Szabo Paul, Relkin Norman, Weksler Marc E
Department of Neurology, Weill Medical College of Cornell University, New York, NY 10021, USA.
Autoimmun Rev. 2008 Jun;7(6):415-20. doi: 10.1016/j.autrev.2008.03.007. Epub 2008 Apr 10.
Properties of human, natural anti-Abeta antibodies and commercially available intravenous immunoglobulin (IVIg) have been examined in light of the beneficial effects of passive immunotherapy with IVIg for patients with mild to moderate Alzheimer's disease (AD). Anti-Abeta antibodies in IVIg recognize conformation-specific epitopes as well as linear epitopes from different regions of the Abeta peptide. Anti-Abeta antibodies in circulation, especially those with high avidity, are often masked by ligands and the avidity of these antibodies increases upon dissociation of the bound ligands from the antibodies. Such natural anti-Abeta antibodies have the capacity to prevent Abeta oligomer-induced neurotoxicity in N2A neuroblastoma cells. This neuro-protective effect may reflect the therapeutic potential of the natural anti-Abeta antibodies found in IVIg for the treatment of patients with AD.
鉴于静脉注射免疫球蛋白（IVIg）对轻度至中度阿尔茨海默病（AD）患者进行被动免疫治疗具有有益效果，已对人天然抗淀粉样蛋白β（Aβ）抗体和市售IVIg的特性进行了研究。IVIg中的抗Aβ抗体识别构象特异性表位以及来自Aβ肽不同区域的线性表位。循环中的抗Aβ抗体，尤其是那些高亲和力的抗体，常常被配体掩盖，并且这些抗体的亲和力在结合的配体与抗体解离时会增加。此类天然抗Aβ抗体具有预防Aβ寡聚体诱导的N2A神经母细胞瘤细胞神经毒性的能力。这种神经保护作用可能反映了IVIg中发现的天然抗Aβ抗体在治疗AD患者方面的治疗潜力。
