Familial carpal tunnel syndrome due to amyloidogenic transthyretin His 114 variant.
We studied two patients from a Japanese family with carpal tunnel syndrome (CTS). The biopsy samples obtained during CTS surgical release revealed deposits of amyloid that stained with antihuman transthyretin (TTR) antiserum. Single-strand conformation polymorphism analysis and sequence analysis of polymerase chain reaction (PCR)-amplified exons of the proband's TTR gene revealed a point mutation resulting in a substitution of histidine for tyrosine at position 114. The mutation was confirmed by PCR-primer-induced restriction analysis. Our findings account for clinical heterogeneity of TTR-derived amyloidosis, and suggest the importance of substitution itself for deposits of amyloid in CTS.
Murakami
T
T
First Department of Internal Medicine, Kumamoto University School of Medicine, Japan.
Tachibana
S
S
Endo
Y
Y
Kawai
R
R
Hara
M
M
Tanase
S
S
Ando
M
M
D000368:Aged; D000595:Amino Acid Sequence; D000682:Amyloid / Q000032:analysis / Q000096:biosynthesis*; D001483:Base Sequence; D002349:Carpal Tunnel Syndrome / Q000235:genetics* / Q000601:surgery; D004247:DNA / Q000737:chemistry; D017931:DNA Primers; D005091:Exons; D005260:Female; D014644:Genetic Variation; D006639:Histidine; D006801:Humans; D007564:Japan; D008297:Male; D008969:Molecular Sequence Data; D017354:Point Mutation; D016133:Polymerase Chain Reaction; D011110:Polymorphism, Genetic; D011228:Prealbumin / Q000235:genetics*; D015183:Restriction Mapping; D014443:Tyrosine
D000682:Amyloid; D017931:DNA Primers; D011228:Prealbumin; D014443:Tyrosine; D006639:Histidine; D004247:DNA