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Two transthyretin mutations (glu42gly, his90asn) in an Italian family with amyloidosis
Author(s) -
Skare James,
Junes Lee Anna,
Myles Noelle,
Kane Kelly,
Milunsky Aubrey,
Cohen Alan,
Skinner Martha
Publication year - 1994
Publication title -
clinical genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 102
eISSN - 1399-0004
pISSN - 0009-9163
DOI - 10.1111/j.1399-0004.1994.tb04030.x
Subject(s) - transthyretin , polyneuropathy , amyloidosis , mutation , asparagine , medicine , genetics , histidine , gene , biology , amino acid
A family with familial amyloidotic polyneuropathy (FAP) was previously found to have a substitution of asparagine for histidine at position 90 of transthyretin. Members with his90asn developed FAP. However, close examination of the transthyretin gene revealed that glu42gly is coinheri‐ted with his90asn in this family. Since glu42gly has already been seen in Japanese FAP patients, and his90asn has been found in Portuguese and German individuals without FAP, we conclude that his90asn is a nonpathogenic variant.