线粒体氧化磷酸化的解偶联消除了胰岛素对糖酵解酶与肌肉细胞骨架结合的刺激作用。

T Livnat, M Chen-Zion, R Beitner
{"title":"线粒体氧化磷酸化的解偶联消除了胰岛素对糖酵解酶与肌肉细胞骨架结合的刺激作用。","authors":"T Livnat,&nbsp;M Chen-Zion,&nbsp;R Beitner","doi":"10.1016/0020-711x(93)90112-r","DOIUrl":null,"url":null,"abstract":"<p><p>1. We show here that treatment of diaphragm muscle with 2,4-dinitrophenol (DNP), an uncoupler of oxidative phosphorylation, abolished the stimulatory action of insulin on binding of the glycolytic enzymes, phosphofructokinase (PFK) and aldolase, to muscle cytoskeleton. This effect was demonstrated with low concentration of DNP, which caused only a small decrease in ATP and did not affect the basic levels of cytoskeleton-bound glycolytic enzymes. 2. Higher concentrations of DNP, which induced a drastic decline in ATP content, caused a decrease in cytoskeleton-bound glycolytic enzymes and damage to myofibrils. 3. These results suggest that mitochondrial ATP is required for both the preservation of the basal levels of cytoskeleton-bound glycolytic enzymes and cell structure, as well as for the expression of the stimulatory action of insulin on glycolytic enzymes' binding to muscle cytoskeleton.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":"25 7","pages":"993-7"},"PeriodicalIF":0.0000,"publicationDate":"1993-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(93)90112-r","citationCount":"9","resultStr":"{\"title\":\"Uncoupling of mitochondrial oxidative phosphorylation abolishes the stimulatory action of insulin on the binding of glycolytic enzymes to muscle cytoskeleton.\",\"authors\":\"T Livnat,&nbsp;M Chen-Zion,&nbsp;R Beitner\",\"doi\":\"10.1016/0020-711x(93)90112-r\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>1. We show here that treatment of diaphragm muscle with 2,4-dinitrophenol (DNP), an uncoupler of oxidative phosphorylation, abolished the stimulatory action of insulin on binding of the glycolytic enzymes, phosphofructokinase (PFK) and aldolase, to muscle cytoskeleton. This effect was demonstrated with low concentration of DNP, which caused only a small decrease in ATP and did not affect the basic levels of cytoskeleton-bound glycolytic enzymes. 2. Higher concentrations of DNP, which induced a drastic decline in ATP content, caused a decrease in cytoskeleton-bound glycolytic enzymes and damage to myofibrils. 3. These results suggest that mitochondrial ATP is required for both the preservation of the basal levels of cytoskeleton-bound glycolytic enzymes and cell structure, as well as for the expression of the stimulatory action of insulin on glycolytic enzymes' binding to muscle cytoskeleton.</p>\",\"PeriodicalId\":22539,\"journal\":{\"name\":\"The International journal of biochemistry\",\"volume\":\"25 7\",\"pages\":\"993-7\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1993-07-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0020-711x(93)90112-r\",\"citationCount\":\"9\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"The International journal of biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1016/0020-711x(93)90112-r\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"The International journal of biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1016/0020-711x(93)90112-r","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 9

摘要

1. 我们在这里表明,用2,4-二硝基苯酚(DNP)处理膈肌,一种氧化磷酸化解耦剂,消除了胰岛素对糖酵解酶,磷酸果糖激酶(PFK)和醛缩酶结合肌肉细胞骨架的刺激作用。低浓度的DNP证明了这种作用,它只引起ATP的少量减少,并且不影响细胞骨架结合的糖酵解酶的基本水平。2. 较高浓度的DNP诱导ATP含量急剧下降,导致细胞骨架结合糖酵解酶减少和肌原纤维损伤。3.这些结果表明,线粒体ATP对于维持细胞骨架结合的糖酵解酶的基础水平和细胞结构,以及胰岛素对糖酵解酶与肌肉细胞骨架结合的刺激作用的表达都是必需的。
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
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Uncoupling of mitochondrial oxidative phosphorylation abolishes the stimulatory action of insulin on the binding of glycolytic enzymes to muscle cytoskeleton.

1. We show here that treatment of diaphragm muscle with 2,4-dinitrophenol (DNP), an uncoupler of oxidative phosphorylation, abolished the stimulatory action of insulin on binding of the glycolytic enzymes, phosphofructokinase (PFK) and aldolase, to muscle cytoskeleton. This effect was demonstrated with low concentration of DNP, which caused only a small decrease in ATP and did not affect the basic levels of cytoskeleton-bound glycolytic enzymes. 2. Higher concentrations of DNP, which induced a drastic decline in ATP content, caused a decrease in cytoskeleton-bound glycolytic enzymes and damage to myofibrils. 3. These results suggest that mitochondrial ATP is required for both the preservation of the basal levels of cytoskeleton-bound glycolytic enzymes and cell structure, as well as for the expression of the stimulatory action of insulin on glycolytic enzymes' binding to muscle cytoskeleton.

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
自引率
0.00%
发文量
0
期刊最新文献
Reduced muscle protein breakdown in septic rats following treatment with interleukin-1 receptor antagonist. Induction of a 60-kDa heat shock protein in rat pancreas by water-immersion stress. Identification of a microsomal retinoic acid synthase as a microsomal cytochrome P-450-linked monooxygenase system. A comparative study on lipid peroxidation in cerebral cortex of stroke-prone spontaneously hypertensive and normotensive rats. Isolation and characterization of fibrinogenase from Candida albicans NH-1.
×
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