RETRACTED: Enhanced transduction of Cu,Zn-superoxide dismutase with HIV-1 Tat protein transduction domains at both termini (Retracted Article)

被引:0
|
作者
Eum, WS
Jang, SH
Kim, DW
Choi, HS
Choi, SH
Kim, SY
An, JJ
Lee, SH
Han, K
Kang, JH
Kang, TC
Won, MH
Cho, YJ
Choi, JH
Kim, TY
Park, J [1 ]
Choi, SY
机构
[1] Hallym Univ, Dept Genet Engn, Chunchon 200702, South Korea
[2] Hallym Univ, Res Inst Biosci & Biotechnol, Chunchon 200702, South Korea
[3] Cheongju Univ, Dept Genet Engn, Cheongju, South Korea
[4] Hallym Univ, Coll Med, Dept Anat, Chunchon 200702, South Korea
[5] Hallym Univ, Coll Med, Dept Neurosurg, Chunchon 200702, South Korea
[6] Res Lab Cell Tech, Chunchon 200702, South Korea
[7] Catholic Univ, Coll Med, Dept Dermatol, Seoul 137040, South Korea
关键词
anti-oxidant enzyme; HIV-1; Tat; protein therapy; protein transduction; Tat-SOD-Tat;
D O I
暂无
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 human immunodeficiency virus type 1 (HIV-1) Tat protein transduction domain (PTD) is responsible for highly efficient protein transduction across plasma membranes. In a previous study, we showed that Tat-Cu,Zn-superoxide dismutase (Tat-SOD) can be directly transduced into mammalian cells across the lipid membrane barrier. In this study, we fused the human SOD gene with a Tat PTD transduction vector at its N- and/or C-terminus. The fusion proteins (Tat-SOD, SOD-Tat, Tat-SOD-Tat) were purified from Escherichia coli and their ability to enter cells in vitro and in vivo compared by Western blotting and immunohistochemistry. The transduction efficiencies and biological activities of the SOD fusion protein with the Tat PTD at either terminus were equivalent and lower than the fusion protein with the Tat PTD at both termini. The availability of a more efficient SOD fusion protein provides a powerful vehicle for therapy in human diseases related to this anti-oxidant enzyme and to reactive oxygen species.
引用
收藏
页码:191 / 197
页数:7
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