Procyanidin A2 Modulates IL-4-Induced CCL26 Production in Human Alveolar Epithelial Cells

Allergic asthma is an inflammatory lung disease that is partly sustained by the chemokine eotaxin-3 (CCL26), which extends eosinophil migration into tissues long after allergen exposure. Modulation of CCL26 could represent a means to mitigate airway inflammation. Here we evaluated procyanidin A2 as...

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Published inInternational journal of molecular sciences Vol. 17; no. 11; p. 1888
Main Authors Coleman, Sara L, Kruger, Marlena C, Sawyer, Gregory M, Hurst, Roger D
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LanguageEnglish
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Abstract Allergic asthma is an inflammatory lung disease that is partly sustained by the chemokine eotaxin-3 (CCL26), which extends eosinophil migration into tissues long after allergen exposure. Modulation of CCL26 could represent a means to mitigate airway inflammation. Here we evaluated procyanidin A2 as a means of modulating CCL26 production and investigated interactions with the known inflammation modulator, Interferon γ (IFNγ). We used the human lung epithelial cell line A549 and optimized the conditions for inducing CCL26. Cells were exposed to a range of procyanidin A2 or IFNγ concentrations for varied lengths of time prior to an inflammatory insult of interleukin-4 (IL-4) for 24 h. An enzyme-linked immunosorbent assay was used to measure CCL26 production. Exposing cells to 5 μM procyanidin A2 (prior to IL-4) reduced CCL26 production by 35% compared with control. Greatest inhibition by procyanidin A2 was seen with a 2 h exposure prior to IL-4, whereas IFNγ inhibition was greatest at 24 h. Concomitant incubation of procyanidin A2 and IFNγ did not extend the inhibitory efficacy of procyanidin A2. These data provide evidence that procyanidin A2 can modulate IL-4-induced CCL26 production by A549 lung epithelial cells and that it does so in a manner that is different from IFNγ.
AbstractList Allergic asthma is an inflammatory lung disease that is partly sustained by the chemokine eotaxin-3 (CCL26), which extends eosinophil migration into tissues long after allergen exposure. Modulation of CCL26 could represent a means to mitigate airway inflammation. Here we evaluated procyanidin A2 as a means of modulating CCL26 production and investigated interactions with the known inflammation modulator, Interferon γ (IFNγ). We used the human lung epithelial cell line A549 and optimized the conditions for inducing CCL26. Cells were exposed to a range of procyanidin A2 or IFNγ concentrations for varied lengths of time prior to an inflammatory insult of interleukin-4 (IL-4) for 24 h. An enzyme-linked immunosorbent assay was used to measure CCL26 production. Exposing cells to 5 μM procyanidin A2 (prior to IL-4) reduced CCL26 production by 35% compared with control. Greatest inhibition by procyanidin A2 was seen with a 2 h exposure prior to IL-4, whereas IFNγ inhibition was greatest at 24 h. Concomitant incubation of procyanidin A2 and IFNγ did not extend the inhibitory efficacy of procyanidin A2. These data provide evidence that procyanidin A2 can modulate IL-4-induced CCL26 production by A549 lung epithelial cells and that it does so in a manner that is different from IFNγ.
Allergic asthma is an inflammatory lung disease that is partly sustained by the chemokine eotaxin-3 (CCL26), which extends eosinophil migration into tissues long after allergen exposure. Modulation of CCL26 could represent a means to mitigate airway inflammation. Here we evaluated procyanidin A2 as a means of modulating CCL26 production and investigated interactions with the known inflammation modulator, Interferon [gamma] (IFN[gamma]). We used the human lung epithelial cell line A549 and optimized the conditions for inducing CCL26. Cells were exposed to a range of procyanidin A2 or IFN[gamma] concentrations for varied lengths of time prior to an inflammatory insult of interleukin-4 (IL-4) for 24 h. An enzyme-linked immunosorbent assay was used to measure CCL26 production. Exposing cells to 5 [mu]M procyanidin A2 (prior to IL-4) reduced CCL26 production by 35% compared with control. Greatest inhibition by procyanidin A2 was seen with a 2 h exposure prior to IL-4, whereas IFN[gamma] inhibition was greatest at 24 h. Concomitant incubation of procyanidin A2 and IFN[gamma] did not extend the inhibitory efficacy of procyanidin A2. These data provide evidence that procyanidin A2 can modulate IL-4-induced CCL26 production by A549 lung epithelial cells and that it does so in a manner that is different from IFN[gamma].
Author Kruger, Marlena C
Sawyer, Gregory M
Coleman, Sara L
Hurst, Roger D
AuthorAffiliation 2 School of Food and Nutrition, Massey Institute of Food Science and Technology, Massey University, Palmerston North 4442, New Zealand; m.c.kruger@massey.ac.nz
1 Food and Wellness Group, The New Zealand Institute for Plant & Food Research Ltd., Palmerston North 4474, New Zealand; greg.sawyer@plantandfood.co.nz (G.M.S.); roger.hurst@plantandfood.co.nz (R.D.H.)
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– name: 1 Food and Wellness Group, The New Zealand Institute for Plant & Food Research Ltd., Palmerston North 4474, New Zealand; greg.sawyer@plantandfood.co.nz (G.M.S.); roger.hurst@plantandfood.co.nz (R.D.H.)
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  surname: Coleman
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Keywords IFNγ
airway inflammation
IL-4
procyanidin A2
eotaxin-3 (CCL26)
Language English
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Snippet Allergic asthma is an inflammatory lung disease that is partly sustained by the chemokine eotaxin-3 (CCL26), which extends eosinophil migration into tissues...
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StartPage 1888
SubjectTerms A549 Cells
airway inflammation
Airway management
Asthma
Asthma - drug therapy
Asthma - immunology
Catechin - pharmacology
Chemokine CCL26
Chemokines
Chemokines, CC - biosynthesis
Chemokines, CC - genetics
Drug Evaluation, Preclinical
eotaxin-3 (CCL26)
Epithelial Cells - drug effects
Epithelial Cells - metabolism
Gene Expression
Humans
IFNγ
IL-4
Immunologic Factors - pharmacology
Inflammation
Interleukin-4 - physiology
Polyphenols
Proanthocyanidins - pharmacology
procyanidin A2
Pulmonary Alveoli - cytology
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Title Procyanidin A2 Modulates IL-4-Induced CCL26 Production in Human Alveolar Epithelial Cells
URI https://www.ncbi.nlm.nih.gov/pubmed/27845745
https://www.proquest.com/docview/1849452174
https://search.proquest.com/docview/1839737521
https://search.proquest.com/docview/1859477169
https://pubmed.ncbi.nlm.nih.gov/PMC5133887
https://doaj.org/article/f07cd7847ad74d6a93da75096ebd0451
Volume 17
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