centromeres, were positively identified. Interestingly, several different H2A and H2B variants were recovered in the PIChed chromatin. The limitations and future potential of PICh in plant chromatin research are discussed.

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“…Other direct or indirect mechanisms by which DEX could influence astroglial maturation may be also involved. Glucocorticoids can up-regulate the high mobility group 1 and 2 proteins (HMG 1 and 2) involved in chromatin remodelling during cell differentiation [22], and DEX stimulates astrocytes to release the HMG-1 protein that promotes membrane-mediated differentiative processes [23].…”

Section: Discussionmentioning

confidence: 99%

Growth Factors and Steroid Mediated Regulation of Cytoskeletal Protein Expression in Serum-Deprived Primary Astrocyte Cultures

et al. 2008

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In this research we aimed to investigate the interactions between growth factors (GFs) and dexamethasone (DEX) on cytoskeletal proteins GFAP and vimentin (VIM) expression under different experimental conditions. Condition I: 24 h pretreatment with bFGF, subsequent 72 h switching in serum-free medium (SFM) and final addition of GFs, alone or by two in the last 24 h, after a prolonged (60 h) DEX treatment. Condition II: 36 h pretreatment with DEX (with bFGF in the last 24 h), followed by SFM for 60 h and final addition for 24 h with growth factors alone or two of them together. Western blot analysis data showed a marked GFAP expression in cultures submitted to Condition I comparing results to untreated or treated controls. VIM expression was instead significantly reduced after GFs addition in the last 24 h of 60 h DEX treatment, respect to control DEX-pretreated ones. Referring data to untreated controls, VIM expression was significantly enhanced after GFs addition. GFAP showed also a significant increase in astrocytes submitted to Condition II, respect to untreated or treated control cultures. VIM expression was up and down regulated under Condition II. Collectively, our findings evidence an interactive dialogue between GFs and DEX in astroglial cultures, co-pretreated with DEX and bFGF, regulating cytoskeletal network under stressful conditions.

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High levels of HMG1‐2 protein expression in the cytoplasm and nucleus of hydrocortisone sensitive amphibian thymocytes

Cited by 11 publications

References 43 publications

HMGB1 in health and disease

HMGB1 in health and disease

Isolation and Proteomics Analysis of Barley Centromeric Chromatin Using PICh

Growth Factors and Steroid Mediated Regulation of Cytoskeletal Protein Expression in Serum-Deprived Primary Astrocyte Cultures

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