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Gene Review

Hmgb1  -  high mobility group box 1

Rattus norvegicus

Synonyms: Ac2-008, Amphoterin, HMG-1, Heparin-binding protein p30, High mobility group protein 1, ...
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Disease relevance of Hmgb1


High impact information on Hmgb1

  • The presence of HMG-1 protein in the cytoplasm of rat liver cells was verified by direct examination of the protein content of selected cytoplasmic fractions [4].
  • A protein with electrophoretic mobility identical to HMG-1 was detected by electrophoresis on polyacrylamide gels containing either sodium dodecylsulfate or urea [4].
  • Immunofluorescence studies with these antibodies reveal that HMG-1 or components which immunologically cross-react with HMG-1 are present in the cytoplasm of Chinese hamster V-79, rat liver TR-12 and bovine trachea EBTr-NBL-4 cells [4].
  • Indeed, the co-localization of RAGE and amphoterin at the leading edge of advancing neurites indicated their potential contribution to cellular migration, and in pathologies such as tumour invasion [5].
  • Specific binding of chromosomal protein HMG1 to DNA damaged by the anticancer drug cisplatin [6].

Chemical compound and disease context of Hmgb1


Biological context of Hmgb1


Anatomical context of Hmgb1

  • The distinct localization to the filopodia of the advancing plasma membrane suggests that endogenous amphoterin has a role in the extension of neurite-type cytoplasmic processes in developing cells [12].
  • In cells that are at an active stage of spreading and extending their cytoplasmic processes amphoterin was especially associated with plasma membrane filopodia [12].
  • Anti-synthetic peptide antibodies raised according to the sequence of amphoterin were shown to bind specifically to the protein isolated from brain, and were used to detect amphoterin in subcellular fractions and in immunostaining of cells [12].
  • We reported recently that HMGB1 was associated with senile plaques and the total protein level significantly increased in AD brain [16].
  • Testis levels of HMG proteins, relative to DNA content, were equivalent to other tissues for HMG1 (13 micrograms/mg of DNA), HMG14 (3 micrograms/mg of DNA), and HMG17 (5 micrograms/mg of DNA) [17].

Associations of Hmgb1 with chemical compounds

  • In this study, diffuse HMGB1 immunoreactivity was observed around dying neurons in the kainic acid- and Abeta1-42 (Abeta42)-injected rat hippocampi [16].
  • Significant losses of DNA ring closure activity were seen upon limited 2-5-h exposures of nonacid-purified HMG-1/2 to perchloric acid and/or trichloroacetic acid [18].
  • HMG 1 was ADP-ribosylated to a greater extent in young but to a lower level in the old by different effectors except spermine which showed no influence in old age [19].
  • Butyrate had no effect on HMG 1, but hydrocortisone decreased it [20].
  • A sharp rise in the phosphorylation of histones H1, H2A, and ubiquitinated H2A is seen on transformation, together with the appearance of three phosphorylated proteins that are extractable by perchloric acid and appear related to high mobility group Protein 14, a constituent of active chromatin [21].

Physical interactions of Hmgb1


Regulatory relationships of Hmgb1


Other interactions of Hmgb1

  • The results presented in this report offered further evidence for the existence of structural and functional similarities between these two proteins implicating an involvement of HMG-1 in the regulation of the rat Hp gene transcription [15].
  • Averaged over the four tissues investigated, there were 0.28 molecule of HMG1, 0.18 molecule of HMG2, and 0.46 molecule of HMG17 per nucleosome [26].
  • Identification of a single-stranded DNA binding protein from rat liver with high mobility group protein 1 [27].
  • This DNA-bending activity appears to be central to at least some of the recently elucidated functions of HMG-1/2, such as the enhancement of progesterone receptor DNA binding [18].
  • HMG1, -2, -14, and -17 were isolated from rat testes by Bio-Rex 70 chromatography combined with preparative gel electrophoresis [17].

Analytical, diagnostic and therapeutic context of Hmgb1

  • The number of PMA-U937 cells was markedly decreased by co-culture with WiDr cells exposed to HMGB1/amphoterin sense S-oligodeoxynucleotide (ODN) in spheroids or monolayers [2].
  • Characterization by high performance liquid chromatography--mass spectrometry (HPLC-MS), partial peptide sequencing and western blot analysis showed the isolated HMG proteins to be HMG-1 and HMG-2 [28].
  • Isoelectric focusing, HPLC-MS and peptide sequencing data also suggested that HMG-1 and SBP-1 were identical [28].
  • The rat liver single-stranded DNA binding protein, S25 and HD25, isolated by differential DNA cellulose affinity chromatography was compared to the high mobility group proteins, HMG1 and HMG2, isolated from rat liver chromatin by the technique of Goodwin et al [27].
  • Incorporation of [3H]lysine into the non-histone chromosomal proteins HMG1, HMG2, and HMG17 and into each of the five major classes of histones was measured in rat liver at various times after partial hepatectomy [29].


  1. Structure of the HMG box motif in the B-domain of HMG1. Weir, H.M., Kraulis, P.J., Hill, C.S., Raine, A.R., Laue, E.D., Thomas, J.O. EMBO J. (1993) [Pubmed]
  2. Colon cancer cell-derived high mobility group 1/amphoterin induces growth inhibition and apoptosis in macrophages. Kuniyasu, H., Yano, S., Sasaki, T., Sasahira, T., Sone, S., Ohmori, H. Am. J. Pathol. (2005) [Pubmed]
  3. Influence of nonhistone chromatin protein HMG-1 on the enzymatic digestion of purified DNA. Shastri, K., Isackson, P.J., Fishback, J.L., Land, M.D., Reeck, G.R. Nucleic Acids Res. (1982) [Pubmed]
  4. Antibodies against chromosomal HMG proteins stain the cytoplasm of mammalian cells. Bustin, M., Neihart, N.K. Cell (1979) [Pubmed]
  5. Blockade of RAGE-amphoterin signalling suppresses tumour growth and metastases. Taguchi, A., Blood, D.C., del Toro, G., Canet, A., Lee, D.C., Qu, W., Tanji, N., Lu, Y., Lalla, E., Fu, C., Hofmann, M.A., Kislinger, T., Ingram, M., Lu, A., Tanaka, H., Hori, O., Ogawa, S., Stern, D.M., Schmidt, A.M. Nature (2000) [Pubmed]
  6. Specific binding of chromosomal protein HMG1 to DNA damaged by the anticancer drug cisplatin. Pil, P.M., Lippard, S.J. Science (1992) [Pubmed]
  7. Adrenomedullin and its binding protein attenuate the proinflammatory response after hemorrhage. Cui, X., Wu, R., Zhou, M., Dong, W., Ulloa, L., Yang, H., Wang, H., Tracey, K.J., Simms, H.H., Wang, P. Crit. Care Med. (2005) [Pubmed]
  8. High-mobility group box 1 protein is an inflammatory mediator in necrotizing enterocolitis: protective effect of the macrophage deactivator semapimod. Zamora, R., Grishin, A., Wong, C., Boyle, P., Wang, J., Hackam, D., Upperman, J.S., Tracey, K.J., Ford, H.R. Am. J. Physiol. Gastrointest. Liver Physiol. (2005) [Pubmed]
  9. Stimulated astrocytes release high-mobility group 1 protein, an inducer of LAN-5 neuroblastoma cell differentiation. Passalacqua, M., Patrone, M., Picotti, G.B., Del Rio, M., Sparatore, B., Melloni, E., Pontremoli, S. Neuroscience (1998) [Pubmed]
  10. Identity in molecular structure between "differentiation enhancing factor" of murine erythroleukemia cells and the 30 kD heparin-binding protein of developing rat brain. Melloni, E., Sparatore, B., Patrone, M., Pessino, A., Passalacqua, M., Pontremoli, S. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  11. HMGB1, a novel cytokine-like mediator linking acute neuronal death and delayed neuroinflammation in the postischemic brain. Kim, J.B., Sig Choi, J., Yu, Y.M., Nam, K., Piao, C.S., Kim, S.W., Lee, M.H., Han, P.L., Park, J.S., Lee, J.K. J. Neurosci. (2006) [Pubmed]
  12. 30-kDa heparin-binding protein of brain (amphoterin) involved in neurite outgrowth. Amino acid sequence and localization in the filopodia of the advancing plasma membrane. Merenmies, J., Pihlaskari, R., Laitinen, J., Wartiovaara, J., Rauvala, H. J. Biol. Chem. (1991) [Pubmed]
  13. Nucleotide sequence of rat liver HMG1 cDNA. Paonessa, G., Frank, R., Cortese, R. Nucleic Acids Res. (1987) [Pubmed]
  14. The significance of changes in high mobility group-1 protein mRNA expression in rats after thermal injury. Fang, W.H., Yao, Y.M., Shi, Z.G., Yu, Y., Wu, Y., Lu, L.R., Sheng, Z.Y. Shock (2002) [Pubmed]
  15. HMG-1 as regulatory trans-acting protein in the acute phase-induced expression of the rat liver haptoglobin gene. Grigorov, I., Milosavljević, T., Cvetković, I., Petrović, M. Gen. Physiol. Biophys. (2001) [Pubmed]
  16. High mobility group box protein-1 inhibits microglial Abeta clearance and enhances Abeta neurotoxicity. Takata, K., Kitamura, Y., Tsuchiya, D., Kawasaki, T., Taniguchi, T., Shimohama, S. J. Neurosci. Res. (2004) [Pubmed]
  17. Characterization of high mobility group protein levels during spermatogenesis in the rat. Bucci, L.R., Brock, W.A., Goldknopf, I.L., Meistrich, M.L. J. Biol. Chem. (1984) [Pubmed]
  18. Increased DNA-bending activity and higher affinity DNA binding of high mobility group protein HMG-1 prepared without acids. Wagner, J.P., Quill, D.M., Pettijohn, D.E. J. Biol. Chem. (1995) [Pubmed]
  19. ADP-ribosylation of HMG proteins and its modulation by different effectors in the liver of aging rats. Thakur, M.K., Prasad, S. Mech. Ageing Dev. (1990) [Pubmed]
  20. Age-dependent effects of sodium butyrate and hydrocortisone on acetylation of high mobility group proteins of rat liver. Prasad, S., Thakur, M.K. Biochem. Int. (1988) [Pubmed]
  21. Changes in nuclear proteins on transformation of rat epithelial thyroid cells by a murine sarcoma retrovirus. Giancotti, V., Berlingieri, M.T., DiFiore, P.P., Fusco, A., Vecchio, G., Crane-Robinson, C. Cancer Res. (1985) [Pubmed]
  22. Receptor for advanced glycation end products (RAGE) signaling induces CREB-dependent chromogranin expression during neuronal differentiation. Huttunen, H.J., Kuja-Panula, J., Rauvala, H. J. Biol. Chem. (2002) [Pubmed]
  23. Sp1-binding elements in the promoter of RAGE are essential for amphoterin-mediated gene expression in cultured neuroblastoma cells. Li, J., Qu, X., Schmidt, A.M. J. Biol. Chem. (1998) [Pubmed]
  24. Comparative analysis of the influence of the high-mobility group box 1 protein on DNA binding and transcriptional activation by the androgen, glucocorticoid, progesterone and mineralocorticoid receptors. Verrijdt, G., Haelens, A., Schoenmakers, E., Rombauts, W., Claessens, F. Biochem. J. (2002) [Pubmed]
  25. Amphoterin stimulates myogenesis and counteracts the antimyogenic factors basic fibroblast growth factor and S100B via RAGE binding. Sorci, G., Riuzzi, F., Arcuri, C., Giambanco, I., Donato, R. Mol. Cell. Biol. (2004) [Pubmed]
  26. Concentrations of high-mobility-group proteins in the nucleus and cytoplasm of several rat tissues. Kuehl, L., Salmond, B., Tran, L. J. Cell Biol. (1984) [Pubmed]
  27. Identification of a single-stranded DNA binding protein from rat liver with high mobility group protein 1. Bonne, C., Sautiere, P., Duguet, M., de Recondo, A.M. J. Biol. Chem. (1982) [Pubmed]
  28. Identity of nuclear high-mobility-group protein, HMG-1, and sulfoglucuronyl carbohydrate-binding protein, SBP-1, in brain. Chou, D.K., Evans, J.E., Jungalwala, F.B. J. Neurochem. (2001) [Pubmed]
  29. Synthesis of high mobility group proteins in regenerating rat liver. Kuehl, L. J. Biol. Chem. (1979) [Pubmed]
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