Onopordopicrin from the Japanese Leaf Burdock Exerts Antiallergic Effects through the Inhibition of I Kappa B Kinase β

IF 3.5 2区 农林科学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Akihiro Maeta, Honoka Ishikawa, Yuka Okamoto, Kyoko Takahashi
{"title":"Onopordopicrin from the Japanese Leaf Burdock Exerts Antiallergic Effects through the Inhibition of I Kappa B Kinase β","authors":"Akihiro Maeta,&nbsp;Honoka Ishikawa,&nbsp;Yuka Okamoto,&nbsp;Kyoko Takahashi","doi":"10.1155/2024/3999202","DOIUrl":null,"url":null,"abstract":"<div>\n <p>Onopordopicrin (OPP), found in burdock leaves and stems, exerts antiallergic properties whose mechanism remains elusive. We aimed to elucidate its mechanism using rat basophilic leukemia cells <i>in vitro</i>. Purified OPP demonstrated concentration-dependent inhibition of degranulation after allergen or PMA/A23187 stimulation. OPP effectively suppressed TNF-<i>α</i> and PGD2 releases. However, OPP did not suppress the increase in intracellular Ca<sup>2+</sup> concentration after allergen stimulation. The <i>α</i>, <i>β</i>-unsaturated carbonyl structure of OPP suggests potential electrophilic reactivity with polyfunctional thiol-trapping agents, such as cysteine residues. Indeed, the degranulation-inhibiting effect of OPP disappeared with the addition of cysteamine, which possesses a thiol group. I kappa B kinase <i>β</i> (IKK<i>β</i>), which regulates degranulation in an NF-<i>κ</i>B-independent manner, possesses a cysteine residue between the activation loop. Moreover, IKK<i>β</i> plays an important role in TNF-<i>α</i> and PGD2 production. OPP was found to reduce IKK<i>β</i> activity in a concentration-dependent manner. Together, our findings suggest that OPP exerts its antiallergic action via binding to cysteine residues in signal proteins such as IKK<i>β</i>, thereby inhibiting their activation.</p>\n </div>","PeriodicalId":15802,"journal":{"name":"Journal of Food Biochemistry","volume":null,"pages":null},"PeriodicalIF":3.5000,"publicationDate":"2024-07-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1155/2024/3999202","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Food Biochemistry","FirstCategoryId":"97","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1155/2024/3999202","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Onopordopicrin (OPP), found in burdock leaves and stems, exerts antiallergic properties whose mechanism remains elusive. We aimed to elucidate its mechanism using rat basophilic leukemia cells in vitro. Purified OPP demonstrated concentration-dependent inhibition of degranulation after allergen or PMA/A23187 stimulation. OPP effectively suppressed TNF-α and PGD2 releases. However, OPP did not suppress the increase in intracellular Ca2+ concentration after allergen stimulation. The α, β-unsaturated carbonyl structure of OPP suggests potential electrophilic reactivity with polyfunctional thiol-trapping agents, such as cysteine residues. Indeed, the degranulation-inhibiting effect of OPP disappeared with the addition of cysteamine, which possesses a thiol group. I kappa B kinase β (IKKβ), which regulates degranulation in an NF-κB-independent manner, possesses a cysteine residue between the activation loop. Moreover, IKKβ plays an important role in TNF-α and PGD2 production. OPP was found to reduce IKKβ activity in a concentration-dependent manner. Together, our findings suggest that OPP exerts its antiallergic action via binding to cysteine residues in signal proteins such as IKKβ, thereby inhibiting their activation.

Abstract Image

日本牛蒡叶中的Onopordopicrin通过抑制I Kappa B激酶β发挥抗过敏作用
牛蒡叶和茎中含有的Onopordopicrin(OPP)具有抗过敏特性,但其机制至今仍不清楚。我们的目的是利用体外大鼠嗜碱性粒细胞白血病细胞来阐明其机制。纯化的 OPP 对过敏原或 PMA/A23187 刺激后的脱颗粒表现出浓度依赖性抑制作用。OPP 能有效抑制 TNF-α 和 PGD2 的释放。然而,OPP 并不能抑制过敏原刺激后细胞内 Ca2+ 浓度的增加。OPP的α、β-不饱和羰基结构表明它可能与多官能硫醇捕获剂(如半胱氨酸残基)发生亲电反应。事实上,加入具有硫醇基团的半胱胺后,OPP 的脱颗粒抑制作用就消失了。I kappa B 激酶 β(IKKβ)以不依赖于 NF-κB 的方式调节脱颗粒,其激活环之间有一个半胱氨酸残基。此外,IKKβ 在 TNF-α 和 PGD2 的产生中起着重要作用。研究发现,OPP 能以浓度依赖性方式降低 IKKβ 的活性。总之,我们的研究结果表明,OPP 是通过与 IKKβ 等信号蛋白中的半胱氨酸残基结合,从而抑制它们的活化来发挥抗过敏作用的。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Journal of Food Biochemistry
Journal of Food Biochemistry 生物-生化与分子生物学
CiteScore
7.80
自引率
5.00%
发文量
488
审稿时长
3.6 months
期刊介绍: The Journal of Food Biochemistry publishes fully peer-reviewed original research and review papers on the effects of handling, storage, and processing on the biochemical aspects of food tissues, systems, and bioactive compounds in the diet. Researchers in food science, food technology, biochemistry, and nutrition, particularly based in academia and industry, will find much of great use and interest in the journal. Coverage includes: -Biochemistry of postharvest/postmortem and processing problems -Enzyme chemistry and technology -Membrane biology and chemistry -Cell biology -Biophysics -Genetic expression -Pharmacological properties of food ingredients with an emphasis on the content of bioactive ingredients in foods Examples of topics covered in recently-published papers on two topics of current wide interest, nutraceuticals/functional foods and postharvest/postmortem, include the following: -Bioactive compounds found in foods, such as chocolate and herbs, as they affect serum cholesterol, diabetes, hypertension, and heart disease -The mechanism of the ripening process in fruit -The biogenesis of flavor precursors in meat -How biochemical changes in farm-raised fish are affecting processing and edible quality
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信