Inhibitory effects of oroxylin A on endothelial protein C receptor shedding in vitro and in vivo
2
조회
0
다운로드
6
인용
0
참고문헌
키워드
초록
Endothelial cell protein C receptor (EPCR) plays important roles in blood coagulation and inflammation. EPCR activity ismarkedly changed by ectodomain cleavage and release as thesoluble EPCR. EPCR can be shed from the cell surface, whichis mediated by tumor necrosis factor-α converting enzyme(TACE). Oroxylin A (OroA), a major component of Scutellariabaicalensis Georgi, is known to exhibit anti-angiogenic, antiinflammation,and anti-invasive activities. However, little isknown about the effects of OroA on EPCR shedding. Datashowed that OroA induced potent inhibition of phorbol-12-myristate 13-acetate (PMA), tumor necrosis factor (TNF)-α,interleukin (IL)-1β and on cecal ligation and puncture (CLP)-induced EPCR shedding through suppression of TACE expressionand activity. In addition, treatment with OroA resulted inreduced PMA-stimulated phosphorylation of p38, extracellularregulated kinases (ERK) 1/2, and c-Jun N-terminal kinase (JNK). These results demonstrate the potential of OroA as ananti-sEPCR shedding reagent against PMA and CLP-mediated EPCR shedding.
Abstract
Endothelial cell protein C receptor (EPCR) plays important roles in blood coagulation and inflammation. EPCR activity ismarkedly changed by ectodomain cleavage and release as thesoluble EPCR. EPCR can be shed from the cell surface, whichis mediated by tumor necrosis factor-α converting enzyme(TACE). Oroxylin A (OroA), a major component of Scutellariabaicalensis Georgi, is known to exhibit anti-angiogenic, antiinflammation,and anti-invasive activities. However, little isknown about the effects of OroA on EPCR shedding. Datashowed that OroA induced potent inhibition of phorbol-12-myristate 13-acetate (PMA), tumor necrosis factor (TNF)-α,interleukin (IL)-1β and on cecal ligation and puncture (CLP)-induced EPCR shedding through suppression of TACE expressionand activity. In addition, treatment with OroA resulted inreduced PMA-stimulated phosphorylation of p38, extracellularregulated kinases (ERK) 1/2, and c-Jun N-terminal kinase (JNK). These results demonstrate the potential of OroA as ananti-sEPCR shedding reagent against PMA and CLP-mediated EPCR shedding.
참고문헌 (30)
- Fukudome, K., "Identification, cloning, and regulation of a novel endothelial cell protein C", activated protein C receptor, 1994, pp.269, 26486~26491
- Fukudome, K., "The endothelial cell protein C receptor. Cell surface expression and direct ligand binding by the soluble receptor", J. Biol. Chem, 271, pp.17491~17498 (1996)
- Mosnier, L. O., "The cytoprotective protein C pathway", Blood, 109, pp.3161~3172 (2007)
- Esmon, C. T., "Structure and functions of the endothelial cell protein C receptor", Crit. Care. Med, 32, pp.298~301 (2004)
- Wang, L., "Novel role of the human alveolar epithelium in regulating intra-alveolar coagulation", Am. J. Respir. Cell Mol. Biol, 36, pp.497~503 (2007)
- Xu, J., "Metalloproteolytic release of endothelial cell protein C receptor", J. Biol. Chem, 275, pp.6038~6044 (2000)
- Kurosawa, S., "Identification of functional endothelial protein C receptor in human plasma", J. Clin. Invest, 100, pp.411~418 (1997)
- Kurosawa, S., "Plasma levels of endothelial cell protein C receptor are elevated in patients with sepsis and systemic lupus erythematosus: lack of correlation with thrombomodulin suggests involvement of different pathological processes", Blood, 91, pp.725~727 (1998)
- Ghosh, S., "Endothelial cell protein C receptor acts as a cellular receptor for factor VIIa on endothelium", J. Biol. Chem, 282, pp.11849~11857 (2007)
- Lopez-Sagaseta, J., "Binding of factor VIIa to the endothelial cell protein C receptor reduces its coagulant activity", J. Thromb. Haemost, 5, pp.1817~1824 (2007)
- Menschikowski, M., "Regulation of endothelial protein C receptor shedding by cytokines is mediated through differential activation of MAP kinase signaling pathways", Exp. Cell Res, 315, pp.2673~2682 (2009)
- Han, H., "CADPE inhibits PMA-stimulated gastric carcinoma cell invasion and matrix metalloproteinase-9 expression by FAK", MEK, Mol. Cancer Res, pp.2010, 8[DOI]
- Leng, Y., "Effects of insulin, contraction, and phorbol esters on mitogen-activated protein kinase signaling in skeletal muscle from lean and ob", ob mice, 2004, pp.53, 1436~1444
- Huovila, A. P., "Shedding light on ADAM metalloproteinases", Trends. Biochem. Sci, 30, pp.413~422 (2005)
- Murphy, G., "The ADAMs: signalling scissors in the tumour microenvironment", Nat. Rev. Cancer, 8, pp.929~941 (2008)
- Li, C., "Pharmacological effects and pharmacokinetics properties of Radix Scutellariae and its bioactive flavones", Biopharm. Drug. Dispos, 32, pp.427~445 (2011)
- Li, H. N., "Apoptosis induction of oroxylin A in human cervical cancer HeLa cell line in vitro and in vivo", Toxicology, 257, pp.80~85 (2009)
- Lu, Z., "Oroxylin A inhibits matrix metalloproteinase-2", 9 expression and activation by up-regulating tissue inhibitor of metalloproteinase- 2 and suppressing the ERK1, Toxicol. Lett, pp.2012, 209[DOI]
- Sun, Y., "Oroxylin A suppresses invasion through down-regulating the expression of matrix metalloproteinase-2", 9 in MDA- MB-435 human breast cancer cells, 2009, pp.603, 22~28
- Tseng, T. L., "Oroxylin-A rescues LPS-induced acute lung injury via regulation of NF-kappaB signaling pathway in rodents", PLoS One, 7, pp.e47403~ (2012)
- Borgel, D., "A comparative study of the protein C pathway in septic and nonseptic patients with organ failure", Am. J. Respir. Crit. Care Med, 176, pp.878~885 (2007)
- Qu, D., "The Ser219- ->Gly dimorphism of the endothelial protein C receptor contributes to the higher soluble protein levels observed in individuals with the A3 haplotype", J. Thromb. Haemost, 4, pp.229~235 (2006)
- Qu, D., "Regulated endothelial protein C receptor shedding is mediated by tumor necrosis factor-alpha converting enzyme", ADAM17, 2007, pp.5, 395~402
- Buras, J. A., "Animal models of sepsis: setting the stage", Nat. Rev. Drug. Discov, 4, pp.854~865 (2005)
- Yang, H., "Reversing established sepsis with antagonists of endogenous high-mobility group box 1", Proc. Natl. Acad. Sci. U.S.A, 101, pp.296~301 (2004)
- Thalhamer, T., "MAPKs and their relevance to arthritis and inflammation", Rheumatology (Oxford), 47, pp.409~414 (2008)
- Bae, J. S, "Activated protein C inhibits high mobility group box 1 signaling in endothelial cells", Blood, 118, pp.3952~3959 (2011)
- Kim, D. C., "Vascular anti-inflammatory effects of curcumin on HMGB1-mediated responses in vitro", Inflamm. Res, 60, pp.1161~1168 (2011)
- Miller, M. A., "ADAM-10 and -17 regulate endometriotic cell migration via concerted ligand and receptor shedding feedback on kinase signaling", Proc. Natl. Acad. Sci. U.S.A, 110, pp.2074~2083 (2013)
- Wang, H., "Cholinergic agonists inhibit HMGB1 release and improve survival in experimental sepsis", Nat. Med, 10, pp.1216~1221 (2004)