Instability of expressed Cu/Zn superoxide dismutase with 2 bp deletion found in familial amyotrophic lateral sclerosis

FEBS Letters

Ohama, Eisaku²  Watanabe, Yasuhiro¹  Nanba, Eiji³  Nakashima, Kenji¹  Kono, Yasuhisa⁴ 

[1]Division of Neurology, Institute of Neurological Sciences, Faculty of Medicine, Tottori University, 36-1 Nishimachi, Yonago 683, Japan

[2]Division of Neuropathology, Institute of Neurological Sciences, Faculty of Medicine, Tottori University, 36-1 Nishimachi, Yonago 683, Japan

[3]Gene Research Center, Tottori University, 36-1 Nishimachi, Yonago 683, Japan

[4]Department of Life Science and Biotechnology, Faculty of Life and Environmental Science, Shimane University, Matsue 690, Japan

关键词: Cu/Zn superoxide dismutase;    Familial amyotrophic lateral sclerosis;    Two basepair deletion;    Expression system;    Copper ion;    Hydroxyl radical;    FALS;    familial amyotrophic lateral sclerosis;    SOD1;    Cu/Zn superoxide dismutase;    RT;    reverse transcription;    PCR;    polymerase chain reaction;    SSCP;    single strand conformational polymorphism;    MBP;    maltose binding protein;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(96)01362-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The mutant Cu/Zn superoxide dismutase (SOD1) associated with familial amyotrophic lateral sclerosis (FALS) with a 2 bp deletion was produced in two protein expression systems. The mutant SOD1, expressed as a fusion protein in E. coli, had immunoreactivity to an anti-human SOD1 antibody but no SOD activity. It was more susceptible to proteolysis and its immunoreactivity decreased more rapidly than the wild type. The mutant SOD1, expressed in Cos1 cells, was not detected by either SOD activity staining or Western blot analysis, although expression of its mRNA was confirmed. These results suggest that the mutant SOD1 is seriously unstable in mammalian cells.

【 授权许可】

Unknown