抗淀粉样蛋白CE/J小鼠菌株表达的一种独特的淀粉样蛋白载脂蛋白血清淀粉样蛋白A (apoSAA)异构体对巨噬细胞的亲和力高于淀粉样蛋白易感CBA/J小鼠表达的apoSAA1和apoSAA2

Jun-shan Liang , Rosemary Elliott-Bryant , Tahar Hajri , Jean D. Sipe , Edgar S. Cathcart
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引用次数: 17

摘要

CBA/J和其他表达淀粉样蛋白血清淀粉样蛋白A (apoSAA)、apoSAA2以及apoSAA1的近交系小鼠对淀粉样蛋白A (AA)淀粉样变性易感,而表达单一独特亚型apoSAACEJ的CE/J小鼠则具有抗性。研究表明,在apoSAACEJ存在的情况下表达apoSAA2的CBA/J×CE/J杂交小鼠可以防止淀粉样蛋白的发生。为了确定apoSAACEJ表达在apoSAA2存在时防止AA形成的机制,我们研究了重组apoSAA (r-apoSAA)异构体与小鼠巨噬细胞的结合,并通过n端测序验证。放射性标记的apoSAA与IC-21巨噬细胞(1×105 cells/ml)在4℃下孵育30分钟后,特异性结合达到最大。125I-r-apoSAA1、125I-r-apoSAA2和125I-r-apoSAACEJ的结合具有特异性和可饱和性,亲和度(Kd)分别约为2.8、3.2和1.3 nM,每个细胞约为2-4×106位点。竞争结合实验表明,apoSAACEJ与巨噬细胞的结合比apoSAA1和apoSAA2具有更高的亲和力。我们认为,与apoSAA2相比,apoSAACEJ具有更大的细胞亲和力,可能通过干扰巨噬细胞与apoSAA2的相互作用,从而导致膜相关或细胞内降解,从而有助于保护某些CBA/J×CE/J杂交小鼠免受AA淀粉样蛋白的侵害。
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A unique amyloidogenic apolipoprotein serum amyloid A (apoSAA) isoform expressed by the amyloid resistant CE/J mouse strain exhibits higher affinity for macrophages than apoSAA1 and apoSAA2 expressed by amyloid susceptible CBA/J mice

CBA/J and other inbred strains of mice that express the amyloidogenic apolipoprotein serum amyloid A (apoSAA) apoSAA2, together with apoSAA1, are susceptible to amyloid A (AA) amyloidosis, whereas CE/J mice that express a single unique isoform, apoSAACEJ, are resistant. Studies indicate that CBA/J×CE/J hybrid mice that express apoSAA2 in the presence of apoSAACEJ are protected from amyloidogenesis. To define a mechanism by which expression of apoSAACEJ may protect from AA formation in the presence of apoSAA2, binding of recombinant apoSAA (r-apoSAA) isoforms, validated by N-terminal sequencing, to a murine macrophage cell line was investigated. Maximal specific binding occurred after incubation of radiolabeled apoSAA with IC-21 macrophages (1×105 cells/ml) for 30 min at 4°C. The binding of 125I-r-apoSAA1, 125I-r-apoSAA2 and 125I-r-apoSAACEJ was specific and saturable, with an affinity (Kd) of about 2.8, 3.2 and 1.3 nM, respectively, and approximately 2–4×106 sites per cell. Competitive binding experiments indicate apoSAACEJ binds with higher affinity to macrophages than does either apoSAA1 or apoSAA2. We suggest that greater cellular affinity of apoSAACEJ compared to apoSAA2 may contribute to protection from AA amyloid in certain CBA/J×CE/J hybrid mice by interfering with interaction of apoSAA2 by macrophages and hence either membrane associated or intracellular degradation.

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