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首页> 外文期刊>Genes to cells : >Heat shock transcription factor 1 down-regulates spermatocyte-specific 70 kDa heat shock protein expression prior to the induction of apoptosis in mouse testes.
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Heat shock transcription factor 1 down-regulates spermatocyte-specific 70 kDa heat shock protein expression prior to the induction of apoptosis in mouse testes.

机译：在小鼠睾丸中诱导凋亡之前，热休克转录因子1下调精母细胞特异性70 kDa热休克蛋白的表达。

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Expression of constitutively active heat shock transcription factor 1 (HSF1) in mouse spermatocytes induces apoptosis and leads to male infertility. We report here that prior to the onset of massive apoptosis caused by expression of active HSF1 in spermatocytes a marked reduction in spermatocyte-specific Hsp70.2 mRNA and protein levels occurs. In addition, HSP70.2 protein relocalizes from a predominant cytoplasmic to a nuclear position in developing spermatocytes that express active HSF1. Later in the developmental stages, cells undergoing HSF1-induced apoptosis essentially lack the HSP70.2 protein. The down-regulation of Hsp70.2 gene expression by HSF1 is paradoxical because HSF1 is the prototypical activator of HSP genes. Furthermore, HSF1-mediated repression neither involved a heat shock element (HSE)-like sequence adjacent to the Hsp70.2 gene nor were Hsp70.2 promoter sequences associated directly with HSF1. Interestingly, other spermatocyte- and spermatid-specific transcripts are also down-regulated in testes of transgenic mice expressing active HSF1, suggesting involvement of a putative HSF1-dependent block of development of spermatogenic cells. Importantly however, transcription of the Hsp70.2 gene is down-regulated in testes of wild-type mice subjected to a hyperthermia that induces transient activation of HSF1, indicating that the spermatocyte-specific activity of HSF1 might misdirect a network of transcription factors required for proper regulation of Hsp70.2.
机译：小鼠精母细胞中组成型活性热休克转录因子1（HSF1）的表达诱导细胞凋亡并导致男性不育。我们在这里报告，在由活跃的HSF1在精母细胞中表达引起的大规模细胞凋亡发作之前，发生了精子细胞特异性Hsp70.2 mRNA和蛋白质水平的明显降低。此外，HSP70.2蛋白在表达活性HSF1的发育中的精母细胞中从主要的细胞质重新定位到核位置。在发育后期，经历HSF1诱导的细胞凋亡的细胞基本上缺少HSP70.2蛋白。 HSF1对Hsp70.2基因表达的下调是自相矛盾的，因为HSF1是HSP基因的原型激活因子。此外，HSF1介导的镇压既不涉及与Hsp70.2基因相邻的热休克元件（HSE）样序列，也不涉及与HSF1直接相关的Hsp70.2启动子序列。有趣的是，其他表达精子细胞的和精子特异的转录物在表达活性HSF1的转基因小鼠的睾丸中也被下调，表明参与了推测的依赖HSF1的生精细胞发育阻滞。然而，重要的是，在经历过高温诱导野生型HSF1激活的野生型小鼠的睾丸中，Hsp70.2基因的转录被下调，这表明HSF1的精母细胞特异性活性可能会误导HSF1所需的转录因子网络对Hsp70.2的适当规定。

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