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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) (A), 8 (K8) (B), 12 (K12) (C) and 16 (K16) (D) in a Sham (control) and trinitrobenzene sulfonic acid (TNBS) rat model of colitis. Results were obtained by Western blotting. In order to evaluate changes in density from different western blotting experiments control densitometry was denoted as 100% and differences were accounted as increase percentage of the control. Representative examples of bands obtained are also illustrated. Columns represent the densitometric evaluation of three independent experiments (mean ± SEM). (*p < 0.05 vs Sham proximal or Sham distal respectively).
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Figure 2: Acetylation on histone 4 (H4) specific lysine residues 5 (K5) (A), 8 (K8) (B), 12 (K12) (C) and 16 (K16) (D) in a Sham (control) and trinitrobenzene sulfonic acid (TNBS) rat model of colitis. Results were obtained by Western blotting. In order to evaluate changes in density from different western blotting experiments control densitometry was denoted as 100% and differences were accounted as increase percentage of the control. Representative examples of bands obtained are also illustrated. Columns represent the densitometric evaluation of three independent experiments (mean ± SEM). (*p < 0.05 vs Sham proximal or Sham distal respectively).

Mentions: Acetylation of lysine (K) residues 8 and 12 were significantly increased in both the inflamed distal (K8: 818 ± 111 vs 138 ± 19%; K12: 741 ± 64 vs 121 ± 34%, both p < 0.05) and less-inflamed proximal (K8: 546 ± 50 vs 100 ± 21%; K12: 533 ± 69 vs 100 ± 26%, both p < 0.05) regions following TNBS treatment (Figure 2). However, the effect was significantly greater in the inflamed tissue than in the less-inflamed tissue for both K8 (818 ± 111 vs 546 ± 50%, p < 0.05) and K12 (741 ± 64 vs 533 ± 69%, p < 0.05).


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) (A), 8 (K8) (B), 12 (K12) (C) and 16 (K16) (D) in a Sham (control) and trinitrobenzene sulfonic acid (TNBS) rat model of colitis. Results were obtained by Western blotting. In order to evaluate changes in density from different western blotting experiments control densitometry was denoted as 100% and differences were accounted as increase percentage of the control. Representative examples of bands obtained are also illustrated. Columns represent the densitometric evaluation of three independent experiments (mean ± SEM). (*p < 0.05 vs Sham proximal or Sham distal respectively).
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 2: Acetylation on histone 4 (H4) specific lysine residues 5 (K5) (A), 8 (K8) (B), 12 (K12) (C) and 16 (K16) (D) in a Sham (control) and trinitrobenzene sulfonic acid (TNBS) rat model of colitis. Results were obtained by Western blotting. In order to evaluate changes in density from different western blotting experiments control densitometry was denoted as 100% and differences were accounted as increase percentage of the control. Representative examples of bands obtained are also illustrated. Columns represent the densitometric evaluation of three independent experiments (mean ± SEM). (*p < 0.05 vs Sham proximal or Sham distal respectively).
Mentions: Acetylation of lysine (K) residues 8 and 12 were significantly increased in both the inflamed distal (K8: 818 ± 111 vs 138 ± 19%; K12: 741 ± 64 vs 121 ± 34%, both p < 0.05) and less-inflamed proximal (K8: 546 ± 50 vs 100 ± 21%; K12: 533 ± 69 vs 100 ± 26%, both p < 0.05) regions following TNBS treatment (Figure 2). However, the effect was significantly greater in the inflamed tissue than in the less-inflamed tissue for both K8 (818 ± 111 vs 546 ± 50%, p < 0.05) and K12 (741 ± 64 vs 533 ± 69%, p < 0.05).

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