Amyloidogenic and non-amyloidogenic transthyretin Asn 90 variants.
Amyloidogenic and non-amyloidogenic transthyretin Asn 90 variants.
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淀粉样变性和非淀粉样变性转甲状腺素蛋白 Asn 90 变体。
DOI：
10.1111/j.1399-0004.1992.tb03131.x
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发表时间：
1992
影响因子：
3.5
通讯作者：
Saraiva,MJ
中科院分区：
文献类型：
--
作者：
Alves,IL;Almeida,MR;Skare,J;Skinner,M;Kurose,K;Sakaki,Y;Costa,PP;Saraiva,MJ
最近，在正常的葡萄牙和德国人群中发现了一种新的转甲状腺素蛋白（TTR）变体。在一个意大利血统的美国家庭中发现了同样的替代与家族性淀粉样变性多发性神经病（FAP）相关。比较等电聚焦研究表明非致病性和致病性变异之间的迁移模式存在差异。然而，对它们之间的比较DNA测序并没有发现任何额外的突变。变体与重组技术产生的 TTR Asn 90 之间的比较等电聚焦表明，非致病性变体具有突变所预期的电泳行为。我们认为，FAP 相关的 Asn 90 变体中可能发生了迄今为止未知的翻译后修饰，将其转变为淀粉样蛋白生成分子。
Recently, a new transthyretin (TTR) variant was described in the normal Portuguese and German populations. The same substitution was found associated with familial amyloidotic polyneuropathy (FAP) in an American family of Italian origin. Comparative isoelectric focusing studies showed a difference in the mobility pattern between the non‐pathogenic and pathogenic variants. However, comparative DNA sequencing between them did not reveal any additional mutation. Comparative isoelectric focusing between the variants and TTR Asn 90 produced by recombinant techniques indicated that the non‐pathogenic variant has the electrophoretic behaviour expected for the mutation. We suggest that an as yet unknown post‐translational modification may have occurred in the FAP‐associated Asn 90 variant, turning it into an amyloidogenic molecule.