Detection of different forms of variant transthyretin (Met30) in cerebrospinal fluid

被引:29
作者
Ando, Y
Suhr, O
Yamashita, T
Ohlsson, PI
Holmgren, G
Obayashi, K
Terazaki, H
Mambule, C
Uchino, M
Ando, M
机构
[1] Umea Univ, Dept Med, S-90185 Umea, Sweden
[2] Kumamoto Univ, Sch Med, Dept Internal Med 1, Kumamoto 860, Japan
[3] Umea Univ, Dept Med Biochem & Biophys, S-90187 Umea, Sweden
[4] Umea Univ, Dept Clin Genet, S-90185 Umea, Sweden
[5] Kumamoto Univ, Sch Med, Dept Neurol, Kumamoto 860, Japan
关键词
familial amyloidotic polyneuropathy; cerebrospinal fluid; mass spectrometry; transthyretin; variant TTR; amyloidosis;
D O I
10.1016/S0304-3940(97)00868-9
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
To detect the variant transthyretin (TTR; Met30) in cerebrospinal fluid (CSF) of familiar amyloidotic polyneuropathy (FAP) patients, we have applied a new method using a centrifugal concentrator device and electrospray ionization mass spectrometry (ESI-MS). Only 100 mu l of CSF and 30 mu l of the antibody for TTR was needed for the analysis. After preparation of the samples with anti-TTR antibody, they were passed through a 1000 kDa cut-off centrifugal concentrator which retained the antibody. By analyzing the obtained filtrate with ESI-MS, three predominant forms of normal and their variant forms of TTR were detected in CSF samples. TTR (Met30), with a molecular weight 32.0 Da higher than the normal form of TTR, was found in all FAP patients' materials. Although the ratio of the three major peaks of TTR were different in each individual, they were always found in CSF and sera. This method will contribute to make a diagnosis of neurologic disorders having a mutant protein in CSF as well as serum. (C) 1997 Elsevier Science Ireland Ltd.
引用
收藏
页码:123 / 126
页数:4
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