Epigenetic Modifications in Placenta are Associated with the Child’s Sensitization to Allergens

Harb, Hani; Alhamwe, Bilal Alashkar; Acevedo, Nathalie; Frumento, Paolo; Johansson, Catharina; Eick, Lisa; Papadogiannakis, Nikos; Alm, Johan; Renz, Harald; Potaczek, Daniel P.; Scheynius, Annika

doi:10.1155/2019/1315257

Cited by 22 publications

(29 citation statements)

References 37 publications

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“…These studies clearly demonstrate the importance of this type of epigenetic modification in etiology and pathophysiology of allergies [ 24 , 25 , 26 , 27 , 28 , 29 , 30 ]. Whereas most of these studies investigated histone modification of genes involved in asthma, Harb et al explored the acetylation status of several genes in the placenta and correlated these with the prevalence of sensitization in children [ 28 ]. Interestingly, a higher histone acetylation of Ifng was associated with a lower risk of sensitization to food, suggesting a role for histone modifications in food allergy development.…”

Section: Introductionmentioning

confidence: 80%

Decreased Histone Acetylation Levels at Th1 and Regulatory Loci after Induction of Food Allergy

et al. 2020

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Immunoglobulin E (IgE)-mediated allergy against cow’s milk protein fractions such as whey is one of the most common food-related allergic disorders of early childhood. Histone acetylation is an important epigenetic mechanism, shown to be involved in the pathogenesis of allergies. However, its role in food allergy remains unknown. IgE-mediated cow’s milk allergy was successfully induced in a mouse model, as demonstrated by acute allergic symptoms, whey-specific IgE in serum, and the activation of mast cells upon a challenge with whey protein. The elicited allergic response coincided with reduced percentages of regulatory T (Treg) and T helper 17 (Th17) cells, matching decreased levels of H3 and/or H4 histone acetylation at pivotal Treg and Th17 loci, an epigenetic status favoring lower gene expression. In addition, histone acetylation levels at the crucial T helper 1 (Th1) loci were decreased, most probably preceding the expected reduction in Th1 cells after inducing an allergic response. No changes were observed for T helper 2 cells. However, increased histone acetylation levels, promoting gene expression, were observed at the signal transducer and activator of transcription 6 (Stat6) gene, a proallergic B cell locus, which was in line with the presence of whey-specific IgE. In conclusion, the observed histone acetylation changes are pathobiologically in line with the successful induction of cow’s milk allergy, to which they might have also contributed mechanistically.

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Section: Introductionmentioning

confidence: 80%

Decreased Histone Acetylation Levels at Th1 and Regulatory Loci after Induction of Food Allergy

et al. 2020

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“…Three major epigenetic processes are active in the placenta namely: DNA methylation, histone acetylation and miRNAs [ 35 , [145] , [146] , [147] ] . These epigenetic processes are closely intertwined as DNA methylation can regulate miRNA expression and vice versa [ 148 ] .…”

Section: Discussionmentioning

confidence: 99%

Placental microRNAs: Responders to environmental chemicals and mediators of pathophysiology of the human placenta

et al. 2020

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“…revealed the strong associations of histone acetylation levels in IFNG, SH2B3, and HDAC4 genes with risk of allergic sensitization. 42 Abbring et al. explored the role of histone acetylation of Th2 genes by using the Chromatin Immunoprecipitation analysis.…”

Section: Discussionmentioning

confidence: 99%

Identification of histone acetylation in a murine model of allergic asthma by proteomic analysis

Ren

Bai

et al. 2020

Exp Biol Med (Maywood)

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The pathogenesis of asthma is closely related to histone acetylation modification, but the specific acetylation sites related to this process remain indistinct. Herein, our study sought to identify differentially modified acetylation sites and their expression distribution in cells involved in asthma in lung tissues. The airway hyper-responsiveness, inflammation, and remodeling were assessed by non-invasive whole-body plethysmography, ELISA, and hematoxylin-eosin staining to confirm the successful establishment of the allergic asthma model. Afterward, the differentially modified acetylation sites in asthmatic lung tissues were identified and validated by using proteomics and western blotting, respectively. The immunohistochemistry analysis was applied to reveal the distribution of identified acetylation sites in asthmatic lung tissues. A total of 15 differentially modified acetylation sites, including 13 upregulated (H3K9ac, H3K14ac, H3K18ac, H3K23ac,H3K27ac, H3K36ac, H2B1KK120ac, H2B2BK20ac, H2BK16ac, H2BK20ac, H2BK108ac, H2BK116ac, and H2BK120ac) and 2 downregulated (H2BK5ac and H2BK11ac) sites were identified and validated. Furthermore, immunohistochemical staining of lung tissues showed that nine of the identified histone acetylation sites (H2BK5, H2BK11, H3K18, H2BK116, H2BK20, H2BK120, H3K9, H3K36, and H3K27) were differentially expressed in airway epithelial cells, and the acetylation of identified H3 histones were observed in both eosinophil and perivascular inflammatory cells. Additionally, differential expression of histone acetylation sites was also observed in nucleus of airway epithelial cells, vascular smooth muscle cells, perivascular inflammatory cells, and airway smooth muscle cells. In conclusion, we identified potential acetylation sites associated with asthma pathogenesis. These findings may contribute greatly in the search for therapeutic approaches for allergic asthma.

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Epigenetic Modifications in Placenta are Associated with the Child’s Sensitization to Allergens

Cited by 22 publications

References 37 publications

Decreased Histone Acetylation Levels at Th1 and Regulatory Loci after Induction of Food Allergy

Decreased Histone Acetylation Levels at Th1 and Regulatory Loci after Induction of Food Allergy

Placental microRNAs: Responders to environmental chemicals and mediators of pathophysiology of the human placenta

Identification of histone acetylation in a murine model of allergic asthma by proteomic analysis

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