CHARACTERIZATION OF A TRANSTHYRETIN (PREALBUMIN) VARIANT ASSOCIATED WITH FAMILIAL AMYLOIDOTIC POLYNEUROPATHY TYPE-II (INDIANA SWISS)
CHARACTERIZATION OF A TRANSTHYRETIN (PREALBUMIN) VARIANT ASSOCIATED WITH FAMILIAL AMYLOIDOTIC POLYNEUROPATHY TYPE-II (INDIANA SWISS)
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DOI：
10.1172/jci112675
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发表时间：
1986-10-01
影响因子：
15.9
通讯作者：
BENSON, MD
中科院分区：
文献类型：
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作者：
DWULET, FE;BENSON, MD
从死于 II 型家族性淀粉样多发性神经病 (FAP) 的两兄弟的心脏组织中分离出淀粉样原纤维。对胰蛋白酶蛋白水解和溴化氰片段化所得肽的序列分析表明，原纤维亚基蛋白源自血浆运甲状腺素蛋白（前白蛋白）。发现约三分之二的原纤维亚基蛋白在第 84 位含有氨基酸取代，其中正常的异亮氨酸残基已被丝氨酸取代。对两兄弟以及两名临床诊断的 FAP II 型家庭成员和受影响个体的四个孩子中的两个的血浆转甲状腺素蛋白（前白蛋白）进行的序列分析显示，第 84 位存在丝氨酸。这种取代的存在也与视黄醇结合蛋白的低血清水平相关，因此第 84 位转甲状腺素蛋白（前白蛋白）可能与这两种蛋白质的相互作用有关。
Amyloid fibrils were isolated from cardiac tissue of two brothers who died from familial amyloidotic polyneuropathy (FAP) type II. Sequence analysis on peptides derived from proteolytic cleavage with trypsin and fragmentation with cyanogen bromide reveal that the fibril subunit protein is derived from plasma transthyretin (prealbumin). About two-thirds of the fibril subunit protein was found to contain an amino acid substitution at position 84 where the normal isoleucine residue has been replaced by serine. Sequence analysis of the plasma transthyretin (prealbumin) from the two brothers as well as two clinically diagnosed FAP type II family members and two of four children of affected individuals showed the presence of serine at position 84. The presence of this substitution also correlates with low serum levels of retinol-binding protein and thus transthyretin (prealbumin) position 84 may be involved with the interaction of these two proteins.