如何利用质谱技术研究 AMPK。

IF 5.6 2区生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY Essays in biochemistry Pub Date : 2024-11-18 DOI:10.1042/EBC20240009

Mark H Rider, Didier Vertommen, Manuel Johanns

{"title":"如何利用质谱技术研究 AMPK。","authors":"Mark H Rider, Didier Vertommen, Manuel Johanns","doi":"10.1042/EBC20240009","DOIUrl":null,"url":null,"abstract":"AMP-activated protein kinase (AMPK) is a key regulator of metabolism and a recognised target for the treatment of metabolic diseases such as Type 2 diabetes (T2D). Here, we review how mass spectrometry (MS) can be used to study short-term control by AMPK via protein phosphorylation and long-term control due to changes in protein expression. We discuss how MS can quantify AMPK subunit levels in tissues from different species. We propose hydrogen-deuterium exchange (HDX)-MS to investigate molecular mechanisms of AMPK activation and thermoproteomic profiling (TPP) to assess off-target effects of pharmacological AMPK activators/inhibitors. Lastly, because large MS data sets are generated, we consider different approaches that can be used for their interpretation.","PeriodicalId":11812,"journal":{"name":"Essays in biochemistry","volume":" ","pages":"283-294"},"PeriodicalIF":5.6000,"publicationDate":"2024-11-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"How mass spectrometry can be exploited to study AMPK.\",\"authors\":\"Mark H Rider, Didier Vertommen, Manuel Johanns\",\"doi\":\"10.1042/EBC20240009\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"AMP-activated protein kinase (AMPK) is a key regulator of metabolism and a recognised target for the treatment of metabolic diseases such as Type 2 diabetes (T2D). Here, we review how mass spectrometry (MS) can be used to study short-term control by AMPK via protein phosphorylation and long-term control due to changes in protein expression. We discuss how MS can quantify AMPK subunit levels in tissues from different species. We propose hydrogen-deuterium exchange (HDX)-MS to investigate molecular mechanisms of AMPK activation and thermoproteomic profiling (TPP) to assess off-target effects of pharmacological AMPK activators/inhibitors. Lastly, because large MS data sets are generated, we consider different approaches that can be used for their interpretation.\",\"PeriodicalId\":11812,\"journal\":{\"name\":\"Essays in biochemistry\",\"volume\":\" \",\"pages\":\"283-294\"},\"PeriodicalIF\":5.6000,\"publicationDate\":\"2024-11-18\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Essays in biochemistry\",\"FirstCategoryId\":\"88\",\"ListUrlMain\":\"https://doi.org/10.1042/EBC20240009\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Essays in biochemistry","FirstCategoryId":"88","ListUrlMain":"https://doi.org/10.1042/EBC20240009","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}

引用次数: 0

摘要

AMP激活蛋白激酶（AMPK）是新陈代谢的关键调节因子，也是公认的治疗代谢性疾病（如2型糖尿病）的靶点。在此，我们回顾了质谱法（MS）如何用于研究 AMPK 通过蛋白磷酸化进行的短期控制以及通过蛋白表达变化进行的长期控制。我们讨论了质谱如何量化不同物种组织中的 AMPK 亚基水平。我们建议用氢-氘交换（HDX）-质谱来研究 AMPK 激活的分子机制，用热蛋白组学分析（TPP）来评估药理 AMPK 激活剂/抑制剂的脱靶效应。最后，由于产生了大量 MS 数据集，我们考虑了可用于解释这些数据集的不同方法。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

How mass spectrometry can be exploited to study AMPK.

AMP-activated protein kinase (AMPK) is a key regulator of metabolism and a recognised target for the treatment of metabolic diseases such as Type 2 diabetes (T2D). Here, we review how mass spectrometry (MS) can be used to study short-term control by AMPK via protein phosphorylation and long-term control due to changes in protein expression. We discuss how MS can quantify AMPK subunit levels in tissues from different species. We propose hydrogen-deuterium exchange (HDX)-MS to investigate molecular mechanisms of AMPK activation and thermoproteomic profiling (TPP) to assess off-target effects of pharmacological AMPK activators/inhibitors. Lastly, because large MS data sets are generated, we consider different approaches that can be used for their interpretation.

求助全文

通过发布文献求助，成功后即可免费获取论文全文。去求助

来源期刊

Essays in biochemistry 生物-生化与分子生物学

CiteScore

10.50

自引率

0.00%

发文量

105

审稿时长

>12 weeks

期刊介绍： Essays in Biochemistry publishes short, digestible reviews from experts highlighting recent key topics in biochemistry and the molecular biosciences. Written to be accessible for those not yet immersed in the subject, each article is an up-to-date, self-contained summary of the topic. Bridging the gap between the latest research and established textbooks, Essays in Biochemistry will tell you what you need to know to begin exploring the field, as each article includes the top take-home messages as summary points. Each issue of the journal is guest edited by a key opinion leader in the area, and whether you are continuing your studies or moving into a new research area, the Journal gives a complete picture in one place. Essays in Biochemistry is proud to publish Understanding Biochemistry, an essential online resource for post-16 students, teachers and undergraduates. Providing up-to-date overviews of key concepts in biochemistry and the molecular biosciences, the Understanding Biochemistry issues of Essays in Biochemistry are published annually in October.

期刊最新文献

NUAK: never underestimate a kinase. New developments in AMPK and mTORC1 cross-talk. How mass spectrometry can be exploited to study AMPK. New concepts in the roles of AMPK in adipocyte stem cell biology. Does AMPK bind glycogen in skeletal muscle or is the relationship correlative?