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ETS-2蛋白的磷酸化:由T细胞抗原受体-CD3复合物调控

Phosphorylation of the ETS-2 protein: regulation by the T-cell antigen receptor-CD3 complex.

作者信息

Fujiwara S, Koizumi S, Fisher R J, Bhat N K, Papas T S

机构信息

Laboratory of Molecular Oncology, National Cancer Institute, Frederick, Maryland 21701-1013.

出版信息

Mol Cell Biol. 1990 Mar;10(3):1249-53. doi: 10.1128/mcb.10.3.1249-1253.1990.

Abstract

Phosphorylation of the human ets-2 protein in response to mitogenic signals to T lymphocytes was investigated in Jurkat cells. Activation of the cells by antibodies against the T-cell antigen receptor-CD3 complex or by concanavalin A was followed within 5 min by increased phosphorylation of the protein, as shown by a mobility shift of the protein from 54 to 56 kilodaltons in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and increased incorporation of 32P. The Ca2+ ionophores A23187 and ionomycin were able to mimic this effect, suggesting that this phosphorylation is mediated by Ca2+.

摘要

在Jurkat细胞中研究了人ets - 2蛋白对T淋巴细胞有丝分裂信号的磷酸化反应。用抗T细胞抗原受体 - CD3复合物的抗体或刀豆球蛋白A激活细胞后,5分钟内该蛋白的磷酸化增加,这在十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳中表现为该蛋白的迁移率从54千道尔顿变为56千道尔顿,同时32P的掺入增加。Ca2 +离子载体A23187和离子霉素能够模拟这种效应,表明这种磷酸化是由Ca2 +介导的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af00/361013/d8fd653841d0/molcellb00039-0398-a.jpg

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