Choi P, Golts N, Snyder H, Chong M, Petrucelli L, Hardy J, Sparkman D, Cochran E, Lee J M, Wolozin B
Department of Pharmacology, Loyola University Medical Center, Bldg. 102, Rm. 3634, 2160 S. 1st Ave., Maywood, IL 60153, USA.
Neuroreport. 2001 Sep 17;12(13):2839-43. doi: 10.1097/00001756-200109170-00017.
Parkin and alpha-synuclein are two proteins that are associated with the pathophysiology of Parkinson's disease (PD). Parkin is present in Lewy bodies and axonal spheroids in brains affected by PD, and mutations in parkin cause hereditary forms of Parkinsonism. Alpha-synuclein is a major component of Lewy bodies and is associated with rare cases of PD. We now show that parkin binds to alpha-synuclein, including conditions associated with alpha-synuclein aggregation. Parkin and alpha-synuclein complexes were observed in BE-M17 cells under basal conditions, in BE- M17 cells under oxidative conditions and in brains from control or PD donors. Double staining of PD brains shows parkin and alpha-synuclein co-localize to the same pathological structures (both Lewy bodies and axonal spheroids). These results suggest that parkin interacts with alpha-synuclein and could contribute to the pathophysiology of PD more generally than was previously considered.
帕金蛋白和α-突触核蛋白是两种与帕金森病（PD）病理生理学相关的蛋白质。帕金蛋白存在于受帕金森病影响的大脑的路易小体和轴突球体中，帕金蛋白的突变会导致遗传性帕金森症。α-突触核蛋白是路易小体的主要成分，与罕见的帕金森病病例有关。我们现在表明，帕金蛋白与α-突触核蛋白结合，包括与α-突触核蛋白聚集相关的情况。在基础条件下的BE-M17细胞、氧化条件下的BE-M17细胞以及对照或帕金森病供体的大脑中均观察到帕金蛋白和α-突触核蛋白复合物。帕金森病大脑的双重染色显示，帕金蛋白和α-突触核蛋白共定位于相同的病理结构（路易小体和轴突球体）。这些结果表明，帕金蛋白与α-突触核蛋白相互作用，并且可能比之前认为的更广泛地参与帕金森病的病理生理学过程。
