Inhibition of LPS-induced cyclooxygenase 2 and nitric oxide production by transduced PEP-1-PTEN fusion protein in Raw 264.7 macrophage cells
Experimental & Molecular Medicine
; : 629-638, 2008.
Article
ي En
| WPRIM
| ID: wpr-59825
المكتبة المسؤولة:
WPRO
ABSTRACT
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-kappa B induced by LPS. These results suggest that the PEP-1-PTEN fusion protein can be used in protein therapy for inflammatory disorders.
Key words
النص الكامل:
1
الفهرس:
WPRIM
الموضوع الرئيسي:
Peptides
/
Recombinant Fusion Proteins
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Signal Transduction
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Cell Line
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Lipopolysaccharides
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NF-kappa B
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Cysteamine
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Enzyme Activation
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PTEN Phosphohydrolase
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Cyclooxygenase 2
المحددات:
Animals
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Humans
اللغة:
En
مجلة:
Experimental & Molecular Medicine
السنة:
2008
نوع:
Article