Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan.
Department of Molecular Physiology, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan.
Lab Invest. 2019 Nov;99(11):1728-1740. doi: 10.1038/s41374-019-0243-8. Epub 2019 Mar 20.
Oculopharyngeal muscular dystrophy (OPMD) is a late-onset disorder characterized by ptosis, dysphagia, and weakness of proximal limbs. OPMD is caused by the expansion of polyalanine in poly(A)-binding protein, nuclear 1 (PABPN1). Although mitochondrial abnormality has been proposed as the possible etiology, the molecular pathogenesis is still poorly understood. The aim of the study was to specify the mechanism by which expanded PABPN1 causes mitochondrial dysfunction in OPMD. We evaluated whether transgenic mouse model of OPMD, by expressing expanded PABPN1, indeed causes mitochondrial abnormality associated with muscle degeneration. We also investigated the mechanism by which expanded PABPN1 would cause mitochondrial dysfunction in the mouse and cell models of OPMD. Mitochondrial localization of PABPN1 was observed in the muscle fibers of patients with OPMD. Moreover, abnormal accumulation of PABPN1 on the inner membrane of mitochondria and reduced expression of OXPHOS complexes were detected in the muscle fibers of the transgenic mice expressing expanded human PABPN1 with a 13-alanine stretch. In cells expressing PABPN1 with a 10-alanine or 18-alanine stretch, both types of PABPN1 accumulated in the mitochondria and interacted with TIM23 mitochondrial protein import complex, but PABPN1 with 18-alanine stretch decreased the cell viability and aggresome formation. We proposed that the abnormal accumulation of expanded PABPN1 in mitochondria may be associated with mitochondrial abnormality in OPMD.
眼咽型肌营养不良症(OPMD)是一种迟发性疾病,其特征为上睑下垂、吞咽困难和四肢近端无力。OPMD 是由多聚(A)结合蛋白 1(PABPN1)中多聚丙氨酸的扩展引起的。尽管已经提出线粒体异常可能是其病因,但分子发病机制仍知之甚少。本研究旨在明确扩展的 PABPN1 如何导致 OPMD 中线粒体功能障碍。我们评估了表达扩展 PABPN1 的 OPMD 转基因小鼠模型是否确实会引起与肌肉退化相关的线粒体异常。我们还研究了扩展的 PABPN1 如何在 OPMD 的小鼠和细胞模型中引起线粒体功能障碍的机制。在 OPMD 患者的肌肉纤维中观察到 PABPN1 的线粒体定位。此外,在表达扩展的人类 PABPN1(带有 13 个丙氨酸延伸)的转基因小鼠的肌肉纤维中,检测到 PABPN1 在 内 膜 上 的 异 常 积 累 和 OXPHOS 复 合 物 的 表 达 下 降 。 在 表 达 具 有 10 个 丙 氨 酸 或 18 个 丙 氨 酸 伸 展 的 PABPN1 的细胞中,两种类型的 PABPN1 都在 线粒体中积累,并与 TIM23 线粒体蛋白导入复合物相互作用,但具有 18 个丙氨酸延伸的 PABPN1 降低了细胞活力和聚集体形成。我们提出,扩展的 PABPN1 在 线粒体中的异常积累可能与 OPMD 中的线粒体异常有关。