Rapid detection of wild-type and mutated transthyretins.
BACKGROUND
Familial amyloid polyneuropathy is caused by a variant transthyretin, which is a serum protein secreted by the liver. We previously reported that mutated transthyretins were detected in serum samples by surface-enhanced laser desorption/ionization time-of-flight mass spectrometry (SELDI-TOF MS). The aim of this study was to evaluate the clinical usefulness of SELDI-TOF MS for diagnosis of transthyretin-related amyloidosis.


METHODS
We used 106 serum samples obtained from patients who were clinically suspected of having amyloidosis between February 2011 and April 2014. SELDI-TOF MS allowed analysis for transthyretin via a 3-h one-step procedure.


RESULTS
Of the 106 patients, 51 are transthyretin amyloidosis. Mutated transthyretins were detected in serum samples from 30 of 51 patients with transthyretin amyloidosis. The results of genetic analysis showed that all of those patients had mutations in the transthyretin gene. For all 18 patients with senile systemic amyloidosis of 51 patients with transthyretin amyloidosis, SELDI-TOF MS detected only wild-type transthyretin peaks, not mutated transthyretin peaks.


CONCLUSIONS
SELDI-TOF MS is a clinically useful tool for diagnosis of transthyretin-related amyloidosis.
Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan Department of Morphological and Physiological Sciences, Graduate School of Health Sciences, Kumamoto University, Kumamoto, Japan.
Masayoshi
M
Tasaki
Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan mitt@rb3.so-net.ne.jp.
Mitsuharu
M
Ueda
Department of Morphological and Physiological Sciences, Graduate School of Health Sciences, Kumamoto University, Kumamoto, Japan.
Konen
K
Obayashi
Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan.
Hiroaki
H
Motokawa
Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan.
Yumiko
Y
Kinoshita
Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan.
Genki
G
Suenaga
Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan.
Akihiro
A
Yanagisawa
Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan.
Risa
R
Toyoshima
Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan.
Yohei
Y
Misumi
Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan.
Teruaki
T
Masuda
Diagnostic Unit for Amyloidosis, Department of Neurology, Kumamoto University Hospital, Kumamoto, Japan.
Taro
T
Yamashita
Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan.
Yukio
Y
Ando
D028227:Amyloid Neuropathies, Familial / Q000097:blood / Q000175:diagnosis* / Q000235:genetics; D004252:DNA Mutational Analysis / Q000379:methods*; D006801:Humans; D025202:Molecular Diagnostic Techniques; D020125:Mutation, Missense; D011228:Prealbumin / Q000235:genetics* / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D011228:Prealbumin
Familial amyloid polyneuropathy; senile systemic amyloidosis; surface-enhanced laser desorption/ionization time-of-flight mass spectrometry; transthyretin