淀粉样变性病是一种蛋白质异常折叠疾病，目前缺乏有效的治疗手段，致死率高。抑制蛋白质异常折叠成为淀粉样变性病治疗中很有前景的靶点。我们在前期研究中曾对沉积在肾脏组织的淀粉样蛋白进行蛋白质组学分析，发现玻连蛋白（Vitronectin, Vn）广泛存在于不同类型的淀粉样沉积物中，同时伴有大量补体成分的沉积。既往的研究表明Vn的肝素结合区为蛋白质相互作用的关键结构域，Vn的C末端和N末端可以抑制补体激活、增强补体的调理作用等，因此我们提出假设：Vn可能通过其肝素结合结构域与淀粉样前体蛋白结合，促进其异常折叠形成淀粉样纤维丝，同时通过Vn的C末端和N末端的补体调节作用抑制单核巨噬细胞系统对沉积于组织上的淀粉样物质进行清除。因此，本研究将：（1）探索Vn与淀粉样变前体蛋白相互作用的机制；（2）深入探索抗Vn抗体通过激活补体系统清除淀粉样纤维丝的机制。本研究有望为淀粉样变性病寻找新的治疗靶点。

Amyloidosis is a protein misfolding disease，which lacking efficient therapy and with high mortality. The inhibition of the protein misfolding is a promising therapy target. In our previous study, proteomic analysis of the amyloid deposit indicates that, the vitronectin is a common constituent of amyloid deposits together with a mount of complement components. Previous study have indicate that the heparin binding domain of vitronectin is the key interaction domain of proteins，and the C terminal of vitronectin can inhibit the complement activation, the N-terminal of vitronectin can enhance the opsonization of complement. Depend on the above, we propose our hypothesis: vitronectin can interact with the amyloid precursor proteins via the heparin binding domain, which can promote the protein misfolding into the fibrils, and the vitronectin can inhibit complement dependent, monocyte-macrophage cell reaction which swiftly removes massive visceral amyloid deposits via the C-terminal and N-terminal. Therefore，the study will（1）explore the interaction of vitronectin with the amyloid precursors; (2) To study the mechanism of the anti-Vn antibody eradicate the amyloid fibrils via the complement system. This study is expected to find new therapy target of amyloidosis.