首页> 外文期刊>FEBS Letters >Aggregates from mutant and wild‐type α‐synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β‐sheet and amyloid‐like filaments
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Aggregates from mutant and wild‐type α‐synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β‐sheet and amyloid‐like filaments

机译:突变和野生型α-突触核蛋白和NAC肽的聚集体通过形成β-折叠和淀粉样样细丝而诱导人神经母细胞瘤细胞凋亡

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>α-Synuclein (α-syn) protein and a fragment of it, called NAC, have been found in association with the pathological lesions of a number of neurodegenerative diseases. Recently, mutations in the α-syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We have shown that human wild-type α-syn, mutant α-syn(Ala30Pro) and mutant α-syn(Ala53Thr) proteins can self-aggregate and form amyloid-like filaments. Here we report that aggregates of NAC and α-syn proteins induced apoptotic cell death in human neuroblastoma SH-SY5Y cells. These findings indicate that accumulation of α-syn and its degradation products may play a major role in the development of the pathogenesis of these neurodegenerative diseases.
机译:已经发现与许多神经退行性疾病的病理损害相关的α-突触核蛋白(α-syn)蛋白及其片段,称为NAC。近来,已经报道了在对帕金森氏病的遗传形式敏感的家庭中α-syn基因的突变。我们已经表明,人类野生型α-syn,突变体α-syn(Ala30Pro)和突变体α-syn(Ala53Thr)蛋白可以自聚集并形成淀粉样蛋白丝。在这里,我们报道了NAC和α-syn蛋白的聚集体诱导人神经母细胞瘤SH-SY5Y细胞凋亡。这些发现表明,α-syn及其降解产物的积累可能在这些神经退行性疾病的发病机理发展中起主要作用。

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