Department of Biological Sciences, Science/Nursing Building, Room 228, Boise State University, Boise, ID 83725, USA.
Neurobiol Dis. 2011 Jul;43(1):68-78. doi: 10.1016/j.nbd.2010.11.003. Epub 2010 Nov 21.
The Beclin-1 protein is essential for the initiation of autophagy, and recent studies suggest this function may be compromised in Alzheimer's disease (AD). In addition, in vitro studies have supported a loss of function of Beclin-1 due to proteolytic modification by caspases. In the present study, we examined whether caspase-cleavage of Beclin-1 occurs in the AD brain by designing a site-directed caspase-cleavage antibody based upon a known cleavage site within the protein at position D149. We confirmed that Beclin-1 is an excellent substrate for caspase-3 and demonstrates cleavage led to the formation of a 35-kDa C-terminal fragment labeled by our novel antibody following Western blot analysis. Application of this antibody termed Beclin-1 caspase-cleavage product antibody or BeclinCCP in frontal cortex tissue sections revealed strong immunolabeling within astrocytes that localized with plaque regions and along blood vessels in all AD cases examined. In addition, weaker, more variable BeclinCCP labeling was also observed within neurofibrillary tangles that colocalized with the early tau conformational marker, MC-1 as well as the late tangle marker, PHF-1. Collectively, these data support a depletion of Beclin-1 in AD following caspase-cleavage. This article is part of a Special Issue entitled "Autophagy and protein degradation in neurological diseases."
Beclin-1 蛋白对于自噬的起始至关重要,最近的研究表明,这种功能可能在阿尔茨海默病(AD)中受损。此外,体外研究支持由于半胱天冬酶的蛋白水解修饰,Beclin-1 功能丧失。在本研究中,我们通过设计基于蛋白在位置 D149 处的已知切割位点的靶向半胱天冬酶切割抗体,来检查 AD 脑中是否存在 Beclin-1 的半胱天冬酶切割。我们证实 Beclin-1 是半胱天冬酶-3 的极佳底物,并且在 Western blot 分析后,该切割导致形成了 35 kDa 的 C 末端片段,该片段被我们的新型抗体标记。该抗体称为 Beclin-1 半胱天冬酶切割产物抗体或 BeclinCCP,在额皮质组织切片中的应用显示,在所有检查的 AD 病例中,星形胶质细胞内均有强烈的免疫标记,定位于斑块区域并沿着血管。此外,还观察到神经原纤维缠结内的 BeclinCCP 标记较弱且更可变,这些缠结与早期 tau 构象标记物 MC-1 以及晚期缠结标记物 PHF-1 共定位。总之,这些数据支持 AD 中 Beclin-1 在半胱天冬酶切割后的耗竭。本文是题为“神经疾病中的自噬和蛋白质降解”的特刊的一部分。