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Hmgb2  -  high mobility group box 2

Rattus norvegicus

Synonyms: HMG-2, High mobility group protein 2, High mobility group protein B2, Hmg2
 
 
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Disease relevance of Hmgb2

  • We also present a semi-quantitative estimate that HMG-1 and HMG-2 occur in chromatin from rapidly dividing, cultured rat hepatoma cells at about 8 times the level that they occur in adult rat liver chromatin [1].
 

High impact information on Hmgb2

  • 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 [2].
  • These results show that the very high level of HMG2 in testis is not associated with proliferative activity as previously hypothesized [3].
  • High levels of HMG2 in the testis were due to pachytene spermatocytes and early spermatids (56 +/- 4 and 47 +/- 6 micrograms/mg of DNA, respectively) [3].
  • The somatic cells of the testis, including isolated populations of Sertoli and Leydig cells, showed very low levels of HMG2 (2 micrograms/mg of DNA), similar to those in nonproliferating somatic tissues [3].
  • Mixtures of spermatogonia and early primary spermatocytes showed lower levels of HMG2 (12 +/- 3 micrograms/mg of DNA) similar to proliferating somatic tissues, whereas late spermatids had no detectable HMG proteins [3].
 

Biological context of Hmgb2

  • In young rats, sodium butyrate and hydrocortisone stimulated acetylation of HMG 14 and 17, and decreased that of HMG 2 [4].
  • Repression of cell cycle progression by antisense HMG2 RNA [5].
  • These results suggest that the fluctuation of the HMG2 message during the cell cycle is not a consequence of but a prerequisite for cell proliferation [5].
  • Progression of the cell cycle of COS-1 cells was repressed during G1 to S phase by expression of the antisense RNA for HMG2, resulting in a decrease of cell growth [5].
  • Northern analysis demonstrated that the level of HMG2 mRNA was markedly enhanced in the post-S phase and reached a maximum at G2 phase, suggesting that expression of the HMG2 gene is not coupled with DNA synthesis [5].
 

Anatomical context of Hmgb2

 

Associations of Hmgb2 with chemical compounds

 

Other interactions of Hmgb2

  • The "fast" form of HMG2 accounted for the large increase of HMG2 levels in rat testes [3].
 

Analytical, diagnostic and therapeutic context of Hmgb2

  • 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 [8].
  • 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 [9].

References

  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. Repression of cell cycle progression by antisense HMG2 RNA. Yamazaki, F., Nagatsuka, Y., Shirakawa, H., Yoshida, M. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  6. 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]
  7. Differential methylation of HMG proteins by dexamethasone in the liver of aging rats. Prasad, S., Thakur, M.K. Aging (Milan, Italy) (1991) [Pubmed]
  8. 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]
  9. Synthesis of high mobility group proteins in regenerating rat liver. Kuehl, L. J. Biol. Chem. (1979) [Pubmed]
 
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