Journal of Acupuncture Research
- 제22권2호
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- Pages.123-132
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- 2005
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- 2586-288X(pISSN)
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- 2586-2898(eISSN)
The Study of $NF-{\kappa}B(P50)$ Suppression mechanism with main Component of Bee Venom and Melittin on Human Synoviocyte
- Kwon, Soon-Jung (College of Traditional Korean Medicine, Kyung Won University) ;
- Song, Ho-Sueb (College of Traditional Korean Medicine, Kyung Won University)
- 발행 : 2005.04.20
초록
Melittin,cationic 26-amino acid, is the principal component of the bee venom (BV) which has been used for treatment of inflammatory disease such as arthritis rheumatism NF-kB is activated by subsequent release of inhibitory IkB via activation of a multisubunit IkB kinase (IKK). We previously found that melittin bind to the sulfhydryl group of p50, a subunit of NF-kB. Since sulfhydryl group is present in kinase domain of IKKa and IKKb, melittin could modify IKK activity by protein-protein interaction. We therefore examined effect of melittin on IKK activities in sodium nitroprusside (SNP)-stimulated synoviocyte obtained from RA patients. Melittin suppressed the SNP-induced release of IkB resulted in inhibition of DNA binding activity of NF-kB and NF-kB-dependent luciferase activity. Consistent with the inhibitory effect on NF-kB activation, IKKa and IKKb activities were also suppressed by melittin. Surface plasmon resonance analysis realized that melitin binds to IKKa