Oxidative stress is found in amyloid deposits in systemic amyloidosis

被引:119
作者
Ando, Y
Nyhlin, N
Suhr, O
Holmgren, G
Uchida, K
ElSahly, M
Yamashita, T
Terasaki, H
Nakamura, M
Uchino, M
Ando, M
机构
[1] KUMAMOTO UNIV,SCH MED,DEPT INTERNAL MED 1,KUMAMOTO 860,JAPAN
[2] KUMAMOTO UNIV,SCH MED,DEPT NEUROL,KUMAMOTO 860,JAPAN
[3] NAGOYA UNIV,SCH AGR,LAB FOOD BIODYNAM,CHIKUSA KU,NAGOYA,AICHI 46401,JAPAN
[4] UMEA UNIV HOSP,DEPT INTERNAL MED,S-90185 UMEA,SWEDEN
[5] UMEA UNIV HOSP,DEPT CLIN GENET,S-90185 UMEA,SWEDEN
关键词
D O I
10.1006/bbrc.1996.5997
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
Oxidative stress in human amyloid deposits from patients with systemic amyloidosis, such as familial amyloidotic polyneuropathy (FAP), primary amyloidosis, and secondary amyloidosis, was examined immunohistochemically by means of an affinity purified anti-hydroxynonenal (HNE) antibody to HNE, a marker of lipid peroxidation. Furthermore, the levels of thiobarbituric acid reactive substances (TBARS), which is another marker of lipid peroxidation, and the levels of protein carbonyl, a maker of protein modifications by free radicals, were determined in FAP patients and healthy controls. Affinity purified anti-HNE antibody reacted with amyloid deposits in all types of amyloid tissues examined, Significantly higher levels of TBARS and protein carbonyl were found in amyloid rich tissues of FAP patients compared with those in the control subjects. These results verify that lipid peroxidation via free radical injury occurs in amyloid deposits in systemic amyloidosis. The protein modifying properties of free radicals increase the likelihood that they play an important role in the amyloid formation process. (C) 1997 Academic Press.
引用
收藏
页码:497 / 502
页数:6
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