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Differential patterns of histone acetylation in inflammatory bowel diseases.

Tsaprouni LG, Ito K, Powell JJ, Adcock IM, Punchard N - J Inflamm (Lond) (2011)

Bottom Line: Post-translational modifications of histones, particularly acetylation, are associated with the regulation of inflammatory gene expression.Acetylation of histone H4 was significantly elevated in the inflamed mucosa in the trinitrobenzene sulfonic acid model of colitis particularly on lysine residues (K) 8 and 12 in contrast to non-inflamed tissue.These results demonstrate that histone acetylation is associated with inflammation and may provide a novel therapeutic target for mucosal inflammation.

View Article: PubMed Central - HTML - PubMed

Affiliation: Airways Disease Section, National Heart & Lung Institute, Imperial College London, Dovehouse Street, London, SW3 6LY, UK. ian.adcock@imperial.ac.uk.

ABSTRACT
Post-translational modifications of histones, particularly acetylation, are associated with the regulation of inflammatory gene expression. We used two animal models of inflammation of the bowel and biopsy samples from patients with Crohn's disease (CD) to study the expression of acetylated histones (H) 3 and 4 in inflamed mucosa. Acetylation of histone H4 was significantly elevated in the inflamed mucosa in the trinitrobenzene sulfonic acid model of colitis particularly on lysine residues (K) 8 and 12 in contrast to non-inflamed tissue. In addition, acetylated H4 was localised to inflamed tissue and to Peyer's patches (PP) in dextran sulfate sodium (DSS)-treated rat models. Within the PP, H3 acetylation was detected in the mantle zone whereas H4 acetylation was seen in both the periphery and the germinal centre. Finally, acetylation of H4 was significantly upregulated in inflamed biopsies and PP from patients with CD. Enhanced acetylation of H4K5 and K16 was seen in the PP. These results demonstrate that histone acetylation is associated with inflammation and may provide a novel therapeutic target for mucosal inflammation.

No MeSH data available.


Related in: MedlinePlus

Acetylation on histone 4 (H4) specific lysine residues 5 (K5), 8 (K8), 12 (K12) and 16 (K16) in Lewis and Sprague-Dawley dextran sulfate sodium (5% DSS). A: Representative bands of H4K5, K8, K12 and K16 acetylation. Lanes for Lewis rats represent: non-DSS treated (control) and DSS-treated. Likewise representative bands are illustrated for the Sprague-Dawley rats. Graphical representation of Western blotting data. H4 acetylation of K5 (B), K8 (C), K12 (D) and K16 (E). Columns represent the mean ± SEM (bar) of three independent experiments.
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Figure 4: Acetylation on histone 4 (H4) specific lysine residues 5 (K5), 8 (K8), 12 (K12) and 16 (K16) in Lewis and Sprague-Dawley dextran sulfate sodium (5% DSS). A: Representative bands of H4K5, K8, K12 and K16 acetylation. Lanes for Lewis rats represent: non-DSS treated (control) and DSS-treated. Likewise representative bands are illustrated for the Sprague-Dawley rats. Graphical representation of Western blotting data. H4 acetylation of K5 (B), K8 (C), K12 (D) and K16 (E). Columns represent the mean ± SEM (bar) of three independent experiments.

Mentions: DSS induced acetylation of histone 4 lysines K5, K8, K12 and K16 in both rat strains (Figure 4). However, a greater induction was seen on K8 in both Lewis (414 ± 51 DSS treated vs 100 ± 23% non-DSS treated animals) and Sprague-Dawley rats (1275 ± 123 DSS treated vs 100 ± 18% non-DSS treated animals). Similar results were seen with K12 in both Lewis (703 ± 64 DSS treated vs 100 ± 14% non-DSS treated animals) and Sprague-Dawley rats (1117 ± 113 DSS treated vs 100 ± 27% non-DSS treated animals). K5 acetylation in Lewis rats (346 ± 17 DSS treated vs 100 ± 12% non-DSS treated animals) and Sprague-Dawley rats (263 ± 22 DSS treated vs 100 ± 16% non-DSS treated animals) was also induced albeit to a lesser extent. Our findings were similar for K16 acetylation in both Lewis (235 ± 43 DSS treated vs 100 ± 22% non-DSS treated animals) and Sprague-Dawley rats (321 ± 24 DSS treated vs 100 ± 26% non-DSS treated animals).


Differential patterns of histone acetylation in inflammatory bowel diseases.

Tsaprouni LG, Ito K, Powell JJ, Adcock IM, Punchard N - J Inflamm (Lond) (2011)

Acetylation on histone 4 (H4) specific lysine residues 5 (K5), 8 (K8), 12 (K12) and 16 (K16) in Lewis and Sprague-Dawley dextran sulfate sodium (5% DSS). A: Representative bands of H4K5, K8, K12 and K16 acetylation. Lanes for Lewis rats represent: non-DSS treated (control) and DSS-treated. Likewise representative bands are illustrated for the Sprague-Dawley rats. Graphical representation of Western blotting data. H4 acetylation of K5 (B), K8 (C), K12 (D) and K16 (E). Columns represent the mean ± SEM (bar) of three independent experiments.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3040698&req=5

Figure 4: Acetylation on histone 4 (H4) specific lysine residues 5 (K5), 8 (K8), 12 (K12) and 16 (K16) in Lewis and Sprague-Dawley dextran sulfate sodium (5% DSS). A: Representative bands of H4K5, K8, K12 and K16 acetylation. Lanes for Lewis rats represent: non-DSS treated (control) and DSS-treated. Likewise representative bands are illustrated for the Sprague-Dawley rats. Graphical representation of Western blotting data. H4 acetylation of K5 (B), K8 (C), K12 (D) and K16 (E). Columns represent the mean ± SEM (bar) of three independent experiments.
Mentions: DSS induced acetylation of histone 4 lysines K5, K8, K12 and K16 in both rat strains (Figure 4). However, a greater induction was seen on K8 in both Lewis (414 ± 51 DSS treated vs 100 ± 23% non-DSS treated animals) and Sprague-Dawley rats (1275 ± 123 DSS treated vs 100 ± 18% non-DSS treated animals). Similar results were seen with K12 in both Lewis (703 ± 64 DSS treated vs 100 ± 14% non-DSS treated animals) and Sprague-Dawley rats (1117 ± 113 DSS treated vs 100 ± 27% non-DSS treated animals). K5 acetylation in Lewis rats (346 ± 17 DSS treated vs 100 ± 12% non-DSS treated animals) and Sprague-Dawley rats (263 ± 22 DSS treated vs 100 ± 16% non-DSS treated animals) was also induced albeit to a lesser extent. Our findings were similar for K16 acetylation in both Lewis (235 ± 43 DSS treated vs 100 ± 22% non-DSS treated animals) and Sprague-Dawley rats (321 ± 24 DSS treated vs 100 ± 26% non-DSS treated animals).

Bottom Line: Post-translational modifications of histones, particularly acetylation, are associated with the regulation of inflammatory gene expression.Acetylation of histone H4 was significantly elevated in the inflamed mucosa in the trinitrobenzene sulfonic acid model of colitis particularly on lysine residues (K) 8 and 12 in contrast to non-inflamed tissue.These results demonstrate that histone acetylation is associated with inflammation and may provide a novel therapeutic target for mucosal inflammation.

View Article: PubMed Central - HTML - PubMed

Affiliation: Airways Disease Section, National Heart & Lung Institute, Imperial College London, Dovehouse Street, London, SW3 6LY, UK. ian.adcock@imperial.ac.uk.

ABSTRACT
Post-translational modifications of histones, particularly acetylation, are associated with the regulation of inflammatory gene expression. We used two animal models of inflammation of the bowel and biopsy samples from patients with Crohn's disease (CD) to study the expression of acetylated histones (H) 3 and 4 in inflamed mucosa. Acetylation of histone H4 was significantly elevated in the inflamed mucosa in the trinitrobenzene sulfonic acid model of colitis particularly on lysine residues (K) 8 and 12 in contrast to non-inflamed tissue. In addition, acetylated H4 was localised to inflamed tissue and to Peyer's patches (PP) in dextran sulfate sodium (DSS)-treated rat models. Within the PP, H3 acetylation was detected in the mantle zone whereas H4 acetylation was seen in both the periphery and the germinal centre. Finally, acetylation of H4 was significantly upregulated in inflamed biopsies and PP from patients with CD. Enhanced acetylation of H4K5 and K16 was seen in the PP. These results demonstrate that histone acetylation is associated with inflammation and may provide a novel therapeutic target for mucosal inflammation.

No MeSH data available.


Related in: MedlinePlus