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An aggressive form of familial amyloid polyneuropathy caused by a Glu54Gly mutation in the transthyretin gene
Author(s) -
Kim H. S.,
Kim S.M.,
Kang S.W.,
Jung S.C.,
Lee K.S.,
Kim T.S.,
Choi Y.C.
Publication year - 2005
Publication title -
european journal of neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.881
H-Index - 124
eISSN - 1468-1331
pISSN - 1351-5101
DOI - 10.1111/j.1468-1331.2005.01005.x
Subject(s) - transthyretin , mutation , medicine , amyloid polyneuropathy , amyloid (mycology) , polyneuropathy , compound heterozygosity , mutant , heterozygote advantage , gene , substitution (logic) , genetics , amyloidosis , gene mutation , endocrinology , age of onset , pathology , allele , biology , disease , computer science , programming language
We report a patient with familial amyloid polyneuropathy. Gene analysis revealed a heterozygous Glu54Gly substitution (A‐to‐G change) in the transthyretin gene. This is the first case of a Glu54Gly substitution that was devoid of a Gly6Ser substitution. Compared with the previously reported case with compound heterozygotes of Glu54Gly and Gly6Ser, the age of onset in our case is much younger and another characteristic findings were the amyloid vasculopathy and the multiple organ involvement. A Glu54Gly mutation is amyloidogenic by itself and a Gly6Ser mutation may offer some protection from the Glu54Gly mutant.