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Familial amyloid polyneuropathy related to transthyretin Gly42 in a Japanese family
Author(s) -
Uemichi Tomoyuki,
Ueno Satoshi,
Fujimura Harutoshi,
Umekage Tadashi,
Yorifuji Shiro,
Matsuzawa Yuji,
Tarui Seiichiro
Publication year - 1992
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880150807
Subject(s) - transthyretin , polyneuropathy , amyloidosis , exon , medicine , amyloid (mycology) , amyloid polyneuropathy , cardiomyopathy , endocrinology , gene , genetics , age of onset , biology , pathology , disease , heart failure
A Japanese family is described in which 6 persons showed familial amyloid polyneuropathy (FAP). Mean ages of onset were 38 for 4 males and 54 for 2 females. Three of the 6 became emaciated and died after 4 to 10 years. In 5, muscular weakness and autonomic dysfunction were the initial symptoms followed by sensory disturbances. Amyloidotic cardiomyopathy was present in 3 of the subjects. Amyloid deposits showed an immunohistological relation to transthyretin (TTR). Analysis of 1 patient's TTR gene revealed a single base change (A→G) that led to amino acid substitution (Glu42→Gly). This base change produced a new restriction site for endonuclease Cfr13 l in exon 2. Polymorphic analysis of the length of the Cfr13 l‐restriction fragment confirmed the base change, and made it possible to detect the mutant TTR Gly42 gene in the FAP subjects. Amino acid sequencing analysis showed a variant of TTR Gly42 in 1 patient's serum. © 1992 John Wiley & Sons, Inc.