シミズ　ユウコ   Shimizu Yuuko   清水　優子    所属   医学部 医学科（東京女子医科大学病院）    職種   教授
論文種別	原著
言語種別	英語
査読の有無	査読あり
表題	Biochemical characteristics of variant transthretins causing hereditary leptomeningeal amyloidosis
掲載誌名	正式名：Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis 略　 称：Amyloid ISSNコード：13506129/17442818
掲載区分	国外
巻・号・頁	12(4),pp.1-10
著者・共著者	Mitsuhashu S, Yazaki M, Tokuda T, Sekijima Y, Washimi Y, Shimizu Y, Ando Y, Benson MD, Ikeda S.
発行年月	2005/12
概要	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