Neurological Surgery, University of Pittsburgh, 4401 Penn Avenue, Pittsburgh, PA, 15224, USA.
Neurology, University of Pittsburgh, 200 Lothrop Street, Pittsburgh, PA, 15261, USA.
Mol Neurobiol. 2021 Jan;58(1):362-374. doi: 10.1007/s12035-020-02123-w. Epub 2020 Sep 19.
Alpha synuclein (α-synuclein) is a neuronal protein found predominately in presynaptic terminals. While the pathological effect of α-synuclein aggregates has been a topic of intense study in several neurodegenerative conditions, less attention has been placed on changes in monomeric α-synuclein and related physiological consequences on neuronal function. A growing body of evidence supports an important physiological role of α-synuclein in neurotransmission. In the context of traumatic brain injury (TBI), we hypothesized that the regional abundance of soluble monomeric α-synuclein is altered over a chronic time period post-injury. To this end, we evaluated α-synuclein in the cortex, hippocampus, and striatum of adult rats at 6 h, 1 day, 1, 2, 4, and 8 weeks after controlled cortical impact (CCI) injury. Western blot analysis demonstrated decreased levels of monomer α-synuclein protein in the ipsilateral hippocampus at 6 h, 1 day, 1, 2, and 8 weeks, as well as in the ipsilateral cortex at 1 and 2 weeks and in the ipsilateral striatum at 6 h after CCI compared with sham animals. Immunohistochemical analysis revealed lower α-synuclein and a modest reduction in synaptophysin staining in the ipsilateral hippocampus at 1 week after CCI compared with sham animals, with no evidence of intracellular or extracellular α-synuclein aggregates. Collectively, these findings demonstrate that monomeric α-synuclein protein abundance in the hippocampus is reduced over an extensive (acute-to-chronic) post-injury interval. This deficit may contribute to the chronically impaired neurotransmission known to occur after TBI.
α-突触核蛋白(α-synuclein)是一种主要存在于突触前末梢的神经元蛋白。虽然 α-突触核蛋白聚集的病理作用一直是几种神经退行性疾病的研究热点,但对单体 α-突触核蛋白的变化及其对神经元功能的相关生理后果的关注较少。越来越多的证据支持 α-突触核蛋白在神经传递中具有重要的生理作用。在创伤性脑损伤(TBI)的背景下,我们假设受伤后慢性期内,可溶性单体 α-突触核蛋白的区域丰度会发生变化。为此,我们在成年大鼠大脑皮质、海马体和纹状体中评估了皮质撞击伤(CCI)后 6 小时、1 天、1、2、4 和 8 周时的 α-突触核蛋白。Western blot 分析表明,在 CCI 后 6 小时、1 天、1、2 和 8 周时,同侧海马体以及 1 和 2 周时的同侧皮质和 6 小时时的同侧纹状体中,单体 α-突触核蛋白蛋白水平降低。免疫组织化学分析显示,与假手术动物相比,CCI 后 1 周时同侧海马体中的 α-突触核蛋白和突触小体蛋白染色减少,且无细胞内或细胞外 α-突触核蛋白聚集的证据。总的来说,这些发现表明,海马体中的单体 α-突触核蛋白蛋白丰度在广泛的(急性到慢性)伤后间隔内减少。这种缺陷可能导致 TBI 后已知的慢性神经传递受损。