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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Inhibitory effects of oroxylin A on endothelial protein C receptor shedding in vitro and in vivo

  • Ku, Sae-Kwang (Department of Anatomy and Histology, College of Oriental Medicine, Daegu Haany University) ;
  • Han, Min-Su (Laboratory for Arthritis and Bone Biology, Fatima Research Institute, Daegu Fatima Hospital) ;
  • Lee, Min Young (College of Pharmacy, CMRI, Research Institute of Pharmaceutical Sciences, Kyungpook National University) ;
  • Lee, You-Mie (College of Pharmacy, CMRI, Research Institute of Pharmaceutical Sciences, Kyungpook National University) ;
  • Bae, Jong-Sup (College of Pharmacy, CMRI, Research Institute of Pharmaceutical Sciences, Kyungpook National University)
  • Received : 2013.09.02
  • Accepted : 2013.10.04
  • Published : 2014.06.30
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Abstract

Endothelial cell protein C receptor (EPCR) plays important roles in blood coagulation and inflammation. EPCR activity is markedly changed by ectodomain cleavage and release as the soluble EPCR. EPCR can be shed from the cell surface, which is mediated by tumor necrosis factor-${\alpha}$ converting enzyme (TACE). Oroxylin A (OroA), a major component of Scutellaria baicalensis Georgi, is known to exhibit anti-angiogenic, antiinflammation, and anti-invasive activities. However, little is known about the effects of OroA on EPCR shedding. Data showed that OroA induced potent inhibition of phorbol-12-myristate 13-acetate (PMA), tumor necrosis factor (TNF)-${\alpha}$, interleukin (IL)-$1{\beta}$ and on cecal ligation and puncture (CLP)-induced EPCR shedding through suppression of TACE expression and activity. In addition, treatment with OroA resulted in reduced PMA-stimulated phosphorylation of p38, extracellular regulated kinases (ERK) 1/2, and c-Jun N-terminal kinase (JNK). These results demonstrate the potential of OroA as an anti-sEPCR shedding reagent against PMA and CLP-mediated EPCR shedding.

Keywords

References

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