The synucleins.
The synucleins.
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突触核素。
DOI：
10.1186/gb-2001-3-1-reviews3002
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发表时间：
2002
期刊：
影响因子：
12.3
通讯作者：
中科院分区：
文献类型：
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作者：
突触核蛋白是主要在脑组织、周围神经系统、视网膜和某些肿瘤中表达的小的可溶性蛋白质。它们的功能尚不清楚，尽管一些数据表明在调节膜稳定性和/或周转中起作用，并且α-突触核蛋白在几种神经退行性疾病中异常积累。突触核蛋白是主要在神经组织和某些肿瘤中表达的小的可溶性蛋白质。该家族包括三种已知的蛋白质：α-突触核蛋白、β-突触核蛋白和γ-突触核蛋白。所有突触核蛋白都具有高度保守的α-螺旋脂质结合基序，与可交换载脂蛋白的A2类脂质结合结构域相似。突触核蛋白家族成员在脊椎动物之外没有发现，尽管它们与植物“晚期胚胎丰富”蛋白具有一些保守的结构相似性。α-和β-突触核蛋白主要存在于脑组织中，主要见于突触前末梢。γ-突触核蛋白主要存在于外周神经系统和视网膜中，但其在乳腺肿瘤中的表达是肿瘤进展的标志物。正常的细胞功能尚未确定任何的突触核蛋白的蛋白质，虽然一些数据表明，在调节膜的稳定性和/或营业额的作用。α-突触核蛋白的突变与早发性帕金森病的罕见家族病例有关，并且该蛋白质在帕金森病，阿尔茨海默病和其他几种神经退行性疾病中异常积累。目前的挑战是了解这些蛋白质的正常细胞功能以及它们如何促进人类疾病的发展。
Synucleins are small, soluble proteins expressed primarily in brain tissue, the peripheral nervous system, the retina and certain tumors. Their functions are not clear, although some data suggest a role in the regulation of membrane stability and/or turnover, and α-synuclein protein accumulates abnormally in several neurodegenerative illnesses. Synucleins are small, soluble proteins expressed primarily in neural tissue and in certain tumors. The family includes three known proteins: α-synuclein, β-synuclein, and γ-synuclein. All synucleins have in common a highly conserved α-helical lipid-binding motif with similarity to the class-A2 lipid-binding domains of the exchangeable apolipoproteins. Synuclein family members are not found outside vertebrates, although they have some conserved structural similarity with plant 'late-embryo-abundant' proteins. The α- and β-synuclein proteins are found primarily in brain tissue, where they are seen mainly in presynaptic terminals. The γ-synuclein protein is found primarily in the peripheral nervous system and retina, but its expression in breast tumors is a marker for tumor progression. Normal cellular functions have not been determined for any of the synuclein proteins, although some data suggest a role in the regulation of membrane stability and/or turnover. Mutations in α-synuclein are associated with rare familial cases of early-onset Parkinson's disease, and the protein accumulates abnormally in Parkinson's disease, Alzheimer's disease, and several other neurodegenerative illnesses. The current challenge is to understand the normal cellular function of these proteins and how they might contribute to the development of human disease.