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Rapid detection of wild-type and mutated transthyretins.

Authors :: Tasaki M
Ueda M
Obayashi K
Motokawa H
Kinoshita Y
Suenaga G
Yanagisawa A
Toyoshima R
Misumi Y
Masuda T
Yamashita T
Ando Y
Source :: Annals of clinical biochemistry [Ann Clin Biochem] 2016 Jul; Vol. 53 (Pt 4), pp. 508-10. Date of Electronic Publication: 2015 Sep 04.
Publication Year :: 2016
Abstract: 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.<br />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.<br />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.<br />Conclusion: SELDI-TOF MS is a clinically useful tool for diagnosis of transthyretin-related amyloidosis.<br /> (© The Author(s) 2015.)