The intracellular distribution and function of the high mobility group chromosomal proteins

Einck, Leo; Bustin, Michael

doi:10.1016/0014-4827(85)90539-7

Cited by 240 publications

(134 citation statements)

References 116 publications

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“…It is generally accepted that anti-HMG1/2 antibodies are antinuclear antibodies (ANA) [24]. However, these proteins are not exclusively distributed in the nucleus, but rather abundant in the cytoplasm [25,26]. In our study, anti-HMG1/2 antibodies did not stain the nucleus of ethanolor formalin-fixed neutrophils on IIF.…”

Section: Discussioncontrasting

confidence: 68%

Novel autoantigens of perinuclear anti-neutrophil cytoplasmic antibodies (P-ANCA) in ulcerative colitis: non-histone chromosomal proteins, HMG1 and HMG2

Sobajima

Ozaki

Osakada

et al. 1997

Clinical and Experimental Immunology

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SUMMARYAnti-neutrophil cytoplasmic antibodies (ANCA) in sera from ulcerative colitis (UC) patients have been described as reacting with proteins in the granules of human neutrophils such as cathepsin G and lactoferrin and with yet unidentified antigens. Here we report the existence of a new member of perinuclear ANCA (P-ANCA) in UC patients. In the previous study, we found that UC patients had a novel P-ANCA against neutrophil 28-kD protein. In this study, we purified the same antigens from HL-60 lysates by using reversed phase high-performance liquid chromatography, and revealed that the 28-kD antigen consisted of two different proteins. The N-terminus amino acids of these proteins are identical with those of high mobility group (HMG) non-histone chromosomal proteins HMG1 and HMG2. Immunoblotting analysis of human neutrophil lysates using rabbit anti-HMG1/2 antisera revealed a single band of 28 kD, and the 28-kD band detected by immunoblotting analysis using patient's serum IgG completely disappeared after preincubation with a mixture of HMG1 and HMG2. Furthermore, rabbit anti-HMG1/2 antisera showed a perinuclear staining pattern in indirect immunofluorescence studies using ethanol-fixed neutrophils. These data demonstrate that HMG1 and HMG2 are novel target antigens of P-ANCA. HMG1 and HMG2 are distributed in the nuclei and cytoplasm of eukaryotic cells and act as transcription factors. Their intracellular localization and functions are distinct from those of the previously reported granular antigens of P-ANCA.

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Section: Discussioncontrasting

confidence: 68%

Novel autoantigens of perinuclear anti-neutrophil cytoplasmic antibodies (P-ANCA) in ulcerative colitis: non-histone chromosomal proteins, HMG1 and HMG2

Sobajima

Ozaki

Osakada

et al. 1997

Clinical and Experimental Immunology

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“…HMG-1,2 protein is the most abundant and ubiquitous low molecular weight non-histone nuclear protein (MW approximately 28 000). 20 Several experiments have indicated that HMG-1,2 has transcriptional activation potential and enhances gene expression without dependence on the type of promoter or transgene. 25 In the present study, using cationic liposomes combined with HMG-1,2, we examined the tumoricidal activity of…”

Section: Discussionmentioning

confidence: 99%

“…To solve this problem, we conducted experiments using novel cationic multilamellar vesicle liposomes composed of N-(␣-trimethylammonioacetyl)-didodecyl-D-glutamate chloride (TMAG), dilauroyl-phosphatidylcholine (DLPC), and dioleoyl phosphatidyl-ethanolamine (DOPE) (1:2:2, molar ratio) containing a strong expression promoter-enhancer system CAG and transcriptional activator high mobility group 1,2 (HMG-1,2) non-histone chromatin proteins. 7,20,21 We encapsulated endotoxin-free plasmid DNA, because endotoxins are known to hinder in vivo transfection, cause endotoxic shock syndrome and activate complement cas-cade. 22 We constructed the plasmids pcagluc and pcagTNF-␣ incorporating beetle luciferase and the human tumor necrosis factor-␣ (TNF-␣) gene, respectively, with a modified chicken ␤-actin promoter, and the immediate-early enhancer of cytomegalovirus.…”

Section: Introductionmentioning

confidence: 99%

Gene transduction for disseminated intraperitoneal tumor using cationic liposomes containing non-histone chromatin proteins: cationic liposomal gene therapy of carcinomatosa

1998

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“…In most eukaryotic cells, HMGB1 is located in the nucleus, where it functions as a nucleosome stabilizer and a regulator of transcription (2,3). HMGB1 recently has been shown to play a role as a cytokine-like molecule when it is released into extracellular space.…”

mentioning

confidence: 99%

Chaperone-like Activity of High-Mobility Group Box 1 Protein and Its Role in Reducing the Formation of Polyglutamine Aggregates

Min

et al. 2013

The Journal of Immunology

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High-mobility group box 1 protein (HMGB1), which mainly exists in the nucleus, has recently been shown to function as a sentinel molecule for viral nucleic acid sensing and an autophagy regulator in the cytoplasm. In this study, we studied the chaperone-like activity of HMGB1 and found that HMGB1 inhibited the chemically induced aggregation of insulin and lysozyme, as well as the heat-induced aggregation of citrate synthase. HMGB1 also restored the heat-induced suppression of cytoplasmic luciferase activity as a reporter protein in hamster lung fibroblast O23 cells with expression of HMGB1. Next, we demonstrated that HMGB1 inhibited the formation of aggregates and toxicity caused by expanded polyglutamine (polyQ), one of the main causes of Huntington disease. HMGB1 directly interacted with polyQ on immunofluorescence and coimmunoprecipitation assay, whereas the overexpression of HMGB1 or exogenous administration of recombinant HMGB1 protein remarkably reduced polyQ aggregates in SHSY5Y cells and hmgb1−/− mouse embryonic fibroblasts upon filter trap and immunofluorescence assay. Finally, overexpressed HMGB1 proteins in mouse embryonic primary striatal neurons also bound to polyQ and decreased the formation of polyQ aggregates. To this end, we have demonstrated that HMGB1 exhibits chaperone-like activity and a possible therapeutic candidate in polyQ disease.

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The intracellular distribution and function of the high mobility group chromosomal proteins

Cited by 240 publications

References 116 publications

Novel autoantigens of perinuclear anti-neutrophil cytoplasmic antibodies (P-ANCA) in ulcerative colitis: non-histone chromosomal proteins, HMG1 and HMG2

Novel autoantigens of perinuclear anti-neutrophil cytoplasmic antibodies (P-ANCA) in ulcerative colitis: non-histone chromosomal proteins, HMG1 and HMG2

Gene transduction for disseminated intraperitoneal tumor using cationic liposomes containing non-histone chromatin proteins: cationic liposomal gene therapy of carcinomatosa

Chaperone-like Activity of High-Mobility Group Box 1 Protein and Its Role in Reducing the Formation of Polyglutamine Aggregates

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