Literature DB >> 2808481

Histone acetyltransferase activity in rat hepatomas.

H H Grunicke1, Y Yamada, Y Natsumeda, W Helliger, B Puschendorf, G Weber.   

Abstract

In view of various reports describing differences in histone acetylation between normal rat liver and hepatomas, the behaviour of histone acetyltransferase (EC 2.3.1.48) activity was elucidated in normal rat liver and in a spectrum of well-characterized rat hepatomas of slow, intermediate and rapid growth rates. In all tumours the acetyltransferase specific activity, expressed as nmol h-1 mg total protein-1, was higher than in the corresponding normal livers and the rise correlated positively with the proliferation rates of the tumors. No difference is observed if acetyltransferase activity is expressed per milligram of histone. This is explained by elevated ratios of histones and of DNA to total protein in the hepatomas compared to the ratios in normal liver. Electrophoretic analysis of [3H]acetate-labeled histones revealed similar patterns in hepatoma and normal liver. The extent of histone H4 acetylation, as indicated by the frequency distribution of non-, mono-, di-, tri-, and tetraacetylated H4-species, was found to be identical in hepatomas and normal liver. The histone protein and acetate labeling patterns were near normal in the slowly growing hepatomas.

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Year:  1989        PMID: 2808481     DOI: 10.1007/bf00393332

Source DB:  PubMed          Journal:  J Cancer Res Clin Oncol        ISSN: 0171-5216            Impact factor:   4.553


  23 in total

1.  Sensitivity of regions of chromatin containing hyperacetylated histones to DNAse I.

Authors:  D A Nelson; W M Perry; R Chalkley
Journal:  Biochem Biophys Res Commun       Date:  1978-05-15       Impact factor: 3.575

2.  Modification of histones immediately following synthesis.

Authors:  L Sealy; R Chalkley
Journal:  Arch Biochem Biophys       Date:  1979-10-01       Impact factor: 4.013

Review 3.  Transcriptionally active chromatin.

Authors:  R Reeves
Journal:  Biochim Biophys Acta       Date:  1984-09-10

Review 4.  Biochemical strategy of cancer cells and the design of chemotherapy: G. H. A. Clowes Memorial Lecture.

Authors:  G Weber
Journal:  Cancer Res       Date:  1983-08       Impact factor: 12.701

5.  Histone acetylation increases the solubility of chromatin and occurs sequentially over most of the chromatin. A novel model for the biological role of histone acetylation.

Authors:  M Perry; R Chalkley
Journal:  J Biol Chem       Date:  1982-07-10       Impact factor: 5.157

6.  Resolution of histones by polyacrylamide gel electrophoresis in presence of nonionic detergents.

Authors:  A Zweidler
Journal:  Methods Cell Biol       Date:  1978       Impact factor: 1.441

7.  Transcriptionally active mononucleosomes from trout testis are heterogeneous in composition.

Authors:  T Hutcheon; G H Dixon; B Levy-Wilson
Journal:  J Biol Chem       Date:  1980-01-25       Impact factor: 5.157

8.  Comparative studies of histone acetylation in nucleosomes, nuclei, and intact cells. Evidence for special factors which modify acetylase action.

Authors:  R L Garcea; B M Alberts
Journal:  J Biol Chem       Date:  1980-12-10       Impact factor: 5.157

9.  Butyrate suppression of histone deacetylation leads to accumulation of multiacetylated forms of histones H3 and H4 and increased DNase I sensitivity of the associated DNA sequences.

Authors:  G Vidali; L C Boffa; E M Bradbury; V G Allfrey
Journal:  Proc Natl Acad Sci U S A       Date:  1978-05       Impact factor: 11.205

10.  Levels of histone H4 diacetylation decrease dramatically during sea urchin embryonic development and correlate with cell doubling rate.

Authors:  S A Chambers; B R Shaw
Journal:  J Biol Chem       Date:  1984-11-10       Impact factor: 5.157

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  1 in total

Review 1.  Enzymatic and nonenzymatic protein acetylations control glycolysis process in liver diseases.

Authors:  Juan Li; Tongxin Wang; Jun Xia; Weilei Yao; Feiruo Huang
Journal:  FASEB J       Date:  2019-08-01       Impact factor: 5.191

  1 in total

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