Li J, Xu M, Zhou H, Ma J, Potter H
Department of Neurobiology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Cell. 1997 Sep 5;90(5):917-27. doi: 10.1016/s0092-8674(00)80356-6.
Mutations in two related genes, presenilin 1 and 2, account for most early-onset familial Alzheimer's disease. Although structural features indicate that the presenilins are membrane proteins, their function(s) is unknown. We have localized the presenilins to the nuclear membrane, its associated interphase kinetochores, and the centrosomes-all subcellular structures involved in cell cycle regulation and mitosis. The colocalization of the presenilins with kinetochores on the nucleoplasmic surface of the inner nuclear membrane, together with other results, suggests that they may play a role in chromosome organization and segregation, perhaps as kinetochore binding proteins/receptors. We discuss a pathogenic pathway for familial Alzheimer's disease in which defective presenilin function causes chromosome missegregation during mitosis, resulting in apoptosis and/or trisomy 21 mosaicism.
两个相关基因早老素1和2的突变是大多数早发性家族性阿尔茨海默病的病因。尽管结构特征表明早老素是膜蛋白,但其功能尚不清楚。我们已将早老素定位于核膜、其相关的间期动粒和中心体——所有参与细胞周期调控和有丝分裂的亚细胞结构。早老素与内核膜核质表面动粒的共定位以及其他结果表明,它们可能在染色体组织和分离中发挥作用,也许作为动粒结合蛋白/受体。我们讨论了家族性阿尔茨海默病的致病途径,其中有缺陷的早老素功能导致有丝分裂期间染色体错误分离,从而导致细胞凋亡和/或21三体嵌合体。