Tabaton M
Department of Pathology, Case Western Reserve University School of Medicine, Cleveland, Ohio.
Clin Geriatr Med. 1994 May;10(2):249-55.
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.
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。