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阿尔茨海默病生物学的研究进展

Research advances in the biology of Alzheimer's disease.

作者信息

Tabaton M

机构信息

Department of Pathology, Case Western Reserve University School of Medicine, Cleveland, Ohio.

出版信息

Clin Geriatr Med. 1994 May;10(2):249-55.

PMID:8039097
Abstract

Research on AD has shed light on the biochemical composition and mechanisms of the formation of amyloid deposits and PHFs, the structural hallmarks of the disease. Amyloid is composed of a 4-kd peptide, beta P, that originates in the metabolism of a 130-kd transmembrane precursor protein. Soluble beta P accumulates in the AD brain until it polymerizes in amyloid fibers. Paired helical filaments are composed of hyperphosphorylated tau, a microtubule-associated protein that normally acts as a tubulin assembly factor. Future research must clarify why beta P accumulates in extracellular spaces of AD tissue and focus on the relation between amyloid deposition and neuronal degeneration.

摘要

对阿尔茨海默病(AD)的研究揭示了淀粉样沉积物和神经原纤维缠结(PHFs)的生化组成及形成机制,它们是该疾病的结构特征。淀粉样蛋白由一种4千道尔顿的肽β-淀粉样蛋白(beta P)组成,其源于一种130千道尔顿跨膜前体蛋白的代谢。可溶性β-淀粉样蛋白在AD大脑中积累,直至聚合成淀粉样纤维。双螺旋丝由高度磷酸化的tau蛋白组成,tau是一种通常作为微管蛋白组装因子的微管相关蛋白。未来的研究必须阐明为何β-淀粉样蛋白会在AD组织的细胞外空间中积累,并聚焦于淀粉样沉积与神经元变性之间的关系。

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