CAJ | 학술논문

帕金森病是一种慢性中枢神经系统退行性疾病,其主要的病理特征是黑质致密部多巴胺能神经元丢失,残存神经元胞质中出现路易小体,其主要成分是异常聚集的α-synu-clein蛋白(α-突触核蛋白)。α-synuclein的聚集与多种因素有关,其中金属离子与α-synuclein结合可导致蛋白构象发生变化引起蛋白发生聚集。近年的研究发现,Cu2+能够特异地结合α-synuclein蛋白,并诱导α-synuclein 的聚集。该文就Cu2+与α-synuclein相互作用的的结合位点、结合模式以及Cu2+在α-synuclein毒性形式中可能发挥的作用作一综述。
파금삼병시일충만성중추신경계통퇴행성질병,기주요적병리특정시흑질치밀부다파알능신경원주실,잔존신경원포질중출현로역소체,기주요성분시이상취집적α-synu-clein단백(α-돌촉핵단백)。α-synuclein적취집여다충인소유관,기중금속리자여α-synuclein결합가도치단백구상발생변화인기단백발생취집。근년적연구발현,Cu2+능구특이지결합α-synuclein단백,병유도α-synuclein 적취집。해문취Cu2+여α-synuclein상호작용적적결합위점、결합모식이급Cu2+재α-synuclein독성형식중가능발휘적작용작일종술。
Parkinson’ s disease ( PD) is a chronic degenerative disease of the central nervous system. The pathological hallmarks of PD are the loss of the nigrostriatal dopaminergic neurons and the presence of intraneuronal proteinacious cytoplasmic inclu-sions, termed“Lewy Bodies” (LBs). Its main component is the abnormal aggregated α-synuclein. Multiple factors have have been shown to affect α-synuclein aggregation. Metal ions com-bine with α-synuclein can lead to protein conformation changes that inducing protein aggregation. In recent years, the study found that Cu2+ could bind specifically to the protein and trigger its aggregation under conditions. It might be relevant for the de-velopment of PD. This present review attempts to look at the evi-dence for coordination, affinity and the physiology function of Cu2+ binding to α-synuclein.