与一种新型变体（Trp41Leu）相关的转甲状腺素蛋白淀粉样变性，表现为玻璃体混浊。

Transthyretin amyloidosis associated with a novel variant (Trp41Leu) presenting with vitreous opacities.

作者信息

Yazaki Masahide, Connors Lawreen H, Eagle Ralph C, Leff Steven R, Skinner Martha, Benson Merrill D

机构信息

Department of Pathology & Laboratory Medicine, Indiana University School of Medicine, 975 West Walnut Street, Indianapolis, IN 46202-5121, USA.

出版信息

Amyloid. 2002 Dec;9(4):263-7. doi: 10.3109/13506120209114104.

DOI:10.3109/13506120209114104

PMID:12557756

Abstract

We report a 45-year-old woman with a new transthyretin (TTR) variant, substitution of leucine for tryptophan at residue 41, who has showed vitreous opacities without any other visceral organ involvement since age of 42. Congo red staining of vitrectomy specimens revealed that the vitreous fluid contained amyloid fibrils, which were strongly positive for immunohistochemical staining using anti-human TTR antiserum. DNA analysis of the TTR gene showed a G to T transversion at the second nucleotide of codon 41, indicating a replacement of tryptophan (TGG) by leucine (TTG). These results indicate that the patient's vitreous amyloid is associated with this novel TTR mutation.

摘要

我们报告了一名45岁女性，其转甲状腺素蛋白（TTR）有一个新的变体，第41位残基处色氨酸被亮氨酸取代，自42岁起就出现了玻璃体混浊，而无任何其他内脏器官受累。玻璃体切除标本的刚果红染色显示，玻璃体液中含有淀粉样纤维，使用抗人TTR抗血清进行免疫组织化学染色呈强阳性。TTR基因的DNA分析显示，密码子41的第二个核苷酸发生了G到T的颠换，表明色氨酸（TGG）被亮氨酸（TTG）取代。这些结果表明，患者的玻璃体淀粉样变性与这种新的TTR突变有关。