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KMID : 0624620090420050286
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BMB Reports
2009 Volume.42 No. 5 p.286 ~ p.292
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Inhibition of LPS-induced nitric oxide production by transduced Tat-arginine deiminase fusion protein in Raw 264.7 cells
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Lee Min-Jung
Kim Dae-Won
Lee Yeom-Pyo
Jeong Hoon-Jae
Kang Hye-Won
Shin Min-Jae
Sohn Eun-Jeong
Kim Mi-Jin
Jang Sang-Ho
Kang Tae-Cheon
Won Moo-Ho
Min Bon-Hong
Cho Sung-Woo
Lee Kil-Soo
Park Jin-Seu
Eum Won-Sik
Choi Soo-Young
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Abstract
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Arginine deiminase (ADI), an arginine-degrading enzyme, has anti-proliferative and anti-tumor activities and is capable of inhibiting the production of nitric oxide (NO). Modulation of nitric oxide (NO) production is considered a promising approach for the treatment of various diseases including cancer, inflammation and neuronal disorders. In this study, an ADI gene was fused with an HIV-1 Tat peptide in a bacterial expression vector to produce an genetic in-frame Tat-ADI fusion protein. When added exogenously to the culture media, the expressed and purified Tat-ADI fusion proteins were efficiently transduced into macrophage Raw 264.7 cells in a time- and dosedependent manner. Furthermore, transduced Tat-ADI fusion proteins markedly increased cell viability in cells treated with lipopolysaccharide (LPS). This increase in viability was mediated by an inhibition of NO production. These results suggest that this Tat-ADI fusion protein can be used in protein therapies of NO-related disorders such as cancer, inflammation and neuronal diseases.
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KEYWORD
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Arginine deiminase (ADI), HIV-1 Tat peptide, Inflammation, Nitric oxide synthase, Protein transduction
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