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
Dans Anglais
| WPRIM
| ID: wpr-59825
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.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Peptides
/
Protéines de fusion recombinantes
/
Transduction du signal
/
Lignée cellulaire
/
Lipopolysaccharides
/
Facteur de transcription NF-kappa B
/
Mercaptamine
/
Activation enzymatique
/
Phosphohydrolase PTEN
/
Cyclooxygenase 2
Limites du sujet:
Animaux
/
Humains
langue:
Anglais
Texte intégral:
Experimental & Molecular Medicine
Année:
2008
Type:
Article
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