Differential expression of the histone H1° gene in U937 and HL‐60 leukemia cell lines

Hochhuth, C.; Doenecke, Detlef

doi:10.1002/jcb.240500312

Cited by 9 publications

(3 citation statements)

References 47 publications

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“…Therefore, investigation of the factors that modulate histone H1f 0 transcription may provide insight into the molecular mechanisms of MAA toxicity. The mRNA of H1f 0 is frequently measured as an indicator of cell response to But [51,52,54] and TSA [53,55] and is strongly correlated with increased acetylation of core histones [55], possibly as a compensatory response of the cell to reduce histone hyperacetylation [57]. Analysis of the temporal and cell/stage-specific pattern of histone H3/H4 hyperacetylation in response to MAA demonstrates that the increased acetylation of the core histones of the cell types vulnerable to MAA toxicity either precedes or occurs concurrently with the onset of cell death, providing support to the hypothesis that hyperacetylation leads to spermatocyte death.…”

Section: Discussionmentioning

confidence: 99%

“…As elevated transcript levels of histone H1f 0 have been reported from cells or tissues in which the enzyme HDAC has been inhibited or in which core histones have been found to be highly acetylated [51][52][53][54][55], we examined the effects of MAA on HDAC activity in vitro and the degree of histone acetylation in the testes of MAA-treated animals. To determine if MAA inhibits HDAC activity in the testis, juvenile rat testes (27 days old) were used as a source of enzyme activity because these contain a much higher proportion of meiotic germ cells relative to testes from sexually mature rats due to the reduced proportion of spermatids at this age.…”

Section: Effect Of Maa On Hdac/hat Activities and Acetylated Histonesmentioning

confidence: 99%

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Methoxyacetic Acid-Induced Spermatocyte Death Is Associated with Histone Hyperacetylation in Rats1

Wade

Kawata

Williams

et al. 2008

Biology of Reproduction

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We used high-density microarrays to evaluate the possible mechanisms by which 2-methoxyacetic acid (MAA) disrupts spermatogenesis. Levels of mRNA transcripts were determined in total RNA isolated from testes of MAA-treated (650 mg/kg i.p.) or concurrent control rats killed 4, 8, 12, or 24 h postexposure (PE). Germ cell death was examined in testis sections using in situ staining for DNA fragmentation. MAA treatment caused increased death of pachytene spermatocytes starting 8 h PE and increasing dramatically at 12 and 24 h PE. Microarray results indicated that at 4 h PE the transcript levels of seven different genes were significantly overrepresented in the testes of MAA-exposed animals. One gene (histone H1 zero [H1f0]) was significantly overrepresented in MAA-treated samples at 4, 8, and 12 h PE. Because expression of this gene has been associated with increased acetylation of core histones, we examined MAA-induced changes in the acetylation of histones H4 (HISTH4) and H3 (HISTH3) in testis nuclear protein. Western blots of acid-extracted testis nuclei indicated that the levels of tetraacetyl histone H4 (4acHIST1H4) and of diacetyl histone H3 (2acHIST1H3) were elevated by MAA treatment at 4, 8, and 12 h PE. Using the same antibodies, 4acHIST1H4 and 2acHIST1H3 were localized primarily to elongating spermatids in testis sections from control animals. At 4 h PE, staining for either histone modification was dramatically increased in spermatogonia and all primary spermatocyte populations except for dividing spermatocytes. MAA treatment of testis nuclear protein extracts from unexposed animals caused both a significant increase in histone acetyltransferase activity and a significant inhibition of histone deacetylase activity, suggesting that increased core histone acetylation results from a combination of these complementary modes of action. Our results indicate that exposure to MAA causes increased acetylation of core histones in several testis germ cell populations, including those in prophase of meiosis, a large proportion of which die rapidly following this treatment.

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Section: Discussionmentioning

confidence: 99%

Section: Effect Of Maa On Hdac/hat Activities and Acetylated Histonesmentioning

confidence: 99%

Methoxyacetic Acid-Induced Spermatocyte Death Is Associated with Histone Hyperacetylation in Rats1

Wade

Kawata

Williams

et al. 2008

Biology of Reproduction

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“…Numerous studies have shown that the level of histone H1°mRNA generally increases after cell exposure to sodium butyrate (28,29,37), but two cell lines had been described to display other features. The human promyelocytic HL-60 cell line failed to induce any accumulation of histone H1°mRNA in presence of the inducer (38), whereas the human hepatoma cell line HepG2 expressed a high level of histone H1°mRNA, which could not be further increased by the inducer (39). Consequently, we studied histone H1°expression in HTC cell line prior to and after addition of sodium butyrate.…”

Section: Resultsmentioning

confidence: 99%

The Effects of Sodium Butyrate on Transcription Are Mediated through Activation of a Protein Phosphatase

Cuisset¹,

Tichonicky²,

Jaffray³

et al. 1997

Journal of Biological Chemistry

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In this study we have investigated the molecular mechanism by which sodium butyrate modulates gene expression when added to cultured cells. As a model system we used hepatoma tissue culture cells in which sodium butyrate treatment increases histone H1°mRNA level and decreases c-myc mRNA level. Because we observed that stimulation of histone H1°gene expression could take place in the absence of protein neosynthesis, we hypothesized that sodium butyrate induced a posttranslational modification of a factor involved in the transcription process. Using different types of well known kinase and phosphatase inhibitors, we studied the implication of kinase or phosphatase activity in this pathway. Interestingly, cell treatment with potent serine-threonine-phosphatase inhibitors, calyculin A or okadaic acid, prevented the regulation of both histone H1°and c-myc gene expressions by sodium butyrate. On the other hand, the tyrosine phosphatase inhibitor, vanadate, or the protein kinase C inhibitor, staurosporine, did not significantly modify sodium butyrate effects. Using protein phosphatase 1 and 2A for in vitro assays, we found a 45% increase of phosphatase activity after cell treatment by sodium butyrate, possibly due to a protein phosphatase 1-type protein phosphatase. These data strongly suggest that signaling pathway(s) triggered by sodium butyrate to modulate gene expression involve(s) a serine-threonine-phosphatase activity.

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Differential expression of nuclear HMG1, HMG2 proteins and H1⁰ histone in various blood cells

Čabart

Kalousek

Jandová

et al. 1995

Cell Biochemistry & Function

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Changes in the levels of chromosomal high-mobility group proteins HMG1, HMG2 and histone H1 zero were investigated in blood cells of various types, proliferation activity and stage of differentiation. The relative amounts of proteins HMG1, HMG2 and histone H1 zero were evaluated densitometrically by SDS-PAGE of 5 per cent w/v perchloric acid extracts of blood cells. Concerning the HMG1 and HMG2, the main conclusions were: the expression of these HMG proteins was higher in malignant cells, namely leukemia cell lines, then in lymphocytes or granulocytes and the distribution of HMG1 and HMG2 was highly cell-specific. In comparison with lymphoid cells, the levels of HMG1/2 were higher in myeloid cells. The results revealed that in myeloid cells HMG2 prevails over HMG1. There was no direct correlation between HMG1/2 expression and proliferation activity. The levels of HMG1/2 did not depend on the transcription of chromatin either. However, there was some connection between irreversibly differentiated nonproliferating cells and a loss of HMG1/2 proteins. Reversibly differentiated leukemic cells retain their HMG1/2 levels. Similarly to HMG1/2,H1 zero showed a strong cell specificity. The level of H1 zero was different in the various blood cell types. As compared with lymphoid cells, the level of H1 zero was several-fold higher in myeloid cells, regardless of whether they were normal or malignant. Moreover, there was an accumulation of H1 zero in differentiating HL-60 cells accompanied by only a slight decline in cell proliferation; this agrees with the idea that H1 zero expression is not directly associated with the inhibition of cell growth. Rather higher expression of H1 zero is related to changes during cell differentiation.

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Differential expression of the histone H1° gene in U937 and HL‐60 leukemia cell lines

Cited by 9 publications

References 47 publications

Methoxyacetic Acid-Induced Spermatocyte Death Is Associated with Histone Hyperacetylation in Rats1

Methoxyacetic Acid-Induced Spermatocyte Death Is Associated with Histone Hyperacetylation in Rats1

The Effects of Sodium Butyrate on Transcription Are Mediated through Activation of a Protein Phosphatase

Differential expression of nuclear HMG1, HMG2 proteins and H1⁰ histone in various blood cells

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Differential expression of the histone H1° gene in U937 and HL‐60 leukemia cell lines

Cited by 9 publications

References 47 publications

Methoxyacetic Acid-Induced Spermatocyte Death Is Associated with Histone Hyperacetylation in Rats1

Methoxyacetic Acid-Induced Spermatocyte Death Is Associated with Histone Hyperacetylation in Rats1

The Effects of Sodium Butyrate on Transcription Are Mediated through Activation of a Protein Phosphatase

Differential expression of nuclear HMG1, HMG2 proteins and H10 histone in various blood cells

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Differential expression of nuclear HMG1, HMG2 proteins and H1⁰ histone in various blood cells