热休克对 NG108-15 细胞球状乙酰胆碱酯酶转录的诱导作用。
An induction effect of heat shock on the transcript of globular acetylcholinesterase in NG108-15 cells.
机构信息
Department of Biology and Center for Chinese Medicine, The Hong Kong University of Science and Technology, Clear Water Bay Road, Kowloon, Hong Kong SAR, China.
出版信息
Chem Biol Interact. 2010 Sep 6;187(1-3):106-9. doi: 10.1016/j.cbi.2010.02.024. Epub 2010 Feb 20.
Heat shock response, an induced transcription of a set of genes in response to high temperature, occurs in all organisms. In neurons, the catalytic subunit of acetylcholinesterase (AChE(T)) interacts with proline-rich membrane anchor (PRiMA) to form a globular tetrameric form (G(4) form). In this study, we examined the effects of heat shock on the transcription and protein assembly of AChE(T) in cultured NG108-15 cells. The transcription of AChE(T) was rapidly induced by heat shock at 40 degrees C, reaching a 15-fold increase in 3h and decreasing thereafter. On the other hand, the level of PRiMA mRNA was not affected after the heat shock. In parallel with AChE(T) mRNA, the enzymatic activity of cellular AChE, in terms of G(1) and G(2) forms, was increased after heat shock; however, the PRiMA-linked G(4) remained unchanged. These results suggest that heat shock can induce the expression level of AChE(T) by the regulation of AChE(T) transcripts in NG108-15 cells.
热休克反应是一种在高温下诱导一组基因转录的现象，存在于所有生物中。在神经元中，乙酰胆碱酯酶（AChE）的催化亚基（AChE(T)）与富含脯氨酸的膜锚定蛋白（PRiMA）相互作用，形成球形四聚体形式（G(4)形式）。在这项研究中，我们研究了热休克对培养的 NG108-15 细胞中 AChE(T)转录和蛋白组装的影响。在 40°C 的热休克下，AChE(T)的转录迅速被诱导，3 小时内增加了 15 倍，此后减少。另一方面，热休克后 PRiMA mRNA 的水平没有受到影响。与 AChE(T) mRNA 平行的是，细胞 AChE 的酶活性，以 G(1)和 G(2)形式，在热休克后增加；然而，PRiMA 连接的 G(4)保持不变。这些结果表明，热休克可以通过调节 NG108-15 细胞中的 AChE(T)转录本来诱导 AChE(T)的表达水平。
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