葡萄糖和嘧啶核苷对埃利希腹水细胞利用[14C]甲酸盐的作用机制

Annette Herscovics, R.M. Johnstone
{"title":"葡萄糖和嘧啶核苷对埃利希腹水细胞利用[14C]甲酸盐的作用机制","authors":"Annette Herscovics,&nbsp;R.M. Johnstone","doi":"10.1016/0926-6550(64)90065-9","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. When Ehrlich ascites cells are incubated in the presence of glucose, uridine, or cytidine, the intracellular concentration of free glutamate is greatly increased. The specific activity of [<sup>14</sup>C]glutamate formed from [<sup>14</sup>C]glucose is decreased 50% in the presence of 1 mM uridine.</p></span></li><li><span>2.</span><span><p>2. [<sup>14</sup>C]Formate incorporation into both proteins and nucleic acids of Ehrlich ascites cells is greatly stimulated by glucose, uridine, glutamine and glutamate.</p></span></li><li><span>3.</span><span><p>3. Methionine sulphoximine completely prevents the stimulations of formate utilization by glucose and uridine. These effects of methionine sulphoximine are reversed by glutamine.</p></span></li><li><span>4.</span><span><p>4. It is suggested that the increased intracellular concentration of glutamate in the presence of exogenous glucose, uridine or glutamate leads to an increased availability of glutamine necessary for the synthesis of purine nucleotides and proteins. The availability of glutamate appears to be limiting for amino acid incorporation into proteins.</p></span></li><li><span>5.</span><span><p>5. Exogenous [<sup>14</sup>C]glutamate is very poorly transported by Ehrlich ascites cells. After 1 h of incubation, a ratio of 0.3 for the distribution of radioactivity between cells and medium is obtained.</p></span></li><li><span>6.</span><span><p>6. The incorporation of [<sup>14</sup>C]formate into free serine is stimulated 20–40-fold by glucose, uridine and cytidine. [<sup>14</sup>C]Formate incorporation into serine is greater under anaerobic conditions than under aerobic conditions.</p></span></li></ul></div>","PeriodicalId":100173,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1964-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6550(64)90065-9","citationCount":"6","resultStr":"{\"title\":\"Mechanism of action of glucose and pyrimidine nucleosides on [14C]formate utilization by Ehrlich ascites cells\",\"authors\":\"Annette Herscovics,&nbsp;R.M. Johnstone\",\"doi\":\"10.1016/0926-6550(64)90065-9\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. When Ehrlich ascites cells are incubated in the presence of glucose, uridine, or cytidine, the intracellular concentration of free glutamate is greatly increased. The specific activity of [<sup>14</sup>C]glutamate formed from [<sup>14</sup>C]glucose is decreased 50% in the presence of 1 mM uridine.</p></span></li><li><span>2.</span><span><p>2. [<sup>14</sup>C]Formate incorporation into both proteins and nucleic acids of Ehrlich ascites cells is greatly stimulated by glucose, uridine, glutamine and glutamate.</p></span></li><li><span>3.</span><span><p>3. Methionine sulphoximine completely prevents the stimulations of formate utilization by glucose and uridine. These effects of methionine sulphoximine are reversed by glutamine.</p></span></li><li><span>4.</span><span><p>4. It is suggested that the increased intracellular concentration of glutamate in the presence of exogenous glucose, uridine or glutamate leads to an increased availability of glutamine necessary for the synthesis of purine nucleotides and proteins. The availability of glutamate appears to be limiting for amino acid incorporation into proteins.</p></span></li><li><span>5.</span><span><p>5. Exogenous [<sup>14</sup>C]glutamate is very poorly transported by Ehrlich ascites cells. After 1 h of incubation, a ratio of 0.3 for the distribution of radioactivity between cells and medium is obtained.</p></span></li><li><span>6.</span><span><p>6. The incorporation of [<sup>14</sup>C]formate into free serine is stimulated 20–40-fold by glucose, uridine and cytidine. [<sup>14</sup>C]Formate incorporation into serine is greater under anaerobic conditions than under aerobic conditions.</p></span></li></ul></div>\",\"PeriodicalId\":100173,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-11-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6550(64)90065-9\",\"citationCount\":\"6\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926655064900659\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926655064900659","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 6

摘要

1.1. 当埃利希腹水细胞在葡萄糖、尿苷或胞苷的存在下孵育时,细胞内游离谷氨酸的浓度大大增加。[14C]葡萄糖形成的[14C]谷氨酸的比活性在1mm尿苷存在下降低50%。[14C]葡萄糖、尿苷、谷氨酰胺和谷氨酸极大地刺激了甲酸进入埃利希腹水细胞的蛋白质和核酸。甲硫氨酸亚砜完全阻止葡萄糖和尿嘧啶对甲酸盐利用的刺激。甲硫氨酸亚砜的这些作用可被谷氨酰胺逆转。这表明,在外源性葡萄糖、尿苷或谷氨酸存在的情况下,细胞内谷氨酸浓度增加导致谷氨酰胺的可用性增加,而谷氨酰胺是合成嘌呤核苷酸和蛋白质所必需的。谷氨酸的可用性似乎限制了氨基酸与蛋白质的结合。外源性[14C]谷氨酸在埃利希腹水细胞中运输很差。孵育1 h后,细胞与培养基之间的放射性分布比例为0.3。葡萄糖、尿苷和胞苷可刺激甲酸[14C]与游离丝氨酸结合20 - 40倍。[14C]在无氧条件下,甲酸掺入丝氨酸比在有氧条件下更多。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Mechanism of action of glucose and pyrimidine nucleosides on [14C]formate utilization by Ehrlich ascites cells

  • 1.

    1. When Ehrlich ascites cells are incubated in the presence of glucose, uridine, or cytidine, the intracellular concentration of free glutamate is greatly increased. The specific activity of [14C]glutamate formed from [14C]glucose is decreased 50% in the presence of 1 mM uridine.

  • 2.

    2. [14C]Formate incorporation into both proteins and nucleic acids of Ehrlich ascites cells is greatly stimulated by glucose, uridine, glutamine and glutamate.

  • 3.

    3. Methionine sulphoximine completely prevents the stimulations of formate utilization by glucose and uridine. These effects of methionine sulphoximine are reversed by glutamine.

  • 4.

    4. It is suggested that the increased intracellular concentration of glutamate in the presence of exogenous glucose, uridine or glutamate leads to an increased availability of glutamine necessary for the synthesis of purine nucleotides and proteins. The availability of glutamate appears to be limiting for amino acid incorporation into proteins.

  • 5.

    5. Exogenous [14C]glutamate is very poorly transported by Ehrlich ascites cells. After 1 h of incubation, a ratio of 0.3 for the distribution of radioactivity between cells and medium is obtained.

  • 6.

    6. The incorporation of [14C]formate into free serine is stimulated 20–40-fold by glucose, uridine and cytidine. [14C]Formate incorporation into serine is greater under anaerobic conditions than under aerobic conditions.

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
×
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