Analysis of transthyretin amyloid fibrils from vitreous samples in familial amyloidotic polyneuropathy (Val30Met)

被引：25

作者：

Ando, Y

Ando, E

Ohlsson, PI

Olofsson, A

Sandgren, O

Suhr, O

Terazaki, H

Obayashi, K

Lundgren, E

Ando, M

Negi, A

机构：

[1] Kumamoto Univ, Sch Med, Dept Internal Med 1, Kumamoto 860, Japan

[2] Umea Univ, Dept Internal Med, S-90185 Umea, Sweden

[3] Umea Univ, Dept Med Biochem & Biophys, S-90187 Umea, Sweden

[4] Umea Univ, Dept Appl Cell & Mol Biol, S-90187 Umea, Sweden

[5] Umea Univ, Dept Ophthalmol, S-90187 Umea, Sweden

[6] Kumamoto Univ, Sch Med, Dept Ophthalmol, Kumamoto 860, Japan

来源：

AMYLOID-INTERNATIONAL JOURNAL OF EXPERIMENTAL AND CLINICAL INVESTIGATION | 1999年 / 6卷 / 02期

关键词：

FAP; transthyretin; amyloid; amyloidosis; mass spectrometry; variant TTR;

D O I：

10.3109/13506129909007312

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The aim of the present study was to analyze the forms of wild type and mutated monomeric transthyretin (Val30Met) in the amyloid fibrils of patients with familial amyloidotic polyneuropathy by electrospray ionization mass spectrometry (ESI-MS). The solubility of amyloid fibrils from the vitrectomized samples was examined to determine the appropriate solution for ESI-MS. ESI-MS analysis revealed that heterozygotic Val30Met amyloid fibrils contained 14.6 +/- 7.5 % normal TTR. In all samples, 3 different types of variant ATTR could be identified: Full length ATTR, and -57, and -157 (or 156) Da from ATTR Val30Met were found. The two peaks showing -57, and -157 (or 156) Da from ATTR Val30Met corresponded to the -Gly, and -Gly-Pro sequences of ATTR Val30Met from the N-terminal. The results illustrate the heterogeneity of ATTR amyloid deposits and this method may be very useful for analyzing amyloid fibrils in ATTR related amyloidosis.

引用

页码：119 / 123

页数：5

共 10 条

[1] A new simple and rapid screening method for variant transthyretin-related amyloidosis [J].