Askanas V, Engel W K, Alvarez R B
USC Neuromuscular Center, University of Southern California School of Medicine, Los Angeles 90017.
Neurosci Lett. 1992 Aug 31;143(1-2):96-100. doi: 10.1016/0304-3940(92)90241-x.
At the postsynaptic domain of the human neuromuscular junction (NMJ), we have demonstrated strong concentrations of the N-terminus 45-62, C-terminus 676-695 and beta-amyloid protein sequences of beta-amyloid precursor protein (beta APP). We used well-characterized monoclonal and polyclonal antibodies for co-localization with three other postsynaptic proteins, applying double and triple fluorescence labeling. Strong immunoreactivity of all three beta APP sequences was found at all NMJs identified by bound alpha-bungarotoxin (alpha BT), where they co-localized with alpha BT and with immunoreactive desmin and dystrophin, which are postsynaptic proteins of human NMJs. This appears to be the first demonstration of beta APP sequences concentrated postsynaptically at human NMJs. beta APP may have a role in normal junction biology and possibly in some diseases affecting NMJs.
在人类神经肌肉接头（NMJ）的突触后区域，我们已经证明β-淀粉样前体蛋白（β-APP）的N端45-62、C端676-695和β-淀粉样蛋白序列有强烈聚集。我们使用了特性明确的单克隆和多克隆抗体，通过双重和三重荧光标记与其他三种突触后蛋白进行共定位。在所有通过结合α-银环蛇毒素（α-BT）鉴定出的NMJ中，均发现所有三种β-APP序列具有强免疫反应性，它们与α-BT以及免疫反应性结蛋白和肌营养不良蛋白共定位，而后两者是人类NMJ的突触后蛋白。这似乎是首次证明β-APP序列在人类NMJ突触后区域聚集。β-APP可能在正常接头生物学中发挥作用，并且可能在一些影响NMJ的疾病中也有作用。
