Maury C P, Baumann M
Fourth Department of Medicine, University of Helsinki, Finland.
Biochim Biophys Acta. 1990 Nov 14;1096(1):84-6. doi: 10.1016/0925-4439(90)90016-i.
Amyloid subunit protein was isolated from familial amyloid polyneuropathy type IV (Finnish type) cardiac tissue and purified to homogeneity. N-terminal amino acid sequence analysis shows that the amyloid protein is a fragment of the inner region of human gelsolin. When compared with the predicted sequence of human plasma gelsolin, the amyloid protein contains an asparagine-for-aspartic acid substitution at position 15 corresponding to residue 187 of the secreted protein. Antibodies raised against the amyloidogenic region of gelsolin specifically stained the amyloid deposited in tissues in familial amyloidosis type IV. The results show that the subunit amyloid protein in familial amyloid polyneuropathy type IV represents a unique type of amyloid derived from a variant (Asn-187) gelsolin molecule by limited proteolysis.
从IV型家族性淀粉样多神经病（芬兰型）心脏组织中分离出淀粉样亚基蛋白，并将其纯化至同质。N端氨基酸序列分析表明，淀粉样蛋白是人类凝溶胶蛋白内部区域的一个片段。与人类血浆凝溶胶蛋白的预测序列相比，淀粉样蛋白在对应于分泌蛋白第187位残基的第15位含有一个天冬酰胺替代天冬氨酸的突变。针对凝溶胶蛋白淀粉样生成区域产生的抗体特异性地染色了IV型家族性淀粉样变性病组织中沉积的淀粉样物质。结果表明，IV型家族性淀粉样多神经病中的亚基淀粉样蛋白代表了一种独特类型的淀粉样物质，它是由变体（Asn-187）凝溶胶蛋白分子通过有限的蛋白水解产生的。
