The isolation of three new high mobility group nuclear proteins

Goodwin, Graham H.; Brown, Elizabeth; Walker, John M.; Johns, Ernest W.

doi:10.1016/0005-2795(80)90260-3

Cited by 31 publications

(6 citation statements)

References 11 publications

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“…Johns and his colleagues further demonstrated that HMG proteins can be extracted by 5% perchloric acid and have 40–50 % α-helix structures which are sensitive to pH around neutrality and the urea concentration (Baker et al, 1976; Cary et al, 1976). In addition to HMG1 and 2, Ernest Johns and colleagues separated other HMG proteins with perchloric acid extracts and divided HMG in two groups: the higher (e.g., HMG-1 and HMG-2) and lower (e.g., HMG-14, HMG-17, and HMG-Y) molecular weight proteins (Brown et al, 1980; Cockerill et al, 1983; Goodwin et al, 1980). Currently, a number of HMG proteins have been discovered in several species with the following properties (Bustin et al, 1990): (1) extractable from chromatin using 0.35 M NaCl; (2) soluble in 5% perchloric acid or tricloroacetic acid; (3) < 30 kDa in molecular weight with a high content of charged amino acids; (4) rapidly mobile in polyacrylamide gels; (5) sensitive to extensive post-translational modifications such as phosphorylation, acetylation, and poly-ADP-ribosylation; and (6) tissue- and development-dependent expression.…”

Section: Introduction and Historical Backgroundmentioning

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: Introduction and Historical Backgroundmentioning

confidence: 99%

HMGB1 in health and disease

Kang

Chen

Zhang

et al. 2014

Molecular Aspects of Medicine

801

828

View full text Add to dashboard Cite

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“…Based on its mobility during polyacrylamide gel electrophoresis, Goodwin et al termed the proteins "high mobility group, " or HMG proteins; however, the group of proteins that migrated more slowly during polyacrylamide gel electrophoresis were termed "low-mobility group" proteins. HMG proteins were therefore divided into two groups based on their molecular weight: higher-HMG-1 and HMG-2 (now HMGB1 and HMGB2), lower-HMG-14 and HMG-17 (now HMGN1 and HMGN2), and HMG-I, -Y (now HMGA1a and HMGA1b) (3)(4)(5)(6)(7)(8)(9).…”

Section: Introductionmentioning

confidence: 99%

Immunological Significance of HMGB1 Post-Translational Modification and Redox Biology

et al. 2020

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Most extracellular proteins are secreted via the classical endoplasmic reticulum (ER)/Golgi-dependent secretion pathway; however, some proteins, including a few danger-associated molecular patterns (DAMPs), are secreted via non-classical ER/Golgi-independent secretion pathways. The evolutionarily conserved high mobility group box1 (HMGB1) is a ubiquitous nuclear protein that can be released by almost all cell types. HMGB1 lacks signal peptide and utilizes diverse non-canonical secretion mechanisms for its extracellular export. Although the post-translational modifications of HMGB1 were demonstrated, the oxidation of HMGB1 and secretion mechanisms are not highlighted yet. We currently investigated that peroxiredoxins I and II (PrxI/II) induce the intramolecular disulfide bond formation of HMGB1 in the nucleus. Disulfide HMGB1 is preferentially transported out of the nucleus by binding to the nuclear exportin chromosome-region maintenance 1 (CRM1). We determined the kinetics of HMGB1 oxidation in bone marrow-derived macrophage as early as a few minutes after lipopolysaccharide treatment, peaking at 4 h while disulfide HMGB1 accumulation was observed within the cells, starting to secrete in the late time point. We have shown that HMGB1 oxidation status, which is known to determine the biological activity in extracellular HMGB1, is crucial for the secretion of HMGB1 from the nucleus. This review summarizes selected aspects of HMGB1 redox biology relevant to the induction and propagation of inflammatory diseases. We implicate the immunological significance and the need for novel HMGB1 inhibitors through mechanism-based studies.

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“…HMG14 elutes in peaks C and D together with some other minor components. The previously described minor HMG-like proteins HMG18, HMG19A and HMG19B [4] elute in peaks B and H but were not further investigated in this study. A protein with similar electrophoretic mobility to HMG14 elutes in peak E but its ultraviolet spectrum shows that it has a high content of aromatic amino acids including tryptophan and is therefore probably not of the lowmolecular-mass HMG14/17 group.…”

Section: Resultsmentioning

confidence: 99%

Fractionation by high-performance liquid chromatography of the low-molecular-mass high-mobility-group (HMG) chromosomal proteins present in proliferating rat cells and an investigation of the HMG proteins present in virus transformed cells

et al. 1985

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The low-molecular-mass high-mobility-group (HMG) proteins from young rat thymus nuclei were fractionated by high-performance liquid chromatography. Two proteins analogous to calf HMG14 and HMGl7 were found together with a third major component HMGI similar to that found in HeLa cells [Lund et al. (1983) FEBS Lelt. 152, 363-1671. HMGI has as amino acid composition similar to but distinct from HMG14 and HMG17. The three proteins form a family of proteins with HMG14 having an amino acid composition intermediate between HMG17 and HMGI. HMGI is present in proliferating fibroblasts and embryos but is present in very low levels in rat liver, a non-dividing tissue, supporting the notion that HMGI is required for proliferating cells. Fibroblasts transformed with avian sarcoma virus have high levels of HMGI and an additional band HMGI' but the presence of HMGI and HMGI' is not dependent on a functional src gene product.Mammalian and avian cells contain two major lowmolecular-mass HMG proteins, HMG14 and HMG17 [I], which have been implicated in modifying the chromatin structure of transcriptionally active genes [2]. Previous studies have shown that all terminally differentiated cells so far studied have these two proteins plus some minor components termed HMG18, HMG19A and HMG19B [3, 41. However recently Lund et al. [5] isolated an HMG-like protein (HMGI) from Hela cells with an electrophoretic migration on acid/ urea gels slower than calf HMG14 and HMG17 and which had an amino acid composition somewhat different from that of Hela HMG17 and that of the avian and mammalian proteins described in this laboratory [3]. It was suggested that this protein may be specific to proliferating cells. However it was not clear whether or not this protein was the human equivalent of HMG14. It was also not known whether this protein was species-specific (i.e. human) or tissue-specific.In this paper we report our results from studies with rat fibroblasts transformed with the avian sarcoma virus in which we observed, in addition to the normal HMG14 and HMG17, a doublet of proteins migrating behind HMG14 on acid/urea gels, in the position reported for human HMGI. Also rat thymus from 4 -6-week-old rats, a tissue which has a high content of proliferating cells at this age, contained an additional single protein migrating near the HMGI position. Rat liver with few dividing cells did not have these additional bands. In order to investigate the relationship between these additional HMG proteins found in proliferating rat tissues, the HMGI protein found in Hela cells, and the wellcharacterized HMG14 and HMG17 protein, we have fractionated the low-molecular-mass HMG proteins in proliferating rat thymus by HPLC and have compared the proteins with those previously isolated. We show that rat thymus nuclei have, in addition to HMG14 and HMGl7 a major additional component with amino acid composition similar to Hela HMGI. This rat HMGI is quite distinct from rat HMG14 and HMGl7 and the minor HMG18/19 proteins. EXPERIMENTAL METHODS Fractionation of HMG pr...

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The isolation of three new high mobility group nuclear proteins

Cited by 31 publications

References 11 publications

HMGB1 in health and disease

HMGB1 in health and disease

Immunological Significance of HMGB1 Post-Translational Modification and Redox Biology

Fractionation by high-performance liquid chromatography of the low-molecular-mass high-mobility-group (HMG) chromosomal proteins present in proliferating rat cells and an investigation of the HMG proteins present in virus transformed cells

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