• 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

γ射线照射后人肾T1细胞组蛋白的多聚ADP核糖基化(体外实验)

Poly-ADP-ribosylation of histone proteins of human kidney T1-cells in vitro following gamma-irradiation.

作者信息

Sharan R N, Schneeweiss F H, Saikia J R, Feinendegen L E

机构信息

Department of Biochemistry, North-Eastern Hill University, Shillong, India.

出版信息

Indian J Biochem Biophys. 1998 Apr;35(2):97-102.

PMID:9753868
Abstract

Poly-ADP-ribosylation of cellular proteins is involved with radiation induced damage and its repair. It has been observed that suspension of human kidney T1-cells in vitro attained elevated levels of poly-ADP-ribosylation due to experimental manipulations necessary for preparation of single cell suspension from monolayer cell cultures. These cells in suspension were exposed to various doses of gamma-rays with or without subsequent repair incubation. The PADPR of histones H3, H1 and H2B increased with increasing dose of radiation and decreased after 90 min or repair incubation. Concomitant with these changes, the affinity of histones to DNA in chromatin reduced immediately after irradiation. Normal affinity was reestablished after post-irradiation repair incubation. The results indicate that induction of poly-ADP-ribosylation of histone proteins by radiation and by manipulations to prepare single cell suspension involved different cellular components.

摘要

细胞蛋白质的多聚 ADP 核糖基化与辐射诱导的损伤及其修复有关。据观察,由于从单层细胞培养物制备单细胞悬液所需的实验操作,人肾 T1 细胞在体外悬浮时多聚 ADP 核糖基化水平升高。将这些悬浮细胞暴露于不同剂量的γ射线,有无后续修复孵育。组蛋白 H3、H1 和 H2B 的多聚 ADP 核糖基化随辐射剂量增加而增加,并在 90 分钟或修复孵育后降低。伴随这些变化,染色质中组蛋白与 DNA 的亲和力在照射后立即降低。照射后修复孵育后恢复正常亲和力。结果表明,辐射和制备单细胞悬液的操作诱导组蛋白的多聚 ADP 核糖基化涉及不同的细胞成分。

相似文献

1
Poly-ADP-ribosylation of histone proteins of human kidney T1-cells in vitro following gamma-irradiation.γ射线照射后人肾T1细胞组蛋白的多聚ADP核糖基化(体外实验)
Indian J Biochem Biophys. 1998 Apr;35(2):97-102.
2
Regulation of the enzymatic catalysis of poly(ADP-ribose) polymerase by dsDNA, polyamines, Mg2+, Ca2+, histones H1 and H3, and ATP.双链DNA、多胺、Mg2+、Ca2+、组蛋白H1和H3以及ATP对聚(ADP - 核糖)聚合酶酶促催化作用的调控。
Biochemistry. 2004 Jan 13;43(1):210-6. doi: 10.1021/bi0301791.
3
Alterations in the polynucleosomal structure of chromatin by poly ADP-ribosylation of nuclear proteins.通过核蛋白的多聚ADP核糖基化作用改变染色质的多核小体结构。
Princess Takamatsu Symp. 1982;12:189-204.
4
Change of ADP-ribosylation in human kidney T1-cells by various external stimuli.多种外部刺激对人肾T1细胞中ADP核糖基化的影响。
Indian J Biochem Biophys. 1995 Jun;32(3):119-24.
5
Neutrons affect ADP-ribosylation of proteins in human kidney T1-cells in vitro.中子在体外影响人肾T1细胞中蛋白质的ADP核糖基化。
Indian J Biochem Biophys. 1996 Aug;33(4):281-4.
6
The life history of poly(ADP-ribose).聚(ADP - 核糖)的生命历程。
Princess Takamatsu Symp. 1983;13:129-40.
7
ADP-ribosylation, DNA repair, cell differentiation and cancer.ADP核糖基化、DNA修复、细胞分化与癌症。
Princess Takamatsu Symp. 1983;13:3-25.
8
Ca2+, Mg2+-dependent endonuclease and ADP-ribosylation.钙、镁依赖性核酸内切酶与ADP核糖基化作用
Princess Takamatsu Symp. 1983;13:183-93.
9
ADP-ribosylation of pancreatic histone H1 and of other histones.胰腺组蛋白H1及其他组蛋白的ADP核糖基化作用。
Can J Biochem. 1980 Jun;58(6):509-15. doi: 10.1139/o80-069.
10
Selective isolation of domains of chromatin proximal to both carcinogen-induced DNA damage and poly-adenosine diphosphate-ribosylation.对致癌物诱导的DNA损伤和多聚二磷酸腺苷核糖基化附近的染色质结构域进行选择性分离。
Cancer Res. 1985 Jan;45(1):386-91.

引用本文的文献

1
Detection and quantification of poly-ADP-ribosylated cellular proteins of spleen and liver tissues of mice in vivo by slot and Western blot immunoprobing using polyclonal antibody against mouse ADP-ribose polymer.利用抗小鼠 ADP 核糖聚合物的多克隆抗体,通过狭缝印迹和 Western 印迹免疫检测法在体内检测和定量小鼠脾脏和肝脏组织中多聚 ADP 核糖基化的细胞蛋白。
Mol Cell Biochem. 2005 Oct;278(1-2):213-21. doi: 10.1007/s11010-005-7588-6.