Inhibitory effects of lysozyme on endothelial protein C receptor shedding in vitro and in vivo
2
조회
0
다운로드
5
인용
0
참고문헌
키워드
초록
Lysozyme protects us from the ever-present danger of bacterial infection and binds to bacterial lipopolysaccharide (LPS) with high affinity. Beyond its role in the activation of protein C, the endothelial cell protein C receptor (EPCR) plays an important role in the cytoprotective pathway. EPCR can be shed from the cell surface, which is mediated by tumor necrosis factor-α converting enzyme (TACE). However, little is known about the effects of lysozyme on EPCR shedding. We investigated this issue by monitoring the effects of lysozyme on phorbol- 12-myristate 13-acetate (PMA)-, tumor necrosis factor (TNF)-α-, interleukin (IL)-1β-, and cecal ligation and puncture (CLP)-mediated EPCR shedding and underlying mechanism. Data demonstrate that lysozyme induced potent inhibition of PMA-, TNF-α-, IL-1β-, and CLP-induced EPCR shedding. Lysozyme also inhibited the expression and activity of PMA-induced TACE in endothelial cells. These results demonstrate the potential of lysozyme as an anti-EPCR shedding reagent against PMA-mediated and CLP-mediated EPCR shedding.
Abstract
Lysozyme protects us from the ever-present danger of bacterial infection and binds to bacterial lipopolysaccharide (LPS) with high affinity. Beyond its role in the activation of protein C, the endothelial cell protein C receptor (EPCR) plays an important role in the cytoprotective pathway. EPCR can be shed from the cell surface, which is mediated by tumor necrosis factor-α converting enzyme (TACE). However, little is known about the effects of lysozyme on EPCR shedding. We investigated this issue by monitoring the effects of lysozyme on phorbol- 12-myristate 13-acetate (PMA)-, tumor necrosis factor (TNF)-α-, interleukin (IL)-1β-, and cecal ligation and puncture (CLP)-mediated EPCR shedding and underlying mechanism. Data demonstrate that lysozyme induced potent inhibition of PMA-, TNF-α-, IL-1β-, and CLP-induced EPCR shedding. Lysozyme also inhibited the expression and activity of PMA-induced TACE in endothelial cells. These results demonstrate the potential of lysozyme as an anti-EPCR shedding reagent against PMA-mediated and CLP-mediated EPCR shedding.
참고문헌 (35)
- Esmon CT, "The endothelial protein C receptor", Curr Opin Hematol, 13, pp.382~385 (2006)
- Fukudome K, "Identification, cloning, and regulation of a novel endothelial cell protein C", activated protein C receptor, 1994, pp.269, 26486~26491
- Stearns-Kurosawa DJ, "The endothelial cell protein C receptor augments protein C activation by the thrombin-thrombomodulin complex", Proc Natl Acad Sci U S A, 93, pp.10212~10216 (1996)
- Mosnier LO, "The cytoprotective protein C pathway", Blood, 109, pp.3161~3172 (2007)
- Xu J, "Metalloproteolytic release of endothelial cell protein C receptor", J Biol Chem, 275, pp.6038~6044 (2000)
- 이원화, "RESEARCH ARTICLE Emodin-6-O-b-D-glucoside down-regulates endothelial protein C receptor shedding", Archives of Pharmacal Research, 36(9), pp.1160~1165 (2013), 대한약학회
- Kurosawa S, "Identification of functional endothelial protein C receptor in human plasma", J Clin Invest, 100, pp.411~418 (1997)
- Liaw PC, "Mechanisms by which soluble endothelial cell protein C receptor modulates protein C and activated protein C function", J Biol Chem, 275, pp.5447~5452 (2000)
- 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)
- 구세광, "Inhibitory effects of oroxylin A on endothelial protein C receptor shedding in vitro and in vivo", BMB Reports, 47(6), pp.336~341 (2014), 생화학분자생물학회
- 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 AP, "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)
- Kelly JA, "X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme", Nature, 282, pp.875~878 (1979)
- Clingolani R, "Bioinspired approaches for human-centric technologies" (2014), Springer
- Nakimbugwe D, "Cell wall substrate specificity of six different lysozymes and lysozyme inhibitory activity of bacterial extracts", FEMS Microbiol Lett, 259, pp.41~46 (2006)
- 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
- Michie HR, "Detection of circulating tumor necrosis factor after endotoxin administration", N Engl J Med, 318, pp.1481~1486 (1988)
- Kremer JP, "Interleukin-1, -6 and tumor necrosis factor-alpha release is down-regulated in whole blood from septic patients", Acta Haematol, 95, pp.268~273 (1996)
- Buras JA, "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)
- Bae JS, "Transforming Growth Factor beta-induced Protein Promotes Severe Vascular Inflammatory Responses", Am J Respir Crit Care Med, 189, pp.779~786 (2014)
- Diehl KH, "A good practice guide to the administration of substances and removal of blood, including routes and volumes", J Appl Toxicol, 21, pp.15~23 (2001)
- Weiler H, "Multiple receptor-mediated functions of activated protein C", Hamostaseologie, 31, pp.185~195 (2011)
- Wang L, "The coagulation cascade in sepsis", Curr Pharm Des, 14, pp.1860~1869 (2008)
- Sugo T, "Activation of prothrombin by factor Xa bound to the membrane surface of human umbilical vein endothelial cells: its catalytic efficiency is similar to that of prothrombinase complex on platelets", J Biochem, 117, pp.244~250 (1995)
- Thalhamer T, "MAPKs and their relevance to arthritis and inflammation", Rheumatology (Oxford), 47, pp.409~414 (2008)
- 구세광, "Antithrombotic activities of sulforaphane via inhibiting platelet aggregation and FIIa", FXa, 2014, pp.37(11), 1454~1463[DOI]
- Miller MA, "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)
- Bae JS, "Antithrombotic and profibrinolytic activities of phloroglucinol", Food Chem Toxicol, 49, pp.1572~1577 (2011)
- Kim TH, "Antithrombotic and profibrinolytic activities of eckol and dieckol", J Cell Biochem, 113, pp.2877~2883 (2012)