Inhibition of Trypsin-Induced Mast Cell Activation by Water Fraction of Lonicera japonica

  • Kang, Ok-Hwa (Department of Oriental Pharmacy, College of Pharmacy, Wonkwang University) ;
  • Choi, Yeon-A (Department of Oriental Pharmacy, College of Pharmacy, Wonkwang University) ;
  • Park, Hye-Jung (Department of Oriental Pharmacy, College of Pharmacy, Wonkwang University) ;
  • Lee, Joo-Young (Department of Oriental Pharmacy, College of Pharmacy, Wonkwang University) ;
  • Kim, Dae-Ki (Department of Oriental Pharmacy, College of Pharmacy) ;
  • Choi, Suck-Chei ( Wonkwang University) ;
  • Kim, Tae-Hyun (Department of Oriental Pharmacy, College of Pharmacy) ;
  • Nah, Yong-Ho ( Wonkwang University) ;
  • Yun, Ki-Jung (Department of Immunology, Chonbuk National University Medical School) ;
  • Choi, Suck-Jun (Institute of Digestive Disease, Wonkwang University School of Medicine) ;
  • Kim, Young-Ho (College of Pharmacy, Chungnam National University) ;
  • Bae, Ki-Hwan (College of Pharmacy, Chungnam National University) ;
  • Lee, Young-Ml (Department of Oriental Pharmacy, College of Pharmacy, Wonkwang University)
  • Published : 2004.11.01

Abstract

Lonicera japonica Thunb.(Caprifoliaceae) has long been known as an anti-inflammatory. In the present study, the effect of water fraction of Lonicera japonica (LJ) on trypsin-induced mast cell activation was examined. HMC-1 cells were stimulated with trypsin (100 nM) in the presence or absence of LJ (10, 100, and 1000 $\mu$ g/mL). TNF-$\alpha$ and tryptase production were measured by enzyme-linked immunosorbent assay (ELISA) and reverse transcription-PCR. Extracellular signal-regulated kinase (ERK) phosphorylation was assessed by Western blot. Trypsin activity was measured by using Bz-DL-Arg-p-nitroanilide (BAPNA) as substrate. LJ (10, 100, and 1000 $\mu$g/mL) inhibited TNF-$\alpha$ secretion in a dose-dependent manner. LJ (10, 100, and 1000 $\mu$g/mL) also inhibited TNF-$\alpha$ and tryptase mRNA expression in trypsin-stimulated HMC-1. Furthermore, LJ inhibited trypsin-induced ERK phosphorylation. However, LJ did not affect the trypsin activity even 1000 $\mu$g/mL. These results indicate that LJ may inhibit trypsin-induced mast cell activation through the inhibition of ERK phosphorylation than the inhibition of trypsin activity.

Keywords

References

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