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A new transthyretin variant from a patient with familial amyloidotic polyneuropathy has asparagine substituted for histidine at position 90
Author(s) -
Skare James C.,
Milunsky Jeffrey M.,
Milunsky Aubrey,
Skare Ilze B.,
Cohen Alan S.,
Skinner Martha
Publication year - 1991
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.1399-0004.1991.tb02979.x
Subject(s) - transthyretin , asparagine , polyneuropathy , histidine , exon , chemistry , amyloidosis , mutation , cleavage (geology) , biochemistry , microbiology and biotechnology , amino acid , biology , medicine , gene , paleontology , fracture (geology)
A new transthyretin variant which lost an Sph I cleavage site within exon 3 has been characterized. A 260 bp sequence containing exon 3 was amplified using the polymerase chain reaction, and the variant was found to possess a Bsm I cleavage site not present in normal transthyretin. This led to the conclusion that the histidine at position 90 was replaced by asparagine, and amino acid analysis supported the conclusion. The discovery of this mutation suggests that intermolecular binding between hydrophobic polypeptide loops on the surface of transthyretin can lead to familial amyloidotic polyneuropathy.