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Volumn 7, Issue 8, 2012, Pages

PR3 and Elastase Alter PAR1 Signaling and Trigger vWF Release via a Calcium-Independent Mechanism from Glomerular Endothelial Cells

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; ELASTASE; MYELOBLASTIN; PROTEINASE ACTIVATED RECEPTOR 1; PROTEINASE ACTIVATED RECEPTOR 2; PROTEINASE ACTIVATED RECEPTOR 3; SMALL INTERFERING RNA; THROMBIN; TRYPSIN; VON WILLEBRAND FACTOR;

EID: 84865584004     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0043916     Document Type: Article
Times cited : (14)

References (59)
  • 2
    • 0028117197 scopus 로고
    • Elevations of neutrophil proteinase 3 in serum of patients with Wegener's granulomatosis and polyarteritis nodosa
    • Henshaw TJ, Malone CC, Gabay JE, Williams RC Jr, (1994) Elevations of neutrophil proteinase 3 in serum of patients with Wegener's granulomatosis and polyarteritis nodosa. Arthritis Rheum 37: 104-112.
    • (1994) Arthritis Rheum , vol.37 , pp. 104-112
    • Henshaw, T.J.1    Malone, C.C.2    Gabay, J.E.3    Williams Jr., R.C.4
  • 3
    • 0030771395 scopus 로고    scopus 로고
    • Complexed plasma elastase as an in vivo marker for leukocyte activation in antineutrophil cytoplasmic antibody-associated vasculitis
    • Haubitz M, Schulzeck P, Schellong S, Schulze M, Koch KM, et al. (1997) Complexed plasma elastase as an in vivo marker for leukocyte activation in antineutrophil cytoplasmic antibody-associated vasculitis. Arthritis Rheum 40: 1680-1684.
    • (1997) Arthritis Rheum , vol.40 , pp. 1680-1684
    • Haubitz, M.1    Schulzeck, P.2    Schellong, S.3    Schulze, M.4    Koch, K.M.5
  • 5
    • 77953088427 scopus 로고    scopus 로고
    • Impairment of neutrophil extracellular trap degradation is associated with lupus nephritis
    • Hakkim A, Furnrohr BG, Amann K, Laube B, Abed UA, et al. (2010) Impairment of neutrophil extracellular trap degradation is associated with lupus nephritis. Proc Natl Acad Sci U S A 107: 9813-9818.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 9813-9818
    • Hakkim, A.1    Furnrohr, B.G.2    Amann, K.3    Laube, B.4    Abed, U.A.5
  • 6
    • 0036433010 scopus 로고    scopus 로고
    • Kinetics of thrombomodulin release and endothelial cell injury by neutrophil-derived proteases and oxygen radicals
    • Boehme MW, Galle P, Stremmel W, (2002) Kinetics of thrombomodulin release and endothelial cell injury by neutrophil-derived proteases and oxygen radicals. Immunology 107: 340-349.
    • (2002) Immunology , vol.107 , pp. 340-349
    • Boehme, M.W.1    Galle, P.2    Stremmel, W.3
  • 7
    • 0036892507 scopus 로고    scopus 로고
    • Novel effects of neutrophil-derived proteinase 3 and elastase on the vascular endothelium involve in vivo cleavage of NF-kappaB and proapoptotic changes in JNK, ERK, and p38 MAPK signaling pathways
    • Preston GA, Zarella CS, Pendergraft WF III, Rudolph EH, Yang JJ, et al. (2002) Novel effects of neutrophil-derived proteinase 3 and elastase on the vascular endothelium involve in vivo cleavage of NF-kappaB and proapoptotic changes in JNK, ERK, and p38 MAPK signaling pathways. J Am Soc Nephrol 13: 2840-2849.
    • (2002) J Am Soc Nephrol , vol.13 , pp. 2840-2849
    • Preston, G.A.1    Zarella, C.S.2    Pendergraft III, W.F.3    Rudolph, E.H.4    Yang, J.J.5
  • 8
    • 0023801387 scopus 로고
    • The human neutrophil serine proteinases, elastase and cathepsin G, can mediate glomerular injury in vivo
    • Johnson RJ, Couser WG, Alpers CE, Vissers M, Schulze M, et al. (1988) The human neutrophil serine proteinases, elastase and cathepsin G, can mediate glomerular injury in vivo. J Exp Med 168: 1169-1174.
    • (1988) J Exp Med , vol.168 , pp. 1169-1174
    • Johnson, R.J.1    Couser, W.G.2    Alpers, C.E.3    Vissers, M.4    Schulze, M.5
  • 9
    • 12944250467 scopus 로고    scopus 로고
    • ANCA induces beta2 integrin and CXC chemokine-dependent neutrophil-endothelial cell interactions that mimic those of highly cytokine-activated endothelium
    • Calderwood JW, Williams JM, Morgan MD, Nash GB, Savage CO, (2005) ANCA induces beta2 integrin and CXC chemokine-dependent neutrophil-endothelial cell interactions that mimic those of highly cytokine-activated endothelium. J Leukoc Biol 77: 33-43.
    • (2005) J Leukoc Biol , vol.77 , pp. 33-43
    • Calderwood, J.W.1    Williams, J.M.2    Morgan, M.D.3    Nash, G.B.4    Savage, C.O.5
  • 10
    • 84865602319 scopus 로고    scopus 로고
    • Neutrophil serine protease mediate inflammatory cell recruitment by glomerular endothelium and progression towards dysfunction
    • (in press)
    • Kuravi SJ, Bevins A, Satchell SC, Harper L, Williams JM, et al. (2012) Neutrophil serine protease mediate inflammatory cell recruitment by glomerular endothelium and progression towards dysfunction. Nephrol Dial Transplant (in press).
    • (2012) Nephrol Dial Transplant
    • Kuravi, S.J.1    Bevins, A.2    Satchell, S.C.3    Harper, L.4    Williams, J.M.5
  • 11
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu TK, Hung DT, Wheaton VI, Coughlin SR, (1991) Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell 64: 1057-1068.
    • (1991) Cell , vol.64 , pp. 1057-1068
    • Vu, T.K.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 12
    • 0025784847 scopus 로고
    • cDNA cloning and expression of a hamster [alpha]-thrombin receptor coupled to Ca2+ mobilization
    • Rasmussen UB, Vouret-Craviari V, Jallat S, Schlesinger Y, Pages G, et al. (1991) cDNA cloning and expression of a hamster [alpha]-thrombin receptor coupled to Ca2+ mobilization. FEBS Letters 288: 123-128.
    • (1991) FEBS Letters , vol.288 , pp. 123-128
    • Rasmussen, U.B.1    Vouret-Craviari, V.2    Jallat, S.3    Schlesinger, Y.4    Pages, G.5
  • 13
    • 0028284760 scopus 로고
    • Alpha-thrombin and trypsin use different receptors to stimulate arachidonic acid metabolism
    • Levine L, (1994) Alpha-thrombin and trypsin use different receptors to stimulate arachidonic acid metabolism. Prostaglandins 47: 437-449.
    • (1994) Prostaglandins , vol.47 , pp. 437-449
    • Levine, L.1
  • 14
    • 28344436780 scopus 로고    scopus 로고
    • Protease-activated receptors in hemostasis, thrombosis and vascular biology
    • Coughlin SR, (2005) Protease-activated receptors in hemostasis, thrombosis and vascular biology. J Thromb Haemost 3: 1800-1814.
    • (2005) J Thromb Haemost , vol.3 , pp. 1800-1814
    • Coughlin, S.R.1
  • 15
    • 33745728319 scopus 로고    scopus 로고
    • Proteinase-activated receptors (PARs): crossroads between innate immunity and coagulation
    • Cirino G, Vergnolle N, (2006) Proteinase-activated receptors (PARs): crossroads between innate immunity and coagulation. Current Opinion in Pharmacology 6: 428-434.
    • (2006) Current Opinion in Pharmacology , vol.6 , pp. 428-434
    • Cirino, G.1    Vergnolle, N.2
  • 16
    • 0032943041 scopus 로고    scopus 로고
    • Endothelial protease-activated receptor-2 induces tissue factor expression and von Willebrand factor release
    • Langer F, Morys-Wortmann C, Kusters B, Storck J, (1999) Endothelial protease-activated receptor-2 induces tissue factor expression and von Willebrand factor release. Br J Haematol 105: 542-550.
    • (1999) Br J Haematol , vol.105 , pp. 542-550
    • Langer, F.1    Morys-Wortmann, C.2    Kusters, B.3    Storck, J.4
  • 17
    • 0028873577 scopus 로고
    • The tethered ligand receptor is the responsible receptor for the thrombin induced release of von Willebrand factor from endothelial cells (HUVEC)
    • Storck J, Kusters B, Zimmermann ER, (1995) The tethered ligand receptor is the responsible receptor for the thrombin induced release of von Willebrand factor from endothelial cells (HUVEC). Thromb Res 77: 249-258.
    • (1995) Thromb Res , vol.77 , pp. 249-258
    • Storck, J.1    Kusters, B.2    Zimmermann, E.R.3
  • 18
    • 0027185888 scopus 로고
    • von Willebrand factor release and P-selectin expression is stimulated by thrombin and trypsin but not IL-1 in cultured human endothelial cells
    • Collins PW, Macey MG, Cahill MR, Newland AC, (1993) von Willebrand factor release and P-selectin expression is stimulated by thrombin and trypsin but not IL-1 in cultured human endothelial cells. Thromb Haemost 70: 346-350.
    • (1993) Thromb Haemost , vol.70 , pp. 346-350
    • Collins, P.W.1    Macey, M.G.2    Cahill, M.R.3    Newland, A.C.4
  • 19
    • 0037458275 scopus 로고    scopus 로고
    • Differential actions of PAR2 and PAR1 in stimulating human endothelial cell exocytosis and permeability: the role of Rho-GTPases
    • Klarenbach SW, Chipiuk A, Nelson RC, Hollenberg MD, Murray AG, (2003) Differential actions of PAR2 and PAR1 in stimulating human endothelial cell exocytosis and permeability: the role of Rho-GTPases. Circ Res 92: 272-278.
    • (2003) Circ Res , vol.92 , pp. 272-278
    • Klarenbach, S.W.1    Chipiuk, A.2    Nelson, R.C.3    Hollenberg, M.D.4    Murray, A.G.5
  • 20
    • 0028814818 scopus 로고
    • Constitutive expression and modulation of the functional thrombin receptor in the human kidney
    • Xu Y, Zacharias U, Peraldi MN, He CJ, Lu C, et al. (1995) Constitutive expression and modulation of the functional thrombin receptor in the human kidney. Am J Pathol 146: 101-110.
    • (1995) Am J Pathol , vol.146 , pp. 101-110
    • Xu, Y.1    Zacharias, U.2    Peraldi, M.N.3    He, C.J.4    Lu, C.5
  • 21
    • 0041342006 scopus 로고    scopus 로고
    • Protease-Activated Receptor-2 Expression in IgA Nephropathy: A Potential Role in the Pathogenesis of Interstitial Fibrosis
    • Grandaliano G, Pontrelli P, Cerullo G, Monno R, Ranieri E, et al. (2003) Protease-Activated Receptor-2 Expression in IgA Nephropathy: A Potential Role in the Pathogenesis of Interstitial Fibrosis. J Am Soc Nephrol 14: 2072-2083.
    • (2003) J Am Soc Nephrol , vol.14 , pp. 2072-2083
    • Grandaliano, G.1    Pontrelli, P.2    Cerullo, G.3    Monno, R.4    Ranieri, E.5
  • 23
    • 23044510603 scopus 로고    scopus 로고
    • Role of coagulation factor Xa and protease-activated receptor 2 in human mesangial cell proliferation
    • Tanaka M, Arai H, Liu N, Nogaki F, Nomura K, et al. (2005) Role of coagulation factor Xa and protease-activated receptor 2 in human mesangial cell proliferation. Kidney Int 67: 2123-2133.
    • (2005) Kidney Int , vol.67 , pp. 2123-2133
    • Tanaka, M.1    Arai, H.2    Liu, N.3    Nogaki, F.4    Nomura, K.5
  • 24
    • 33847193578 scopus 로고    scopus 로고
    • Roles of coagulation pathway and factor Xa in rat mesangioproliferative glomerulonephritis
    • Nomura K, Liu N, Nagai K, Hasegawa T, Kobayashi I, et al. (2006) Roles of coagulation pathway and factor Xa in rat mesangioproliferative glomerulonephritis. Lab Invest 87: 150-160.
    • (2006) Lab Invest , vol.87 , pp. 150-160
    • Nomura, K.1    Liu, N.2    Nagai, K.3    Hasegawa, T.4    Kobayashi, I.5
  • 25
    • 0034614895 scopus 로고    scopus 로고
    • Protease-Activated Receptor 1 Mediates Thrombin-Dependent, Cell-Mediated Renal Inflammation in Crescentic Glomerulonephritis
    • Cunningham MA, Rondeau E, Chen X, Coughlin SR, Holdsworth SR, et al. (2000) Protease-Activated Receptor 1 Mediates Thrombin-Dependent, Cell-Mediated Renal Inflammation in Crescentic Glomerulonephritis. J Exp Med 191: 455-462.
    • (2000) J Exp Med , vol.191 , pp. 455-462
    • Cunningham, M.A.1    Rondeau, E.2    Chen, X.3    Coughlin, S.R.4    Holdsworth, S.R.5
  • 26
    • 34548816164 scopus 로고    scopus 로고
    • Protease-Activated Receptor-2 Augments Experimental Crescentic Glomerulonephritis
    • Moussa L, Apostolopoulos J, Davenport P, Tchongue J, Tipping PG, (2007) Protease-Activated Receptor-2 Augments Experimental Crescentic Glomerulonephritis. Am J Pathol 171: 800-808.
    • (2007) Am J Pathol , vol.171 , pp. 800-808
    • Moussa, L.1    Apostolopoulos, J.2    Davenport, P.3    Tchongue, J.4    Tipping, P.G.5
  • 27
    • 77649224137 scopus 로고    scopus 로고
    • Activated protein C action in inflammation
    • Sarangi PP, Lee HW, Kim M, (2010) Activated protein C action in inflammation. Br J Haematol 148: 817-833.
    • (2010) Br J Haematol , vol.148 , pp. 817-833
    • Sarangi, P.P.1    Lee, H.W.2    Kim, M.3
  • 28
    • 0029790055 scopus 로고    scopus 로고
    • The endothelial cell protein C receptor augments protein C activation by the thrombin-thrombomodulin complex
    • Stearns-Kurosawa DJ, Kurosawa S, Mollica JS, Ferrell GL, Esmon CT, (1996) The endothelial cell protein C receptor augments protein C activation by the thrombin-thrombomodulin complex. Proc Natl Acad Sci U S A 93: 10212-10216.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 10212-10216
    • Stearns-Kurosawa, D.J.1    Kurosawa, S.2    Mollica, J.S.3    Ferrell, G.L.4    Esmon, C.T.5
  • 31
    • 0027337230 scopus 로고
    • A Simplified Method for Culture of Endothelial Cells and Analysis of Adhesion of Blood Cells under Conditions of Flow
    • Cooke BM, Usami S, Perry I, Nash GB, (1993) A Simplified Method for Culture of Endothelial Cells and Analysis of Adhesion of Blood Cells under Conditions of Flow. Microvascular Research 45: 33-45.
    • (1993) Microvascular Research , vol.45 , pp. 33-45
    • Cooke, B.M.1    Usami, S.2    Perry, I.3    Nash, G.B.4
  • 32
    • 33646529152 scopus 로고    scopus 로고
    • Conditionally immortalized human glomerular endothelial cells expressing fenestrations in response to VEGF
    • Satchell SC, Tasman CH, Singh A, Ni L, Geelen J, et al. (2006) Conditionally immortalized human glomerular endothelial cells expressing fenestrations in response to VEGF. Kidney Int 69: 1633-1640.
    • (2006) Kidney Int , vol.69 , pp. 1633-1640
    • Satchell, S.C.1    Tasman, C.H.2    Singh, A.3    Ni, L.4    Geelen, J.5
  • 33
    • 0017710978 scopus 로고
    • Characteristics of a Human Cell Line Transformed by DNA from Human Adenovirus Type 5
    • Graham FL, Smiley J, Russell WC, Nairn R, (1977) Characteristics of a Human Cell Line Transformed by DNA from Human Adenovirus Type 5. J Gen Virol 36: 59-72.
    • (1977) J Gen Virol , vol.36 , pp. 59-72
    • Graham, F.L.1    Smiley, J.2    Russell, W.C.3    Nairn, R.4
  • 34
    • 0032911415 scopus 로고    scopus 로고
    • Evaluation of proteinase-activated receptor-1 (PAR1) agonists and antagonists using a cultured cell receptor desensitization assay: activation of PAR2 by PAR1-targeted ligands
    • Kawabata A, Saifeddine M, Al Ani B, Leblond L, Hollenberg MD, (1999) Evaluation of proteinase-activated receptor-1 (PAR1) agonists and antagonists using a cultured cell receptor desensitization assay: activation of PAR2 by PAR1-targeted ligands. J Pharmacol Exp Ther 288: 358-370.
    • (1999) J Pharmacol Exp Ther , vol.288 , pp. 358-370
    • Kawabata, A.1    Saifeddine, M.2    Al Ani, B.3    Leblond, L.4    Hollenberg, M.D.5
  • 35
    • 33644840620 scopus 로고    scopus 로고
    • Cellular Pathology of Atherosclerosis: Smooth Muscle Cells Promote Adhesion of Platelets to Cocultured Endothelial Cells
    • Tull SP, Anderson SI, Hughan SC, Watson SP, Nash GB, et al. (2006) Cellular Pathology of Atherosclerosis: Smooth Muscle Cells Promote Adhesion of Platelets to Cocultured Endothelial Cells. Circ Res 98: 98-104.
    • (2006) Circ Res , vol.98 , pp. 98-104
    • Tull, S.P.1    Anderson, S.I.2    Hughan, S.C.3    Watson, S.P.4    Nash, G.B.5
  • 36
    • 0030018812 scopus 로고    scopus 로고
    • Characterization of altered calcium signalling in T lymphocytes from patients with rheumatoid arthritis (RA)
    • Carruthers DM, Naylor WG, Allen ME, Kitas GD, Bacon PA, et al. (1996) Characterization of altered calcium signalling in T lymphocytes from patients with rheumatoid arthritis (RA). Clin Exp Immunol 105: 291-296.
    • (1996) Clin Exp Immunol , vol.105 , pp. 291-296
    • Carruthers, D.M.1    Naylor, W.G.2    Allen, M.E.3    Kitas, G.D.4    Bacon, P.A.5
  • 37
    • 0028111114 scopus 로고
    • Changes in the structure and function of the human thrombin receptor during receptor activation, internalization, and recycling
    • Brass LF, Pizarro S, Ahuja M, Belmonte E, Blanchard N, et al. (1994) Changes in the structure and function of the human thrombin receptor during receptor activation, internalization, and recycling. J Biol Chem 269: 2943-2952.
    • (1994) J Biol Chem , vol.269 , pp. 2943-2952
    • Brass, L.F.1    Pizarro, S.2    Ahuja, M.3    Belmonte, E.4    Blanchard, N.5
  • 38
    • 0027378281 scopus 로고
    • Internalization and recycling of activated thrombin receptors
    • Hoxie JA, Ahuja M, Belmonte E, Pizarro S, Parton R, et al. (1993) Internalization and recycling of activated thrombin receptors. J Biol Chem 268: 13756-13763.
    • (1993) J Biol Chem , vol.268 , pp. 13756-13763
    • Hoxie, J.A.1    Ahuja, M.2    Belmonte, E.3    Pizarro, S.4    Parton, R.5
  • 40
    • 84859127474 scopus 로고    scopus 로고
    • Tumor-Derived Microvesicles Induce Proangiogenic Phenotype in Endothelial Cells via Endocytosis
    • Kawamoto T, Ohga N, Akiyama K, Hirata N, Kitahara S, et al. (2012) Tumor-Derived Microvesicles Induce Proangiogenic Phenotype in Endothelial Cells via Endocytosis. PLoS One 7: e34045.
    • (2012) PLoS One , vol.7
    • Kawamoto, T.1    Ohga, N.2    Akiyama, K.3    Hirata, N.4    Kitahara, S.5
  • 41
    • 84861214572 scopus 로고    scopus 로고
    • Endothelin Induces Rapid, Dynamin-mediated Budding of Endothelial Caveolae Rich in ET-B
    • Oh P, Horner T, Witkiewicz H, Schnitzer JE, (2012) Endothelin Induces Rapid, Dynamin-mediated Budding of Endothelial Caveolae Rich in ET-B. J Biol Chem 287: 17353-17362.
    • (2012) J Biol Chem , vol.287 , pp. 17353-17362
    • Oh, P.1    Horner, T.2    Witkiewicz, H.3    Schnitzer, J.E.4
  • 42
    • 0026690665 scopus 로고
    • Cloned platelet thrombin receptor is necessary for thrombin-induced platelet activation
    • Hung DT, Vu TK, Wheaton VI, Ishii K, Coughlin SR, (1992) Cloned platelet thrombin receptor is necessary for thrombin-induced platelet activation. J Clin Invest 89: 1350-1353.
    • (1992) J Clin Invest , vol.89 , pp. 1350-1353
    • Hung, D.T.1    Vu, T.K.2    Wheaton, V.I.3    Ishii, K.4    Coughlin, S.R.5
  • 43
    • 0037371578 scopus 로고    scopus 로고
    • Selective tryptic cleavage at the tethered ligand site of the amino terminal domain of proteinase-activated receptor-2 in intact cells
    • Al Ani B, Hollenberg MD, (2003) Selective tryptic cleavage at the tethered ligand site of the amino terminal domain of proteinase-activated receptor-2 in intact cells. J Pharmacol Exp Ther 304: 1120-1128.
    • (2003) J Pharmacol Exp Ther , vol.304 , pp. 1120-1128
    • Al Ani, B.1    Hollenberg, M.D.2
  • 44
    • 0034609557 scopus 로고    scopus 로고
    • Proteolysis of the exodomain of recombinant protease-activated receptors: prediction of receptor activation or inactivation by MALDI mass spectrometry
    • Loew D, Perrault C, Morales M, Moog S, Ravanat C, et al. (2000) Proteolysis of the exodomain of recombinant protease-activated receptors: prediction of receptor activation or inactivation by MALDI mass spectrometry. Biochemistry 39: 10812-10822.
    • (2000) Biochemistry , vol.39 , pp. 10812-10822
    • Loew, D.1    Perrault, C.2    Morales, M.3    Moog, S.4    Ravanat, C.5
  • 45
    • 65949091143 scopus 로고    scopus 로고
    • Proteases display biased agonism at protease-activated receptors: Location matters!
    • Russo A, Soh UJ, Trejo J, (2009) Proteases display biased agonism at protease-activated receptors: location matters! Mol Interv. 9: 87-96.
    • (2009) Mol Interv , vol.9 , pp. 87-96
    • Russo, A.1    Soh, U.J.2    Trejo, J.3
  • 46
    • 65549087489 scopus 로고    scopus 로고
    • Caveolae are required for protease-selective signaling by protease-activated receptor-1
    • Russo A, Soh UJ, Paing MM, Arora P, Trejo J, (2009) Caveolae are required for protease-selective signaling by protease-activated receptor-1. Proc Natl Acad Sci U S A 106: 6393-6397.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 6393-6397
    • Russo, A.1    Soh, U.J.2    Paing, M.M.3    Arora, P.4    Trejo, J.5
  • 47
    • 70949084458 scopus 로고    scopus 로고
    • Leukocyte elastase induces lung epithelial apoptosis via a PAR-1-, NF-kappaB-, and p53-dependent pathway
    • Suzuki T, Yamashita C, Zemans RL, Briones N, Van Linden A, et al. (2009) Leukocyte elastase induces lung epithelial apoptosis via a PAR-1-, NF-kappaB-, and p53-dependent pathway. Am J Respir Cell Mol Biol 41: 742-755.
    • (2009) Am J Respir Cell Mol Biol , vol.41 , pp. 742-755
    • Suzuki, T.1    Yamashita, C.2    Zemans, R.L.3    Briones, N.4    Van Linden, A.5
  • 48
    • 77955410626 scopus 로고    scopus 로고
    • Reciprocal coupling of coagulation and innate immunity via neutrophil serine proteases
    • Massberg S, Grahl L, von Bruehl ML, Manukyan D, Pfeiler S, et al. (2010) Reciprocal coupling of coagulation and innate immunity via neutrophil serine proteases. Nat Med.
    • (2010) Nat Med
    • Massberg, S.1    Grahl, L.2    von Bruehl, M.L.3    Manukyan, D.4    Pfeiler, S.5
  • 49
    • 57349120511 scopus 로고    scopus 로고
    • Modulation of tissue factor and tissue factor pathway inhibitor-1 by neutrophil proteases
    • Steppich BA, Seitz I, Busch G, Stein A, Ott I, (2008) Modulation of tissue factor and tissue factor pathway inhibitor-1 by neutrophil proteases. Thromb Haemost 100: 1068-1075.
    • (2008) Thromb Haemost , vol.100 , pp. 1068-1075
    • Steppich, B.A.1    Seitz, I.2    Busch, G.3    Stein, A.4    Ott, I.5
  • 50
    • 37049012509 scopus 로고    scopus 로고
    • The ligand occupancy of endothelial protein C receptor switches the protease-activated receptor 1-dependent signaling specificity of thrombin from a permeability-enhancing to a barrier-protective response in endothelial cells
    • Bae JS, Yang L, Manithody C, Rezaie AR, (2007) The ligand occupancy of endothelial protein C receptor switches the protease-activated receptor 1-dependent signaling specificity of thrombin from a permeability-enhancing to a barrier-protective response in endothelial cells. Blood 110: 3909-3916.
    • (2007) Blood , vol.110 , pp. 3909-3916
    • Bae, J.S.1    Yang, L.2    Manithody, C.3    Rezaie, A.R.4
  • 51
    • 79960114650 scopus 로고    scopus 로고
    • Neutrophil elastase acts as a biased agonist for proteinase-activated receptor-2 (PAR2)
    • Ramachandran R, Mihara K, Chung H, Renaux B, Lau CS, et al. (2011) Neutrophil elastase acts as a biased agonist for proteinase-activated receptor-2 (PAR2). J Biol Chem 286: 24638-24648.
    • (2011) J Biol Chem , vol.286 , pp. 24638-24648
    • Ramachandran, R.1    Mihara, K.2    Chung, H.3    Renaux, B.4    Lau, C.S.5
  • 52
    • 70349324342 scopus 로고    scopus 로고
    • Agonist-biased signaling via proteinase activated receptor-2: differential activation of calcium and mitogen-activated protein kinase pathways
    • Ramachandran R, Mihara K, Mathur M, Rochdi MD, Bouvier M, et al. (2009) Agonist-biased signaling via proteinase activated receptor-2: differential activation of calcium and mitogen-activated protein kinase pathways. Mol Pharmacol 76: 791-801.
    • (2009) Mol Pharmacol , vol.76 , pp. 791-801
    • Ramachandran, R.1    Mihara, K.2    Mathur, M.3    Rochdi, M.D.4    Bouvier, M.5
  • 53
    • 79959546461 scopus 로고    scopus 로고
    • N-linked glycosylation regulates human proteinase-activated receptor-1 cell surface expression and disarming via neutrophil proteinases and thermolysin
    • Xiao YP, Morice AH, Compton SJ, Sadofsky L, (2011) N-linked glycosylation regulates human proteinase-activated receptor-1 cell surface expression and disarming via neutrophil proteinases and thermolysin. J Biol Chem 286: 22991-23002.
    • (2011) J Biol Chem , vol.286 , pp. 22991-23002
    • Xiao, Y.P.1    Morice, A.H.2    Compton, S.J.3    Sadofsky, L.4
  • 54
    • 0036905071 scopus 로고    scopus 로고
    • Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling
    • Compton SJ, Sandhu S, Wijesuriya SJ, Hollenberg MD, (2002) Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling. Biochem J 368: 495-505.
    • (2002) Biochem J , vol.368 , pp. 495-505
    • Compton, S.J.1    Sandhu, S.2    Wijesuriya, S.J.3    Hollenberg, M.D.4
  • 55
    • 0037372534 scopus 로고    scopus 로고
    • Proteinase-Activated Receptor-2 and Human Lung Epithelial Cells: Disarming by Neutrophil Serine Proteinases
    • Dulon S, Cande C, Bunnett NW, Hollenberg MD, Chignard M, et al. (2003) Proteinase-Activated Receptor-2 and Human Lung Epithelial Cells: Disarming by Neutrophil Serine Proteinases. Am J Respir Cell Mol Biol 28: 339-346.
    • (2003) Am J Respir Cell Mol Biol , vol.28 , pp. 339-346
    • Dulon, S.1    Cande, C.2    Bunnett, N.W.3    Hollenberg, M.D.4    Chignard, M.5
  • 56
    • 0037108503 scopus 로고    scopus 로고
    • Activation of human oral epithelial cells by neutrophil proteinase 3 through protease-activated receptor-2
    • Uehara A, Sugawara S, Muramoto K, Takada H, (2002) Activation of human oral epithelial cells by neutrophil proteinase 3 through protease-activated receptor-2. J Immunol 169: 4594-4603.
    • (2002) J Immunol , vol.169 , pp. 4594-4603
    • Uehara, A.1    Sugawara, S.2    Muramoto, K.3    Takada, H.4
  • 57
    • 0037797300 scopus 로고    scopus 로고
    • Neutrophil Serine Proteinases Activate Human Nonepithelial Cells to Produce Inflammatory Cytokines Through Protease-Activated Receptor 2
    • Uehara A, Muramoto K, Takada H, Sugawara S, (2003) Neutrophil Serine Proteinases Activate Human Nonepithelial Cells to Produce Inflammatory Cytokines Through Protease-Activated Receptor 2. J Immunol 170: 5690-5696.
    • (2003) J Immunol , vol.170 , pp. 5690-5696
    • Uehara, A.1    Muramoto, K.2    Takada, H.3    Sugawara, S.4
  • 58
    • 0036533649 scopus 로고    scopus 로고
    • Activation of Protease-Activated Receptor (PAR)-1, PAR-2, and PAR-4 Stimulates IL-6, IL-8, and Prostaglandin E2 Release from Human Respiratory Epithelial Cells
    • Asokananthan N, Graham PT, Fink J, Knight DA, Bakker AJ, et al. (2002) Activation of Protease-Activated Receptor (PAR)-1, PAR-2, and PAR-4 Stimulates IL-6, IL-8, and Prostaglandin E2 Release from Human Respiratory Epithelial Cells. J Immunol 168: 3577-3585.
    • (2002) J Immunol , vol.168 , pp. 3577-3585
    • Asokananthan, N.1    Graham, P.T.2    Fink, J.3    Knight, D.A.4    Bakker, A.J.5
  • 59
    • 77954615097 scopus 로고    scopus 로고
    • The role of proteinase 3 (PR3) and the protease-activated receptor-2 (PAR-2) pathway in dendritic cell (DC) maturation of human-DC-like monocytes and murine DC
    • Jiang B, Grage-Griebenow E, Csernok E, Butherus K, Ehlers S, et al. (2010) The role of proteinase 3 (PR3) and the protease-activated receptor-2 (PAR-2) pathway in dendritic cell (DC) maturation of human-DC-like monocytes and murine DC. Clin Exp Rheumatol 28: 56-61.
    • (2010) Clin Exp Rheumatol , vol.28 , pp. 56-61
    • Jiang, B.1    Grage-Griebenow, E.2    Csernok, E.3    Butherus, K.4    Ehlers, S.5


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