Song S, Ohba M, Saito Y, Honda T, Takashima A, Takahashi H
Mitsubishi Kasei Institute of Life Sciences, 11 Minamiooya, Machida-shi, Tokyo, Japan.
Neurosci Lett. 2000 Mar 17;282(1-2):65-8. doi: 10.1016/s0304-3940(00)00845-4.
Numerous mutations causing early-onset familial Alzheimer's disease have been identified in the presenilin-1 gene. Presenilin-1 protein is produced as a 47 kDa holoprotein and proteolytically processed to an N-terminal 28 kDa and a C-terminal 19 kDa fragments by unidentified presenilinase in mammalian cells. We have demonstrated that this proteolytic processing also occurs in yeast. We also show that degradation of C-terminal fragment of presenilin-1 is dependent of proteasomal function. This yeast system will be a good tool to identify presenilinase and to study the role of presenilin-1 in amyloid precursor protein processing.
在早老素-1基因中已鉴定出许多导致早发性家族性阿尔茨海默病的突变。早老素-1蛋白最初以47 kDa的全蛋白形式产生，并在哺乳动物细胞中被未知的早老素酶蛋白水解加工成N端28 kDa和C端19 kDa的片段。我们已经证明这种蛋白水解加工在酵母中也会发生。我们还表明，早老素-1 C端片段的降解依赖于蛋白酶体功能。这个酵母系统将是鉴定早老素酶以及研究早老素-1在淀粉样前体蛋白加工中作用的良好工具。
