Ampicillin activates Mpk1 phosphorylation in Saccharomyces cerevisiaeand ERK1/2 phosphorylation in HepG2 cells

IF 1.1 4区 生物学 Q3 BIOLOGY Turkish Journal of Biology Pub Date : 2017-08-01 DOI:10.3906/BIY-1611-8
Yu-Kyong Shin, Ki-Young Kim
{"title":"Ampicillin activates Mpk1 phosphorylation in Saccharomyces cerevisiaeand ERK1/2 phosphorylation in HepG2 cells","authors":"Yu-Kyong Shin, Ki-Young Kim","doi":"10.3906/BIY-1611-8","DOIUrl":null,"url":null,"abstract":"Ampicillin has been widely used to treat bacterial infections. When we used ampicillin to eliminate bacterial contamination in yeast cultures, we observed induction of phosphorylation of MAP kinase 1 (Mpk1), a previously unknown function of ampicillin. We therefore investigated whether ampicillin activates the signal transduction pathway. Phosphorylation of Saccharomyces cerevisiae Mpk1 was induced by ampicillin in a dose- and time-dependent manner through the PKC1-CWI pathway. Mpk1 phosphorylation was maximal after treatment with 3 mM ampicillin for 90 min. Despite activation of Mpk1 phosphorylation, ampicillin did not influence yeast cell growth. Ampicillin reduced miconazole antifungal activity; miconazole had a minimum inhibitory concentration of 3.125 µg/mL against Candida albicans, which increased to 25 µg/mL after 48 h of treatment with 3 mM ampicillin. Finally, ampicillin activated phosphorylation of ERK1/2 (a mammalian homolog of Mpk1), with maximum effect at 3 mM ampicillin, in human HepG2 cells, but did not influence cell viability. The results of this study clearly indicate that ampicillin activated Mpk1 phosphorylation in yeast and ERK1/2 phosphorylation in HepG2 cells. In addition to its clinical application to eliminate bacteria, ampicillin could also be used to activate Mpk1 or ERK1/2 in the laboratory.","PeriodicalId":23358,"journal":{"name":"Turkish Journal of Biology","volume":null,"pages":null},"PeriodicalIF":1.1000,"publicationDate":"2017-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3906/BIY-1611-8","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Turkish Journal of Biology","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.3906/BIY-1611-8","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Ampicillin has been widely used to treat bacterial infections. When we used ampicillin to eliminate bacterial contamination in yeast cultures, we observed induction of phosphorylation of MAP kinase 1 (Mpk1), a previously unknown function of ampicillin. We therefore investigated whether ampicillin activates the signal transduction pathway. Phosphorylation of Saccharomyces cerevisiae Mpk1 was induced by ampicillin in a dose- and time-dependent manner through the PKC1-CWI pathway. Mpk1 phosphorylation was maximal after treatment with 3 mM ampicillin for 90 min. Despite activation of Mpk1 phosphorylation, ampicillin did not influence yeast cell growth. Ampicillin reduced miconazole antifungal activity; miconazole had a minimum inhibitory concentration of 3.125 µg/mL against Candida albicans, which increased to 25 µg/mL after 48 h of treatment with 3 mM ampicillin. Finally, ampicillin activated phosphorylation of ERK1/2 (a mammalian homolog of Mpk1), with maximum effect at 3 mM ampicillin, in human HepG2 cells, but did not influence cell viability. The results of this study clearly indicate that ampicillin activated Mpk1 phosphorylation in yeast and ERK1/2 phosphorylation in HepG2 cells. In addition to its clinical application to eliminate bacteria, ampicillin could also be used to activate Mpk1 or ERK1/2 in the laboratory.
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
氨苄青霉素激活酿酒酵母Mpk1磷酸化和HepG2细胞ERK1/2磷酸化
氨苄青霉素已被广泛用于治疗细菌感染。当我们使用氨苄青霉素消除酵母培养物中的细菌污染时,我们观察到MAP激酶1(Mpk1)的磷酸化诱导,这是氨苄青霉素以前未知的功能。因此,我们研究了氨苄青霉素是否激活信号转导途径。氨苄青霉素通过PKC1-CWI途径以剂量和时间依赖的方式诱导酿酒酵母Mpk1磷酸化。用3mM氨苄青霉素处理90分钟后,Mpk1磷酸化最大。尽管Mpk1磷酸化被激活,但氨苄青霉素不影响酵母细胞生长。氨苄青霉素降低了咪康唑的抗真菌活性;咪康唑对白色念珠菌的最低抑制浓度为3.125µg/mL,用3mM氨苄青霉素治疗48小时后,该浓度增至25µg/mL。最后,在人HepG2细胞中,氨苄青霉素激活ERK1/2(Mpk1的哺乳动物同源物)的磷酸化,在3mM氨苄青霉素时效果最大,但不影响细胞活力。该研究的结果清楚地表明,氨苄青霉素激活了酵母中的Mpk1磷酸化和HepG2细胞中的ERK1/2磷酸化。氨苄青霉素除了在临床上用于消灭细菌外,还可以在实验室中用于激活Mpk1或ERK1/2。
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 去求助
来源期刊
CiteScore
4.60
自引率
0.00%
发文量
20
审稿时长
6-12 weeks
期刊介绍: The Turkish Journal of Biology is published electronically 6 times a year by the Scientific and Technological Research Council of Turkey (TÜBİTAK) and accepts English-language manuscripts concerning all kinds of biological processes including biochemistry and biosynthesis, physiology and metabolism, molecular genetics, molecular biology, genomics, proteomics, molecular farming, biotechnology/genetic transformation, nanobiotechnology, bioinformatics and systems biology, cell and developmental biology, stem cell biology, and reproductive biology. Contribution is open to researchers of all nationalities.
期刊最新文献
CircRNA LDLR promotes proliferation and aerobic glycolysis of gastric cancer cells by targeting CHD1 with miR-449b-5p Divergent Proteomic Profiles of Opium Poppy Cultivars Beneficial effects of a novel polyherbal formulation on the skeletal muscle antioxidant status, inflammation, and muscle-signaling proteins in exercised rats Prognostic gene biomarkers for c-Src inhibitor Si162 sensitivity in melanoma cells Effect of thymol on oxidative stress and reelin signaling pathway in Alzheimer's disease model
×
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
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 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 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1