A second transthyretin mutation at position 33 (Leu/Phe) associated with familial amyloidotic polyneuropathy.
Genomic DNA was isolated from peripheral blood lymphocytes of a patient with familial amyloidotic polyneuropathy (FAP) and the transthyretin (TTR) gene examined for sequence mutations. Polymerase chain reaction was used to asymmetrically amplify the TTR exons. Direct DNA sequencing of the PCR product revealed a C for T mutation at the first base of codon 33 located in exon 2 of one transthyretin gene. This resulted in a substitution of leucine for phenylalanine at position 33. Exons 3 and 4 were examined and found to be normal. The mutation creates a novel DdeI restriction site at the point of the mutation.
Department of Medicine, Boston University School of Medicine, MA 02118.
J
J
Harding
J
J
Skare
M
M
Skinner
D000686:Amyloidosis / Q000235:genetics*; D001483:Base Sequence; D005091:Exons / Q000235:genetics; D005260:Female; D009477:Hereditary Sensory and Autonomic Neuropathies / Q000235:genetics*; D006801:Humans; D008297:Male; D008875:Middle Aged; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D016133:Polymerase Chain Reaction; D011228:Prealbumin / Q000235:genetics*; D011487:Protein Conformation
D011228:Prealbumin