LYMPHOCYTE-ACTIVATION INDUCES RAPID CHANGES IN NUCLEAR AND CYTOPLASMIC GLYCOPROTEINS
LYMPHOCYTE-ACTIVATION INDUCES RAPID CHANGES IN NUCLEAR AND CYTOPLASMIC GLYCOPROTEINS
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DOI：
10.1073/pnas.88.5.1701
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发表时间：
1991-03-01
影响因子：
11.1
通讯作者：
HART, GW
中科院分区：
文献类型：
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作者：
KEARSE, KP;HART, GW
核质和细胞质蛋白糖基化的一种独特形式，O-连接GlcNAc（O-GlcNAc）存在于从酵母到人类的蛋白质中，包括许多染色质蛋白、转录因子、核孔蛋白和某些类型的细胞骨架蛋白。在这份报告中，我们研究了细胞活化对O-GlcNAc修饰的蛋白质的影响，使用T淋巴细胞作为模型系统。结果表明，淋巴细胞活化后，许多核蛋白上的O-GlcNAc表观水平迅速增加，几小时后恢复到对照水平。相比之下，在细胞活化后，不同细胞溶质蛋白群体上的O-GlcNAc的表观水平迅速降低，并且在几小时后也恢复到对照水平。这些数据与O-GlcNAc是一种调节修饰的假设一致，并表明O-GlcNAc修饰可能在T淋巴细胞活化的早期阶段发挥重要作用。
A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, (O-GlcNAc) is present on proteins ranging from those of yeast to man, including many chromatin proteins, transcription factors, nuclear pore proteins, and certain types of cytoskeletal proteins. In this report we have studied the effects of cellular activation on O-GlcNAc-modified proteins, using T lymphocytes as a model system. Results indicate that the apparent levels of O-GlcNAc on many nuclear proteins increases rapidly after lymphocyte activation, returning to control levels after a few hours. In contrast, the apparent levels of O-GlcNAc on a distinct population of cytosolic proteins decreases rapidly after cellular activation and also returns to control levels after a few hours. These data are consistent with the hypothesis that O-GlcNAc is a regulatory modification and suggest that O-GlcNAc modification may play an important role in the early stages of T-lymphocyte activation.