Amino-terminal identity of co-existent amyloid and non-amyloid immunoglobulin κ light chain deposits.: A human disease to study alterations of protein conformation
Amino-terminal identity of co-existent amyloid and non-amyloid immunoglobulin κ light chain deposits.: A human disease to study alterations of protein conformation
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DOI：
10.1046/j.1365-2249.1997.4421454.x
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发表时间：
1997-12-01
影响因子：
4.6
通讯作者：
Gallo, G
中科院分区：
文献类型：
--
作者：
Kaplan, B;Vidal, R;Gallo, G
单克隆免疫球蛋白轻链组织沉积是某些B细胞增生性疾病患者的严重并发症。淀粉样蛋白（AL）的沉积物典型为纤原性和嗜铜性，轻链沉积病（LCDD）的沉积物典型为非纤原性和嗜铜性，很少在同一患者中共存。从一个在不同部位有纤维性和非纤维性kappa轻链沉积的个体的死后组织中，我们分别从分离的肾小球中提取和分析了非淀粉样沉积物，从分离的肾动脉中提取了淀粉样物质，从心肌中提取了淀粉样物质，其中淀粉样物质仅局限于壁动脉。对提取的淀粉样蛋白和非淀粉样蛋白沉积物进行Western blotting分析，发现25-kD条带与抗kappa抗体有免疫反应，并且n端氨基酸序列属于可变区kappa（IV）轻链亚群。这是首次对抗原性相似但形态不同的沉积物分别进行生物化学分析的人类疾病。我们认为LCDD和AL合并是一种理想的人类疾病，可以研究非淀粉样向淀粉样构象转化的关系和影响因素。
Tissue deposition of monoclonal immunoglobulin light chains is a serious complication in some patients with B cell proliferative disorders. The deposits are typically fibrillar and Congophilic in amyloid (AL) and non-fibrillar and Congophobic in light chain deposition disease (LCDD), and rarely coexist in the same patient. From post-mortem tissue of an individual with fibrillar and non-fibrillar kappa light chain deposits in different sites, we separately extracted and analysed biochemically and immunochemically the non-amyloid deposits from isolated glomeruli, the amyloid from isolated renal arteries and the amyloid from myocardium in which the only deposits were amyloid restricted to mural arteries. Western blotting analysis of both the extracted amyloid and the non-amyloid deposits demonstrated 25-kD bands immunoreactive with anti-kappa antibody, and the identity of the N-terminal amino acid sequences that belong to the variable region kappa(IV) light chain subgroup. This is the first human disease in which antigenically similar but morphologically different deposits have been separately biochemically analysed. We propose that combined LCDD and AL is an ideal human disease to study the relationships and the factors that influence the conversion of non-amyloidogenic to amyloidogenic conformations.