Bastar-Juarez Liliana, Castillo-Estrada Ximena, Margarit-Mendez Daniela, Coca-Gutierrez Paola
Facultad Mexicana de Medicina Universidad La Salle, Las Fuentes 17, Tlalpan Centro I, Tlalpan, 14000, Ciudad de México, CDMX, México.
Mol Neurobiol. 2025 Jun 7. doi: 10.1007/s12035-025-05112-z.
Creutzfeldt-Jakob disease (CJD) is a prion-caused condition characterized by progressive neurodegeneration and spongiform structural changes in the brain due to vacuolization and neuronal death. The disease is driven by the accumulation of abnormally folded prion proteins (PrPSc), derived from the normal cellular protein (PrPC). Actin, a fundamental protein essential for maintaining cellular structure and function, is critically involved in the pathophysiology of several neurodegenerative diseases, including Creutzfeldt-Jakob disease (CJD). In CJD, the dysregulation of actin-binding proteins such as cofilin and gelsolin significantly contributes to disease progression by disrupting actin turnover and cytoskeletal reorganization. The actin cytoskeleton is also essential for synaptic plasticity and the functionality of excitatory neurotransmitter receptors, such as glutamate-gated ion channels (AMPA) and N-methyl-D-aspartate (NMDA) receptors. As cytoskeletal integrity deteriorates, receptor dynamics become impaired, leading to disrupted calcium signaling and deficits in cognitive functions. Additionally, actin-based structures, known as tunneling nanotubes (TNTs), play crucial roles in prion spread by facilitating cell-to-cell transfer of prions. Simultaneously, the prion-infected neuronal environment promotes the formation of these structures, further driving disease progression. Targeting actin dynamics through the modulation of actin-binding proteins and related signaling pathways presents a promising avenue for therapeutic development. These approaches hold potential for addressing CJD for broader applications in neurodegenerative diseases characterized by cytoskeletal dysfunction. Current strategies focus on targeting cytoskeletal components such as microtubule stabilizers, actin-binding proteins, HDAC6 inhibitors, and small GTPases, further expanding the possibilities for effective treatments across various neurodegenerative conditions.
克雅氏病(CJD)是一种由朊病毒引起的疾病,其特征是由于空泡化和神经元死亡导致大脑进行性神经变性和海绵状结构变化。该疾病由源自正常细胞蛋白(PrPC)的异常折叠朊病毒蛋白(PrPSc)的积累所驱动。肌动蛋白是维持细胞结构和功能所必需的一种基本蛋白质,它在包括克雅氏病(CJD)在内的几种神经退行性疾病的病理生理学中起着关键作用。在克雅氏病中,诸如丝切蛋白和凝溶胶蛋白等肌动蛋白结合蛋白的失调通过破坏肌动蛋白周转和细胞骨架重组,显著促进了疾病进展。肌动蛋白细胞骨架对于突触可塑性以及兴奋性神经递质受体(如谷氨酸门控离子通道(AMPA)和N-甲基-D-天冬氨酸(NMDA)受体)的功能也至关重要。随着细胞骨架完整性的恶化,受体内在变化受损,导致钙信号传导中断和认知功能缺陷。此外,被称为隧道纳米管(TNTs)的基于肌动蛋白的结构,通过促进朊病毒在细胞间的转移,在朊病毒传播中发挥着关键作用。同时,被朊病毒感染的神经元环境促进了这些结构的形成,进一步推动了疾病进展。通过调节肌动蛋白结合蛋白和相关信号通路来靶向肌动蛋白动力学,为治疗开发提供了一条有前景的途径。这些方法有望解决克雅氏病问题,并在以细胞骨架功能障碍为特征的神经退行性疾病中得到更广泛的应用。目前的策略集中在靶向细胞骨架成分,如微管稳定剂、肌动蛋白结合蛋白、HDAC6抑制剂和小GTP酶,进一步扩大了针对各种神经退行性疾病进行有效治疗的可能性。