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引用次数: 4
摘要
多种人类疾病，如病毒感染、糖尿病和神经退行性变，在细胞水平上的特征是内质网(ER)无法正确折叠蛋白质，导致“内质网应激”的发生。未经纠正的内质网应激激活凋亡细胞死亡途径，并且已经假设这些途径可能被操纵以获得治疗益处。在化学筛选中，Boyce等人发现了一种小分子(salubrinal)，可以保护细胞免受内质网应激诱导的凋亡。Salubrinal选择性抑制真核翻译起始因子α (eIF2α)的去磷酸化，抑制疱疹病毒的复制。因此，eIF2α可能是内质网应激相关疾病的有价值的药物靶点。M. Boyce, K. F. Bryant, C. Jousse, K. Long, H. P. Harding, D. Scheuner, R. J. Kaufman, D. Ma, D. M. Coen, D. Ron, J. Yuan。科学通报，2003,19(4)。【摘要】【全文】
Diverse human diseases such as viral infections, diabetes, and neurodegeneration are characterized at the cellular level by an inability of the endoplasmic reticulum (ER) to fold proteins properly, resulting in the onset of "ER stress." Uncorrected ER stress activates apoptotic cell death pathways, and it has been hypothesized that these pathways might be manipulated for therapeutic benefit. In a chemical screen, Boyce et al. identified a small molecule (salubrinal) that protects cells from ER-stress-induced apoptosis. Salubrinal selectively inhibited the dephosphorylation of eukaryotic translation initiation factor α (eIF2α) and inhibited herpesvirus replication. Thus, eIF2α may be a valuable drug target for diseases involving ER stress. M. Boyce, K. F. Bryant, C. Jousse, K. Long, H. P. Harding, D. Scheuner, R. J. Kaufman, D. Ma, D. M. Coen, D. Ron, J. Yuan, A selective inhibitor of eIF2α dephosphorylation protects cells from ER stress. Science 307, 935-939 (2005). [Abstract] [Full Text]
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