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KMID : 0620920080400060629
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Experimental & Molecular Medicine
2008 Volume.40 No. 6 p.629 ~ p.638
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Inhibition of LPS-induced cyclooxygenase 2 and nitric oxide production by transduced PEP-1-PTEN fusion protein in Raw 264.7 macrophage cells
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Lee Sun-Hwa
Choi Soo-Young
Kwon Hyung-Joo
Park Jin-Seu
Kim Dae-Won
Kim So-Young
Jang Sang-Ho
Cho Sung-Woo
Eum Won-Sik
Kim Yeon-Hyang
Lee Yeom-Pyo
Lee Min-Jung
Jeong Min-Seop
Kang Hye-Won
Jeong Hoon-Jae
Sohn Eun-Joung
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Abstract
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Phosphatase and tensin homologue deleted on chromosome 10 (PTEN) is a tumor suppressor. Although it is well known to have various physiological roles in cancer, its inhibitory effect on inflammation remains poorly understood. In the present study, a human PTEN gene was fused with PEP-1 peptide in a bacterial expression vector to produce a genetic in-frame PEP-1-PTEN fusion protein. The expressed and purified PEP-1-PTEN fusion protein were transduced efficiently into macrophage Raw 264.7 cells in a time- and dose- dependent manner when added exogenously in culture media. Once inside the cells, the transduced PEP-1-PTEN protein was stable for 24 h. Transduced PEP-1-PTEN fusion protein inhibited the LPS-induced cyclooxygenase 2 (COX-2) and iNOS expression levels in a dose-dependent manner. Furthermore, transduced PEP-1-PTEN fusion protein inhibited the activation of NF-?B induced by LPS. These results suggest that the PEP-1-PTEN fusion protein can be used in protein therapy for inflammatory disorders.
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KEYWORD
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cyclooxygenase 2, inflammation, lipopolysaccharides, nitric oxide, PTEN phosphohydrolase
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