SHIMIZU Yuko    Department   School of Medicine(Tokyo Women's Medical University Hospital), School of Medicine    Position   Professor
Article types	Original article
Language	English
Peer review	Peer reviewed
Title	Biochemical characteristics of variant transthretins causing hereditary leptomeningeal amyloidosis
Journal	Formal name：Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis Abbreviation：Amyloid ISSN code：13506129/17442818
Domestic / Foregin	Foregin
Volume, Issue, Page	12(4),pp.1-10
Author and coauthor	Mitsuhashu S, Yazaki M, Tokuda T, Sekijima Y, Washimi Y, Shimizu Y, Ando Y, Benson MD, Ikeda S.
Publication date	2005/12
Summary	Transthyretin (TTR) is a tetrameric protein that can dissociate into amyloidogenic monomers and cause TTR-related amyloidosis. A rare phenotype, called hereditary leptomeningeal TTR amyloidosis, in which TTR amyloid deposition occurs mainly in leptomeninges and subarachnoid vessels, has been reported in patients with several different TTR variants. In the present study, we examined TTR variants immunoprecipitated from the serum and cerebrospinal fluid (CSF) of patients with hereditary leptomeningeal TTR amyloidosis using matrix-assisted laser desorption ionization/time-of-flight mass spectrometry (IP-Mass method). The leptomeningeal-type TTR variants were not detected in the serum but were found at low levels in the CSF. The undetectable levels of the leptomeningeal-type TTR variants in serum could explain the minute amounts of systemic deposition of these variants. The relatively high level of unstable TTR variants in CSF, probably due to increased secretion from the choroid plexus, is considered to be the pathogenesis of the leptomeningeal-type of TTR amyloidosis.
DOI	10.1080/13506120500352404
PMID	16399646