Specificity of antibodies raised against triacetylated histone H4

Muller, Sylviane; Isabey, Agnès; Couppez, Maurice; Plaué, S.; Sommermeyer, G.; Regenmortel, M.H.V. Van

doi:10.1016/0161-5890(87)90062-9

Cited by 52 publications

(34 citation statements)

References 42 publications

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“…Their identity was checked by matrix-assisted laser desorption and ionization time-of-flight mass spectrometry using a protein time-of-flight apparatus (Brucker Spectrospin, Bremen, Germany). Individual histones were prepared from calf thymus and purified, as described previously (32).…”

Section: Peptides Histones and Nucleosomesmentioning

confidence: 99%

CD4+ T Cells from (New Zealand Black × New Zealand White)F1 Lupus Mice and Normal Mice Immunized Against Apoptotic Nucleosomes Recognize Similar Th Cell Epitopes in the C Terminus of Histone H3

Fournel

Neichel

Dali

et al. 2003

The Journal of Immunology

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We have previously reported that peptide 88-99 of histone H4 represents a minimal T cell epitope recognized by Th cells from nonautoimmune BALB/c (H-2d/d) mice immunized with nucleosomes. In this study, we tested a panel of overlapping peptides spanning the whole sequences of H4 and H3 for recognition by CD4+ T cells from unprimed (New Zealand Black (NZB) × New Zealand White (NZW))F1 lupus mice (H-2d/z). None of the 11 H4 peptides was recognized by CD4+ T cells from (NZB × NZW)F1 mice. In contrast, these cells proliferated and secreted IL-2, IL-10, and IFN-γ upon ex vivo stimulation with H3 peptides representing sequences 53-70, 64-78, and 68-85. Peptides 56-73 and 61-78 induced the production of IFN-γ and IL-10, respectively, without detectable proliferation, suggesting that they may act as partial agonist of the TCR. Th cells from unprimed BALB/c mice and other lupus-prone mice such as SNF1 (H-2d/q) and MRL/lpr (H-2k/k) mice did not recognize any peptides present within the H3 region 53-85. We further demonstrated that immunization of normal BALB/c mice with syngeneic liver nucleosomes and spleen apoptotic cells, but not with nonapoptotic syngeneic cells, induced Th cell responses against several peptides of the H3 region 53-85. Moreover, we found that this conserved region of H3, which is accessible at the surface of nucleosomes, is targeted by Abs from (NZB × NZW)F1 mice and lupus patients, and contains motifs recognized by several distinct HLA-DR molecules. It might thus be important in the self-tolerance breakdown in lupus.

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Section: Peptides Histones and Nucleosomesmentioning

confidence: 99%

CD4+ T Cells from (New Zealand Black × New Zealand White)F1 Lupus Mice and Normal Mice Immunized Against Apoptotic Nucleosomes Recognize Similar Th Cell Epitopes in the C Terminus of Histone H3

Fournel

Neichel

Dali

et al. 2003

The Journal of Immunology

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“…Rabbit specific anti-histone sera had been previously tested : H2B (Muller et al, 1985), H3 (Muller et al, 1982), and H4 (Muller et al, 1987 (Courtens et al, 1983(Courtens et al, , 1988 antisera.…”

Section: Reagentsmentioning

confidence: 99%

Immunocytochemical localization of histones H2B, H3 and H4 in pronuclei and four-cell stages of porcine embryos. Preliminary results

Rozinek¹,

Muller²,

Courtens³

1989

Reprod. Nutr. Dévelop.

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Summary ― In this preliminary work, using pig embryos ultrastructural immunocytochemistry with polyclonal antibodies against purified histones was used to demonstrate both their localization and the time of their appearance in pronuclei, from 15 h after ovulation (pronuclear stage) to 48 h postinsemination (4-cell stage).In pronuclei, the histones H2B, H3, and H4 were located in the heterochromatin as soon as it appeared. Usually, one of the pronuclei seemed to be more heavily labelled. The chromatin facing the zone of pronuclear contact formed a bowl-shaped region in each pronucleus heavily labelled for these histones. The so-called pseudo-nucleoli were present in both pronuclei and contained H2B.In 4-cell stages, the labelling intensities of heterochromatin for H2B, H3 and H4 were equal in all the nuclei. H2B was still evident in the pseudo-nucleoli, but in a lower quantity than before. The condensed chromatin located either under the nuclear envelope or surrounding the pseudo-nucleoli was heavily labelled for H2B, H3 and H4.

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“…[30][31][32][33][34] This method is very sensitive but relies on the specificity and availability of antibodies, which have come under scrutiny. 35,36 Peptide mapping by mass spectrometry has also been extensively used as a powerful approach for the identification of proteins and investigation of post-translational modifications. [37][38][39] For example, Person et al used peptide mass mapping to determine H4 acetylation from different H4 isoforms separated by acetic acid-urea polyacrylamide gel electrophoresis (AU-PAGE) and in-gel-digested with chymotrypsin.…”

Section: Introductionmentioning

confidence: 99%

Histone H4 N-Terminal Acetylation in Kasumi-1 Cells Treated with Depsipeptide Determined by Acetic Acid−Urea Polyacrylamide Gel Electrophoresis, Amino Acid Coded Mass Tagging, and Mass Spectrometry

Zhang

Liu

et al. 2006

J. Proteome Res.

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Disrupted patterns of acetylation and deacetylation of core histones play an important role in silencing transcription of hematopoietic important genes in acute myeloid leukemia (AML). A thorough investigation of these mechanisms and the response to pharmacologic modifiers will provide a better understanding of the role of histone acetylation in leukemogenesis. We describe here an analytical approach that combines acid urea polyacrylamide gel electrophoresis (AU-PAGE), amino acid coded mass tagging (AACM), and mass spectrometry (MS) for the investigation of histone acetylation patterns. The combined approach was used to follow the dynamics of H4 acetylation in Kasumi-1 cells harboring the fusion gene AML1/ETO shown to aberrantly recruit histone deacetylases (HDACs). The histones in Kasumi-1 cells were labeled by growing the cells in media in which lysine was replaced with stable isotope-labeled lysine (Lys-D 4 ). Labeled and unlabeled cells were treated with depsipeptide and analyzed at different time points (0,4,8,12,24, and 48 h). The cells were mixed, the histone was extracted, and acetylated H4 isoforms were separated using AU-PAGE before in-gel trypsin digestion. The digests were analyzed by MALDI-TOF MS. Peptides were identified by mass and isotope pattern. LC-MS/MS of Arg-C digests were also performed to verify the acetylation pattern for H4. The major pattern of acetylation was determined as follows: initial acetylation at K16, followed by acetylation at K12, and finally acetylation of either K8 and/or K5.

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Specificity of antibodies raised against triacetylated histone H4

Cited by 52 publications

References 42 publications

CD4+ T Cells from (New Zealand Black × New Zealand White)F1 Lupus Mice and Normal Mice Immunized Against Apoptotic Nucleosomes Recognize Similar Th Cell Epitopes in the C Terminus of Histone H3

CD4+ T Cells from (New Zealand Black × New Zealand White)F1 Lupus Mice and Normal Mice Immunized Against Apoptotic Nucleosomes Recognize Similar Th Cell Epitopes in the C Terminus of Histone H3

Immunocytochemical localization of histones H2B, H3 and H4 in pronuclei and four-cell stages of porcine embryos. Preliminary results

Histone H4 N-Terminal Acetylation in Kasumi-1 Cells Treated with Depsipeptide Determined by Acetic Acid−Urea Polyacrylamide Gel Electrophoresis, Amino Acid Coded Mass Tagging, and Mass Spectrometry

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