• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

甲状腺激素对大鼠肝细胞核蛋白体外磷酸化、乙酰化及 ADP 核糖基化的影响。

The effects of thyroid hormone on in vitro phosphorylation, acetylation, and ADP ribosylation of rat liver nuclear proteins.

作者信息

Nikodem V M, Huang D R, Trus B L, Rall J E

出版信息

Horm Metab Res. 1983 Nov;15(11):550-4. doi: 10.1055/s-2007-1018785.

DOI:10.1055/s-2007-1018785
PMID:6654319
Abstract

The effect of thyroid hormone on acetylation, phosphorylation and ADP ribosylation of rat liver nucleoproteins was studied by incubating intact nuclei with labeled precursors. Acetylation, which occurred in histones and low molecular weight proteins (less than 30,000), was depressed in nuclei from thyroidectomized animals. The administration of L-3,5,3'-triiodothyronine (T3) increased acetate incorporation to 50% over control levels. Incorporation of labeled phosphate from ATP into most proteins was decreased in nuclei from thyroidectomized animals and increased by the administration of T3. The greatest increase produced by T3 (to 140% of control values) was seen in proteins of molecular weight greater than 68,000. Nuclei from thyroidectomized animals incorporated less ADP ribose in most proteins. Both high molecular weight proteins (greater than 68,000) and low molecular weight proteins (less than 30,000) showed a further decrease in ADP ribose incorporation in nuclei from thyroidectomized rats given T3. However, a few proteins of the middle molecular weight class showed increased ADP ribose incorporation subsequent to the injection of T3. It is suggested that a generalized increase in protein synthetic rates previously noted to be caused by T3 is accompanied by increased acetylation and phosphorylation of histones and other proteins. These changes could accelerate transcription of already active genes.

摘要

通过用标记前体孵育完整细胞核,研究了甲状腺激素对大鼠肝脏核蛋白乙酰化、磷酸化和ADP核糖基化的影响。乙酰化发生在组蛋白和低分子量蛋白(小于30,000)中,甲状腺切除动物的细胞核中乙酰化受到抑制。给予L-3,5,3'-三碘甲状腺原氨酸(T3)后,乙酸掺入量比对照水平增加了50%。甲状腺切除动物的细胞核中,ATP中标记磷酸盐掺入大多数蛋白的量减少,而给予T3后则增加。T3产生的最大增加量(达到对照值的140%)出现在分子量大于68,000的蛋白中。甲状腺切除动物的细胞核在大多数蛋白中掺入的ADP核糖较少。高分子量蛋白(大于68,000)和低分子量蛋白(小于30,000)在给予T3的甲状腺切除大鼠的细胞核中,ADP核糖掺入量都进一步减少。然而,少数中等分子量类别的蛋白在注射T3后显示出ADP核糖掺入增加。有人提出,先前注意到由T3引起的蛋白质合成速率普遍增加伴随着组蛋白和其他蛋白乙酰化和磷酸化的增加。这些变化可能会加速已激活基因的转录。

相似文献

1
The effects of thyroid hormone on in vitro phosphorylation, acetylation, and ADP ribosylation of rat liver nuclear proteins.甲状腺激素对大鼠肝细胞核蛋白体外磷酸化、乙酰化及 ADP 核糖基化的影响。
Horm Metab Res. 1983 Nov;15(11):550-4. doi: 10.1055/s-2007-1018785.
2
Spermine-induced variations in the adenosine 5'-diphosphate ribosylation patterns of nuclear proteins from rat liver and hepatoma.
Cancer Res. 1979 Apr;39(4):1382-9.
3
Thyroid hormone action: in vitro characterization of solubilized nuclear receptors from rat liver and cultured GH1 cells.甲状腺激素作用:大鼠肝脏和培养的GH1细胞中可溶性核受体的体外特性研究
J Clin Invest. 1974 Oct;54(4):853-65. doi: 10.1172/JCI107825.
4
[Binding of triiodothyronine to the nuclear matrix of the rat liver. The effect of thyroid hormones on the phosphorylation of nuclear matrix proteins].[三碘甲状腺原氨酸与大鼠肝脏核基质的结合。甲状腺激素对核基质蛋白磷酸化的影响]
Biokhimiia. 1986 Jan;51(1):112-7.
5
ADP-ribosylation of nuclear proteins is increased by phenobarbital. Identification of the ADP-ribosylated histone fractions in rat liver nuclei.苯巴比妥可增加核蛋白的 ADP 核糖基化。大鼠肝细胞核中 ADP 核糖基化组蛋白组分的鉴定。
FEBS Lett. 1986 Apr 21;199(2):164-8. doi: 10.1016/0014-5793(86)80472-0.
6
Effect of thyroid hormone on the phosphorylation of 110k proteins and the activity of protein kinase NII of rat liver nucleoli.甲状腺激素对大鼠肝脏核仁110k蛋白磷酸化及蛋白激酶NII活性的影响。
Biochem Int. 1988 May;16(5):895-901.
7
Protein ADP-ribosylation in rat liver cytosol.大鼠肝细胞溶胶中的蛋白质 ADP 核糖基化作用。
Biochem Int. 1983 Dec;7(6):747-54.
8
ADP-ribosylation of proteins--a multifunctional process.
Hoppe Seylers Z Physiol Chem. 1981 Nov;362(11):1415-25.
9
Maturation of human promyelocytic leukemia cells induced by nicotinamide: evidence of a regulatory role for ADP-ribosylation of chromosomal proteins.烟酰胺诱导人早幼粒细胞白血病细胞成熟:染色体蛋白ADP-核糖基化起调节作用的证据
J Cell Physiol. 1984 Nov;121(2):334-40. doi: 10.1002/jcp.1041210210.
10
[Effect of insulin of acetylation of histones and non-histone proteins in the cell nuclei of the liver of albine rats of different age].
Vopr Med Khim. 1976 Nov-Dec;22(6):795-8.