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Volumn 8, Issue 9, 2013, Pages

Disruption of the Endothelial Barrier by Proteases from the Bacterial Pathogen Pseudomonas aeruginosa: Implication of Matrilysis and Receptor Cleavage

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; METALLOPROTEINASE; METALLOPROTEINASE LASB; OCCLUDIN; PHOSPHORAMIDON; PROTEINASE; UNCLASSIFIED DRUG; VASCULAR ENDOTHELIAL CADHERIN; VON WILLEBRAND FACTOR;

EID: 84884359440     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0075708     Document Type: Article
Times cited : (32)

References (73)
  • 1
    • 33646695668 scopus 로고    scopus 로고
    • Pericellular proteases in angiogenesis and vasculogenesis
    • doi:10.1161/01.ATV.0000209518.58252.17
    • van Hinsbergh VWM, Engelse MA, Quax PHA, (2006) Pericellular proteases in angiogenesis and vasculogenesis. Arterioscler Thromb Vasc Biol 26: 716-728. doi:10.1161/01.ATV.0000209518.58252.17. PubMed: 16469948.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 716-728
    • van Hinsbergh, V.W.M.1    Engelse, M.A.2    Quax, P.H.A.3
  • 2
    • 79955584619 scopus 로고    scopus 로고
    • Structure, function and pathophysiology of protease activated receptors
    • doi:10.1016/j.pharmthera.2011.01.003
    • Adams MN, Ramachandran R, Yau M-K, Suen JY, Fairlie DP, et al. (2011) Structure, function and pathophysiology of protease activated receptors. Pharmacol Therapeut 130: 248-282. doi:10.1016/j.pharmthera.2011.01.003. PubMed: 21277892.
    • (2011) Pharmacol Therapeut , vol.130 , pp. 248-282
    • Adams, M.N.1    Ramachandran, R.2    Yau, M.-K.3    Suen, J.Y.4    Fairlie, D.P.5
  • 3
    • 0029391519 scopus 로고
    • Endothelial cell injury induced by plasmin in-vitro
    • Okajima K, Abe H, Binder BR, (1995) Endothelial cell injury induced by plasmin in-vitro. J Lab Clin Med 126: 377-384. PubMed: 7561447.
    • (1995) J Lab Clin Med , vol.126 , pp. 377-384
    • Okajima, K.1    Abe, H.2    Binder, B.R.3
  • 4
    • 0035060384 scopus 로고    scopus 로고
    • Matrix metalloproteinase-1 and -9 activation by plasmin regulates a novel endothelial cell-mediated mechanism of collagen gel contraction and capillary tube regression in three-dimensional collagen matrices
    • Davis GE, Pintar Allen KA, Salazar R, Maxwell SA, (2000) Matrix metalloproteinase-1 and-9 activation by plasmin regulates a novel endothelial cell-mediated mechanism of collagen gel contraction and capillary tube regression in three-dimensional collagen matrices. J Cell Sci 114: 917-930. PubMed: 11181175.
    • (2000) J Cell Sci , vol.114 , pp. 917-930
    • Davis, G.E.1    Pintar Allen, K.A.2    Salazar, R.3    Maxwell, S.A.4
  • 5
    • 0030850248 scopus 로고    scopus 로고
    • Integrins and anoikis
    • doi:10.1016/S0955-0674(97)80124-X
    • Frisch SM, Ruoslahti E, (1997) Integrins and anoikis. Curr Opin Cell Biol 9: 701-706. doi:10.1016/S0955-0674(97)80124-X. PubMed: 9330874.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 701-706
    • Frisch, S.M.1    Ruoslahti, E.2
  • 6
    • 3943086318 scopus 로고    scopus 로고
    • Proteolysis of the pericellular matrix: a novel element determining cell survival and death in the pathogenesis of plaque erosion and rupture
    • doi:10.1161/01.ATV.0000135322.78008.55
    • Lindstedt KA, Leskinen MJ, Kovanen PT, (2004) Proteolysis of the pericellular matrix: a novel element determining cell survival and death in the pathogenesis of plaque erosion and rupture. Arterioscler Thromb Vasc Biol 24: 1350-1358. doi:10.1161/01.ATV.0000135322.78008.55. PubMed: 15191939.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 1350-1358
    • Lindstedt, K.A.1    Leskinen, M.J.2    Kovanen, P.T.3
  • 7
    • 33750436906 scopus 로고    scopus 로고
    • Retention and activation of blood-borne proteases in the arterial wall
    • doi:10.1016/j.jacc.2006.04.098
    • Houard X, Leclercq A, Fontaine V, Coutard M, Martin-Ventura B, et al. (2006) Retention and activation of blood-borne proteases in the arterial wall. J Am Coll Cardiol 48: A3-A9. doi:10.1016/j.jacc.2006.04.098.
    • (2006) J Am Coll Cardiol , vol.48
    • Houard, X.1    Leclercq, A.2    Fontaine, V.3    Coutard, M.4    Martin-Ventura, B.5
  • 8
    • 82755190844 scopus 로고    scopus 로고
    • Anoikis: an emerging hallmark in health and diseases
    • doi:10.1002/path.3000
    • Taddei ML, Giannoni E, Fiaschi T, Chiarugi P, (2012) Anoikis: an emerging hallmark in health and diseases. J Pathol 226: 380-393. doi:10.1002/path.3000. PubMed: 21953325.
    • (2012) J Pathol , vol.226 , pp. 380-393
    • Taddei, M.L.1    Giannoni, E.2    Fiaschi, T.3    Chiarugi, P.4
  • 9
    • 0037247739 scopus 로고    scopus 로고
    • Interaction of pathogens with the endothelium
    • Hippenstiel S, Suttorp N, (2003) Interaction of pathogens with the endothelium. Thromb Haemost 89: 18-24. PubMed: 12540949.
    • (2003) Thromb Haemost , vol.89 , pp. 18-24
    • Hippenstiel, S.1    Suttorp, N.2
  • 10
    • 33645734097 scopus 로고    scopus 로고
    • The endothelium as a target for infections
    • Valbuena G, Walker DH, (2006) The endothelium as a target for infections. Annu Rev Pathol Mech Dis 1: 171-198.
    • (2006) Annu Rev Pathol Mech Dis , vol.1 , pp. 171-198
    • Valbuena, G.1    Walker, D.H.2
  • 11
    • 33847216826 scopus 로고    scopus 로고
    • Endothelial cell infection and hemostasis
    • doi:10.1016/j.thromres.2006.06.006
    • Sahni SK, (2007) Endothelial cell infection and hemostasis. Thromb Res 119: 531-549. doi:10.1016/j.thromres.2006.06.006. PubMed: 16875715.
    • (2007) Thromb Res , vol.119 , pp. 531-549
    • Sahni, S.K.1
  • 12
    • 75749139748 scopus 로고    scopus 로고
    • Breaking the wall: targeting of the endothelium by pathogenic bacteria
    • Lemichez E, Lecuit M, Nassif X, Bourdoulous S, (2010) Breaking the wall: targeting of the endothelium by pathogenic bacteria. Nat Rev Microbiol 8: 93-104. PubMed: 20040916.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 93-104
    • Lemichez, E.1    Lecuit, M.2    Nassif, X.3    Bourdoulous, S.4
  • 14
    • 34848896609 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa bloodstream infections: how should we treat them?
    • Van Delden C, (2007) Pseudomonas aeruginosa bloodstream infections: how should we treat them? Int J Antimicrob Ag 30S: S71-S75. PubMed: 17698326.
    • (2007) Int J Antimicrob Ag , vol.30 S
    • Van Delden, C.1
  • 15
    • 84863518296 scopus 로고    scopus 로고
    • Contribution of an arsenal of virulence factors to pathogenesis of Pseudomonas aeruginosa infections
    • doi:10.1007/s13213-011-0273-y
    • Strateva T, Mitov I, (2011) Contribution of an arsenal of virulence factors to pathogenesis of Pseudomonas aeruginosa infections. Ann Microbiol 61: 717-732. doi:10.1007/s13213-011-0273-y.
    • (2011) Ann Microbiol , vol.61 , pp. 717-732
    • Strateva, T.1    Mitov, I.2
  • 16
    • 10044291650 scopus 로고    scopus 로고
    • Role of bacterial proteases in pseudomonal and serratial keratitis
    • Matsumoto K, (2004) Role of bacterial proteases in pseudomonal and serratial keratitis. Biol Chem 385: 1007-1016. PubMed: 15576320.
    • (2004) Biol Chem , vol.385 , pp. 1007-1016
    • Matsumoto, K.1
  • 17
    • 59849110833 scopus 로고    scopus 로고
    • Role of Pseudomonas aeruginosa type III effectors in disease
    • doi:10.1016/j.mib.2008.12.007
    • Engel J, Balachandran P, (2009) Role of Pseudomonas aeruginosa type III effectors in disease. Curr Opin Microbiol 12: 61-66. doi:10.1016/j.mib.2008.12.007. PubMed: 19168385.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 61-66
    • Engel, J.1    Balachandran, P.2
  • 18
    • 78649734744 scopus 로고    scopus 로고
    • Biological "glue" and "Velcro": molecular tools for adhesion and biofilm formation in the hairy and gluey bug Pseudomonas aeruginosa
    • Giraud C, Bernard CS, Ruer S, de Bentzmann S, (2010) Biological "glue" and "Velcro": molecular tools for adhesion and biofilm formation in the hairy and gluey bug Pseudomonas aeruginosa. Environ Microbiol Rep 2: 343-358. PubMed: 23766107.
    • (2010) Environ Microbiol Rep , vol.2 , pp. 343-358
    • Giraud, C.1    Bernard, C.S.2    Ruer, S.3    de Bentzmann, S.4
  • 19
    • 84858126311 scopus 로고    scopus 로고
    • The role of endogenous and exogenous enzymes in chronic wounds: a focus on the implications of aberrant levels of both host and bacterial proteases in wound healing
    • doi:10.1111/j.1524-475X.2012.00763.x
    • McCarty SM, Cochrane CA, Clegg PD, Percival SL, (2012) The role of endogenous and exogenous enzymes in chronic wounds: a focus on the implications of aberrant levels of both host and bacterial proteases in wound healing. Wound Rep Reg 20: 125-136. doi:10.1111/j.1524-475X.2012.00763.x. PubMed: 22380687.
    • (2012) Wound Rep Reg , vol.20 , pp. 125-136
    • McCarty, S.M.1    Cochrane, C.A.2    Clegg, P.D.3    Percival, S.L.4
  • 20
    • 0036273016 scopus 로고    scopus 로고
    • Bacterial protease inhibitors
    • doi:10.1002/med.10007
    • Supuran CT, Scozzafava A, Clare BW, (2002) Bacterial protease inhibitors. Med Res Rev 22: 329-372. doi:10.1002/med.10007. PubMed: 12111749.
    • (2002) Med Res Rev , vol.22 , pp. 329-372
    • Supuran, C.T.1    Scozzafava, A.2    Clare, B.W.3
  • 21
    • 34547622484 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa LasB metalloproteinase regulates the human urokinase-type plasminogen activator receptor through domain-specific endoproteolysis
    • doi:10.1128/IAI.00015-07
    • Leduc D, Beaufort N, de Bentzmann S, Rousselle JC, Namane A, et al. (2007) The Pseudomonas aeruginosa LasB metalloproteinase regulates the human urokinase-type plasminogen activator receptor through domain-specific endoproteolysis. Infect Immun 75: 3848-3858. doi:10.1128/IAI.00015-07. PubMed: 17517866.
    • (2007) Infect Immun , vol.75 , pp. 3848-3858
    • Leduc, D.1    Beaufort, N.2    de Bentzmann, S.3    Rousselle, J.C.4    Namane, A.5
  • 22
    • 0345097569 scopus 로고    scopus 로고
    • Transcription of quorum-sensing system genes in clinical and environmental isolates of Pseudomonas aeruginosa
    • doi:10.1128/JB.185.24.7222-7230.2003
    • Cabrol S, Olliver A, Pier GB, Andremont A, Ruimy R, (2003) Transcription of quorum-sensing system genes in clinical and environmental isolates of Pseudomonas aeruginosa. J Bacteriol 185: 7222-7230. doi:10.1128/JB.185.24.7222-7230.2003. PubMed: 14645283.
    • (2003) J Bacteriol , vol.185 , pp. 7222-7230
    • Cabrol, S.1    Olliver, A.2    Pier, G.B.3    Andremont, A.4    Ruimy, R.5
  • 23
    • 79955014644 scopus 로고    scopus 로고
    • Type II secretion system of Pseudomonas aeruginosa: in vivo evidence of a significant role in death due to lung infection
    • Jyot J, Balloy V, Jouvion G, Verma A, Touqui L, et al. (2011) Type II secretion system of Pseudomonas aeruginosa: in vivo evidence of a significant role in death due to lung infection. J Infect Dis 203: 369-377.
    • (2011) J Infect Dis , vol.203 , pp. 369-377
    • Jyot, J.1    Balloy, V.2    Jouvion, G.3    Verma, A.4    Touqui, L.5
  • 24
    • 61449163214 scopus 로고    scopus 로고
    • Corruption of innate immunity by bacterial proteases
    • doi:10.1159/000181144
    • Potempa J, Pike RN, (2009) Corruption of innate immunity by bacterial proteases. J Innate Immun 1: 70-87. doi:10.1159/000181144. PubMed: 19756242.
    • (2009) J Innate Immun , vol.1 , pp. 70-87
    • Potempa, J.1    Pike, R.N.2
  • 25
    • 0034982736 scopus 로고    scopus 로고
    • Hemorragic activity and muscle damaging effect of Pseudomonas aeruginosa metalloproteinase (elastase)
    • doi:10.1016/S0041-0101(01)00084-8
    • Komori Y, Nonogaki T, Nikai T, (2001) Hemorragic activity and muscle damaging effect of Pseudomonas aeruginosa metalloproteinase (elastase). Toxicon 39: 1327-1332. doi:10.1016/S0041-0101(01)00084-8. PubMed: 11384720.
    • (2001) Toxicon , vol.39 , pp. 1327-1332
    • Komori, Y.1    Nonogaki, T.2    Nikai, T.3
  • 26
    • 15544362250 scopus 로고    scopus 로고
    • Gingipains from Porphyromonas gingivalis W83 induce cell adhesion molecule cleavage and apoptosis in endothelial cells
    • doi:10.1128/IAI.73.3.1543-1552.2005
    • Sheets SM, Potempa J, Travis J, Casiano CA, Fletcher HM, (2005) Gingipains from Porphyromonas gingivalis W83 induce cell adhesion molecule cleavage and apoptosis in endothelial cells. Infect Immun 73: 1543-1552. doi:10.1128/IAI.73.3.1543-1552.2005. PubMed: 15731052.
    • (2005) Infect Immun , vol.73 , pp. 1543-1552
    • Sheets, S.M.1    Potempa, J.2    Travis, J.3    Casiano, C.A.4    Fletcher, H.M.5
  • 27
    • 12844258218 scopus 로고    scopus 로고
    • A functional virulence complex composed of gingipains, adhesins, and lipopolysaccharide shows high affinity to host cells and matrix proteins and escapes recognition by host immune systems
    • doi:10.1128/IAI.73.2.883-893.2005
    • Takii R, Kadowaki T, Baba A, Tsukuba T, Yamamoto K, (2005) A functional virulence complex composed of gingipains, adhesins, and lipopolysaccharide shows high affinity to host cells and matrix proteins and escapes recognition by host immune systems. Infect Immun 73: 883-893. doi:10.1128/IAI.73.2.883-893.2005. PubMed: 15664930.
    • (2005) Infect Immun , vol.73 , pp. 883-893
    • Takii, R.1    Kadowaki, T.2    Baba, A.3    Tsukuba, T.4    Yamamoto, K.5
  • 28
    • 0034530902 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa induces apoptosis in human endothelial cells
    • doi:10.1006/mpat.2000.0400
    • Valente E, Assis MC, Alvim IMP, Pereira GMB, Plotkowski MC, (2000) Pseudomonas aeruginosa induces apoptosis in human endothelial cells. Microb Pathog 29: 345-356. doi:10.1006/mpat.2000.0400. PubMed: 11095919.
    • (2000) Microb Pathog , vol.29 , pp. 345-356
    • Valente, E.1    Assis, M.C.2    Alvim, I.M.P.3    Pereira, G.M.B.4    Plotkowski, M.C.5
  • 29
    • 79960384623 scopus 로고    scopus 로고
    • The thermolysin-like metalloproteinase and virulence factor LasB from pathogenic Pseudomonas aeruginosa induces anoikis of human vascular cells
    • doi:10.1111/j.1462-5822.2011.01606.x
    • Beaufort N, Corvazier E, Hervieu A, Choqueux C, Dussiot M, et al. (2011) The thermolysin-like metalloproteinase and virulence factor LasB from pathogenic Pseudomonas aeruginosa induces anoikis of human vascular cells. Cell Microbiol 13: 1149-1167. doi:10.1111/j.1462-5822.2011.01606.x. PubMed: 21501369.
    • (2011) Cell Microbiol , vol.13 , pp. 1149-1167
    • Beaufort, N.1    Corvazier, E.2    Hervieu, A.3    Choqueux, C.4    Dussiot, M.5
  • 30
    • 0029612321 scopus 로고
    • The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa
    • doi:10.1111/j.1365-2958.1995.18050877.x
    • McIver KS, Kessler E, Olson JC, Ohman DE, (1995) The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa. Mol Microbiol 18: 877-889. doi:10.1111/j.1365-2958.1995.18050877.x. PubMed: 8825092.
    • (1995) Mol Microbiol , vol.18 , pp. 877-889
    • McIver, K.S.1    Kessler, E.2    Olson, J.C.3    Ohman, D.E.4
  • 31
    • 18244426126 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa virulence factors delay airway epithelial wound repair by altering the actin cytoskeleton and inducing overactivation of epithelial matrix metalloproteinase-2
    • doi:10.1038/labinvest.3780024
    • de Bentzmann S, Polette M, Zahm JM, Hinnrasky J, Kileztky C, et al. (2000) Pseudomonas aeruginosa virulence factors delay airway epithelial wound repair by altering the actin cytoskeleton and inducing overactivation of epithelial matrix metalloproteinase-2. Lab Invest 80: 209-219. doi:10.1038/labinvest.3780024. PubMed: 10701690.
    • (2000) Lab Invest , vol.80 , pp. 209-219
    • de Bentzmann, S.1    Polette, M.2    Zahm, J.M.3    Hinnrasky, J.4    Kileztky, C.5
  • 32
    • 77954918983 scopus 로고    scopus 로고
    • Activation of human pro-urokinase by unrelated proteases secreted by Pseudomonas aeruginosa
    • doi:10.1042/BJ20091806
    • Beaufort N, Seweryn P, de Bentzmann S, Tang A, Kellermann J, et al. (2010) Activation of human pro-urokinase by unrelated proteases secreted by Pseudomonas aeruginosa. Biochem J 428: 473-482. doi:10.1042/BJ20091806. PubMed: 20337595.
    • (2010) Biochem J , vol.428 , pp. 473-482
    • Beaufort, N.1    Seweryn, P.2    de Bentzmann, S.3    Tang, A.4    Kellermann, J.5
  • 33
    • 0035869555 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa protease IV enzyme assays and comparison to other Pseudomonas proteases
    • doi:10.1006/abio.2001.4999
    • Caballero AR, Moreau JM, Engel LS, Marquart ME, Hill et al,. (2001) Pseudomonas aeruginosa protease IV enzyme assays and comparison to other Pseudomonas proteases. Anal Biochem 290: 330-337. doi:10.1006/abio.2001.4999. PubMed: 11237336.
    • (2001) Anal Biochem , vol.290 , pp. 330-337
    • Caballero, A.R.1    Moreau, J.M.2    Engel, L.S.3    Marquart, M.E.4    Hill5
  • 34
    • 27744460321 scopus 로고    scopus 로고
    • Blood-brain barrier-specific properties of a human adult brain endothelial cell line
    • Weksler BB, Subileau EA, Perrière N, Charneau P, Holloway K, et al. (2005) Blood-brain barrier-specific properties of a human adult brain endothelial cell line. FASEB J 19: 1872-1874. PubMed: 16141364.
    • (2005) FASEB J , vol.19 , pp. 1872-1874
    • Weksler, B.B.1    Subileau, E.A.2    Perrière, N.3    Charneau, P.4    Holloway, K.5
  • 35
    • 33751191637 scopus 로고    scopus 로고
    • Blockade of αvβ3 and αvβ5 integrins by RGD mimetics induces anoikis and not integrin-mediated death in human endothelial cells
    • doi:10.1182/blood-2006-05-023580
    • Maubant S, Saint-Dizier D, Boutillon M, Perron-Sierra F, Casara PJ, et al. (2006) Blockade of αvβ3 and αvβ5 integrins by RGD mimetics induces anoikis and not integrin-mediated death in human endothelial cells. Blood 108: 3035-3044. doi:10.1182/blood-2006-05-023580. PubMed: 16835373.
    • (2006) Blood , vol.108 , pp. 3035-3044
    • Maubant, S.1    Saint-Dizier, D.2    Boutillon, M.3    Perron-Sierra, F.4    Casara, P.J.5
  • 36
    • 0035815747 scopus 로고    scopus 로고
    • Gene expression profile of antithrombotic protein C defines new mechanisms modulating inflammation and apoptosis
    • doi:10.1074/jbc.C100017200
    • Joyce DE, Gelbert L, Ciaccia A, DeHoff B, Grinnell BW, (2001) Gene expression profile of antithrombotic protein C defines new mechanisms modulating inflammation and apoptosis. J Biol Chem 276: 11199-11203. doi:10.1074/jbc.C100017200. PubMed: 11278252.
    • (2001) J Biol Chem , vol.276 , pp. 11199-11203
    • Joyce, D.E.1    Gelbert, L.2    Ciaccia, A.3    DeHoff, B.4    Grinnell, B.W.5
  • 37
    • 0030826772 scopus 로고    scopus 로고
    • Aprotinin reduces blood loss after cardiopulmonary bypass by direct inhibition of plasmin
    • Ray MJ, Marsh NA, (1997) Aprotinin reduces blood loss after cardiopulmonary bypass by direct inhibition of plasmin. Thromb Haemost 78: 1021-1026. PubMed: 9308747.
    • (1997) Thromb Haemost , vol.78 , pp. 1021-1026
    • Ray, M.J.1    Marsh, N.A.2
  • 38
    • 0035874516 scopus 로고    scopus 로고
    • Proteolysis of the urokinase-type plasminogen activator receptor by metalloproteinase-12: implication for angiogenesis in fibrin matrices
    • doi:10.1182/blood.V97.10.3123
    • Koolwijk P, Sidenius N, Peters E, Sier CFM, Hanemaaijer R, et al. (2001) Proteolysis of the urokinase-type plasminogen activator receptor by metalloproteinase-12: implication for angiogenesis in fibrin matrices. Blood 97: 3123-3131. doi:10.1182/blood.V97.10.3123. PubMed: 11342439.
    • (2001) Blood , vol.97 , pp. 3123-3131
    • Koolwijk, P.1    Sidenius, N.2    Peters, E.3    Sier, C.F.M.4    Hanemaaijer, R.5
  • 39
    • 0037097672 scopus 로고    scopus 로고
    • The immunostimulatory activity of the lung surfactant protein-A involves Toll-like receptor 4
    • Guillot L, Balloy V, McCormack FX, Golenbock DT, Chignard M, et al. (2002) The immunostimulatory activity of the lung surfactant protein-A involves Toll-like receptor 4. J Immunol 168: 5989-5992. PubMed: 12055204.
    • (2002) J Immunol , vol.168 , pp. 5989-5992
    • Guillot, L.1    Balloy, V.2    McCormack, F.X.3    Golenbock, D.T.4    Chignard, M.5
  • 40
    • 0025978352 scopus 로고
    • Control of growth and differentiation of vascular cells by extracellular matrix proteins
    • doi:10.1146/annurev.ph.53.030191.001113
    • Carey DJ, (1991) Control of growth and differentiation of vascular cells by extracellular matrix proteins. Annu Rev Physiol 53: 161-177. doi:10.1146/annurev.ph.53.030191.001113. PubMed: 2042957.
    • (1991) Annu Rev Physiol , vol.53 , pp. 161-177
    • Carey, D.J.1
  • 42
    • 0032724684 scopus 로고    scopus 로고
    • Structure and function of von Willebrand factor
    • Ruggeri ZM, (1999) Structure and function of von Willebrand factor. Thromb Haemost 82: 576-584. PubMed: 10605754.
    • (1999) Thromb Haemost , vol.82 , pp. 576-584
    • Ruggeri, Z.M.1
  • 43
    • 0021337951 scopus 로고
    • von Willebrand protein binds to extracellular matrices independently of collagen
    • doi:10.1073/pnas.81.2.471
    • Wagner DD, Urban-Pickering M, Marder VJ, (1984) von Willebrand protein binds to extracellular matrices independently of collagen. Proc Natl Acad Sci U S A 81: 471-475. doi:10.1073/pnas.81.2.471. PubMed: 6320190.
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 471-475
    • Wagner, D.D.1    Urban-Pickering, M.2    Marder, V.J.3
  • 44
    • 21244505889 scopus 로고    scopus 로고
    • Extracellular matrix remodeling by human granzyme B via cleavage of vitronectin, fibronectin, and laminin
    • doi:10.1074/jbc.M412001200
    • Buzza MS, Zamurs L, Sun J, Bird CH, Smith AI, et al. (2005) Extracellular matrix remodeling by human granzyme B via cleavage of vitronectin, fibronectin, and laminin. J Biol Chem 280: 23549-23558. doi:10.1074/jbc.M412001200. PubMed: 15843372.
    • (2005) J Biol Chem , vol.280 , pp. 23549-23558
    • Buzza, M.S.1    Zamurs, L.2    Sun, J.3    Bird, C.H.4    Smith, A.I.5
  • 45
    • 0031867833 scopus 로고    scopus 로고
    • Cleavage of β-catenin and plakoglobin and shedding of VE-cadherin durin endothelial apoptosis: evidence for a role of caspases and metalloproteinases
    • doi:10.1091/mbc.9.6.1589
    • Herren B, Levkau B, Raines EW, Ross R, (1998) Cleavage of β-catenin and plakoglobin and shedding of VE-cadherin durin endothelial apoptosis: evidence for a role of caspases and metalloproteinases. Mol Biol Cell 9: 1589-1601. doi:10.1091/mbc.9.6.1589. PubMed: 9614196.
    • (1998) Mol Biol Cell , vol.9 , pp. 1589-1601
    • Herren, B.1    Levkau, B.2    Raines, E.W.3    Ross, R.4
  • 46
    • 38449120854 scopus 로고    scopus 로고
    • Importance of snake venom metalloproteinases in cell biology: effects on platelets, inflammatory and endothelial cells
    • doi:10.2174/138161207782023711
    • Moura-da-Silva AM, Butera D, Tanjoni I, (2007) Importance of snake venom metalloproteinases in cell biology: effects on platelets, inflammatory and endothelial cells. Curr Pharm Des 13: 2893-2905. doi:10.2174/138161207782023711. PubMed: 17979734.
    • (2007) Curr Pharm Des , vol.13 , pp. 2893-2905
    • Moura-da-Silva, A.M.1    Butera, D.2    Tanjoni, I.3
  • 47
    • 77954054834 scopus 로고    scopus 로고
    • Neisseria meningitides induces brain microvascular endothelial cell detachment from the matrix and cleavage of occludin: a role of MMP-8
    • Schubert-Unkmeir A, Konrad C, Slanina H, Czapek F, Hebling S, et al. (2010) Neisseria meningitides induces brain microvascular endothelial cell detachment from the matrix and cleavage of occludin: a role of MMP-8. PLOS Pathog 6: e1000874.
    • (2010) PLOS Pathog , vol.6
    • Schubert-Unkmeir, A.1    Konrad, C.2    Slanina, H.3    Czapek, F.4    Hebling, S.5
  • 48
    • 38549128935 scopus 로고    scopus 로고
    • VE-cadherin. The major endothelial adhesion molecule controlling cellular junctions and blood vessel formation
    • Vestweber D, (2008) VE-cadherin. The major endothelial adhesion molecule controlling cellular junctions and blood vessel formation. Arterioscler Thromb Vasc Biol 28: 223-232. PubMed: 18162609.
    • (2008) Arterioscler Thromb Vasc Biol , vol.28 , pp. 223-232
    • Vestweber, D.1
  • 49
    • 59649092177 scopus 로고    scopus 로고
    • The control of vascular integrity by endothelial cell junctions: molecular basis and pathological implications
    • doi:10.1016/j.devcel.2009.01.004
    • Dejana E, Tournier-Lasserve E, Weinstein BM, (2009) The control of vascular integrity by endothelial cell junctions: molecular basis and pathological implications. Dev Cell 16: 209-221. doi:10.1016/j.devcel.2009.01.004. PubMed: 19217423.
    • (2009) Dev Cell , vol.16 , pp. 209-221
    • Dejana, E.1    Tournier-Lasserve, E.2    Weinstein, B.M.3
  • 50
    • 84855274887 scopus 로고    scopus 로고
    • Soluble VE-cadherin in rheumatoid arthritis patients correlates with disease activity
    • doi:10.1002/art.33336
    • Sidibé A, Mannic T, Arboleas M, Subileau M, Gulino-Debrac D, et al. (2012) Soluble VE-cadherin in rheumatoid arthritis patients correlates with disease activity. Arthritis Rheum 64: 77-87. doi:10.1002/art.33336. PubMed: 21905018.
    • (2012) Arthritis Rheum , vol.64 , pp. 77-87
    • Sidibé, A.1    Mannic, T.2    Arboleas, M.3    Subileau, M.4    Gulino-Debrac, D.5
  • 51
    • 0038820001 scopus 로고    scopus 로고
    • Mechanisms of VE-cadherin processing and degradation in microvascular endothelial cells
    • doi:10.1074/jbc.M211746200
    • Xiao K, Allison DF, Kottke MD, Summers S, Sorescu GP, et al. (2003) Mechanisms of VE-cadherin processing and degradation in microvascular endothelial cells. J Biol Chem 278: 19199-19208. doi:10.1074/jbc.M211746200. PubMed: 12626512.
    • (2003) J Biol Chem , vol.278 , pp. 19199-19208
    • Xiao, K.1    Allison, D.F.2    Kottke, M.D.3    Summers, S.4    Sorescu, G.P.5
  • 52
    • 2942580900 scopus 로고    scopus 로고
    • The specific fates of tight junction proteins in apoptotic epithelial cells
    • doi:10.1242/jcs.01071
    • Bojarski C, Weiske J, Schöneberg T, Schröder W, Mankertz J, et al. (2004) The specific fates of tight junction proteins in apoptotic epithelial cells. J Cell Sci 117: 2097-2107. doi:10.1242/jcs.01071. PubMed: 15054114.
    • (2004) J Cell Sci , vol.117 , pp. 2097-2107
    • Bojarski, C.1    Weiske, J.2    Schöneberg, T.3    Schröder, W.4    Mankertz, J.5
  • 53
    • 33947493391 scopus 로고    scopus 로고
    • Matrix metalloproteinase-mediated disruption of tight junction proteins in cerebral vessels is reversed by synthetic matrix metalloproteinase inhibitor in focal ischemia in rat
    • Yang Y, Estrada EY, Thompson JF, Liu W, Rosenberg GA, (2007) Matrix metalloproteinase-mediated disruption of tight junction proteins in cerebral vessels is reversed by synthetic matrix metalloproteinase inhibitor in focal ischemia in rat. J Cereb Blood Flow Metab 27: 697-709. PubMed: 16850029.
    • (2007) J Cereb Blood Flow Metab , vol.27 , pp. 697-709
    • Yang, Y.1    Estrada, E.Y.2    Thompson, J.F.3    Liu, W.4    Rosenberg, G.A.5
  • 54
    • 33746797624 scopus 로고    scopus 로고
    • Vascular integrins in tumor angiogenesis: mediators and therapeutic targets
    • doi:10.1080/10623320600698037
    • Alghisi GC, Rüegg C, (2006) Vascular integrins in tumor angiogenesis: mediators and therapeutic targets. Endothelium 13: 113-135. doi:10.1080/10623320600698037. PubMed: 16728329.
    • (2006) Endothelium , vol.13 , pp. 113-135
    • Alghisi, G.C.1    Rüegg, C.2
  • 55
    • 33947321575 scopus 로고    scopus 로고
    • uPAR - uPA - PAI-1 interactions and signaling: a vascular biologist's view
    • Binder BR, Mihaly J, Prager GW, (2007) uPAR - uPA - PAI-1 interactions and signaling: a vascular biologist's view. Thromb Haemost 97: 336-342. PubMed: 17334498.
    • (2007) Thromb Haemost , vol.97 , pp. 336-342
    • Binder, B.R.1    Mihaly, J.2    Prager, G.W.3
  • 56
    • 77951883821 scopus 로고    scopus 로고
    • The urokinase receptor: focused cell surface proteolysis, cell adhesion and signaling
    • doi:10.1016/j.febslet.2009.12.039
    • Blasi F, Sidenius N, (2010) The urokinase receptor: focused cell surface proteolysis, cell adhesion and signaling. FEBS Lett 584: 1923-1930. doi:10.1016/j.febslet.2009.12.039. PubMed: 20036661.
    • (2010) FEBS Lett , vol.584 , pp. 1923-1930
    • Blasi, F.1    Sidenius, N.2
  • 57
    • 72949116366 scopus 로고    scopus 로고
    • Regulation of cell signalling by uPAR
    • doi:10.1038/nrm2821
    • Smith HW, Marshall CJ, (2010) Regulation of cell signalling by uPAR. Nat Rev Mol Cell Biol 11: 23-36. doi:10.1038/nrm2821. PubMed: 20027185.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 23-36
    • Smith, H.W.1    Marshall, C.J.2
  • 58
    • 78149486483 scopus 로고    scopus 로고
    • Mechanisms by which cleaved kininogen inhibits endothelial cell differentiation and signaling
    • doi:10.1160/TH10-01-0017
    • Colman RW, Wu Y, Liu Y, (2010) Mechanisms by which cleaved kininogen inhibits endothelial cell differentiation and signaling. Thromb Haemost 104: 875-885. doi:10.1160/TH10-01-0017. PubMed: 20886177.
    • (2010) Thromb Haemost , vol.104 , pp. 875-885
    • Colman, R.W.1    Wu, Y.2    Liu, Y.3
  • 59
    • 33745841867 scopus 로고    scopus 로고
    • Urokinase signaling through its receptor protects against anoikis by increasing BCL-xL expression levels
    • doi:10.1074/jbc.M601812200
    • Alfano D, Iaccarino I, Stoppelli MP, (2006) Urokinase signaling through its receptor protects against anoikis by increasing BCL-xL expression levels. J Biol Chem 281: 17758-17767. doi:10.1074/jbc.M601812200. PubMed: 16632475.
    • (2006) J Biol Chem , vol.281 , pp. 17758-17767
    • Alfano, D.1    Iaccarino, I.2    Stoppelli, M.P.3
  • 60
    • 60849136639 scopus 로고    scopus 로고
    • Urokinase mediates endothelial cell survival via induction of the X-linked inhibitor of apoptosis protein
    • doi:10.1182/blood-2008-06-164210
    • Prager GW, Mihaly J, Brunner PM, Koshelnick Y, Hoyer-Hansen G, et al. (2009) Urokinase mediates endothelial cell survival via induction of the X-linked inhibitor of apoptosis protein. Blood 113: 1383-1390. doi:10.1182/blood-2008-06-164210. PubMed: 18948573.
    • (2009) Blood , vol.113 , pp. 1383-1390
    • Prager, G.W.1    Mihaly, J.2    Brunner, P.M.3    Koshelnick, Y.4    Hoyer-Hansen, G.5
  • 61
    • 0035954232 scopus 로고    scopus 로고
    • Proteolysis of integrin α5 and β1 subunits involved in retinoic acid-induced apoptosis in human hepatoma Hep3B cells
    • doi:10.1016/S0304-3835(01)00479-7
    • Hsu SL, Cheng CC, Shi YR, Chiang CW, (2001) Proteolysis of integrin α5 and β1 subunits involved in retinoic acid-induced apoptosis in human hepatoma Hep3B cells. Cancer Lett 167: 193-204. doi:10.1016/S0304-3835(01)00479-7. PubMed: 11369141.
    • (2001) Cancer Lett , vol.167 , pp. 193-204
    • Hsu, S.L.1    Cheng, C.C.2    Shi, Y.R.3    Chiang, C.W.4
  • 62
    • 42049087603 scopus 로고    scopus 로고
    • Diverse type III secretion phenotypes among Pseudomonas aeruginosa strains upon infection of murine macrophage-like and endothelial cell lines
    • doi:10.1016/j.micpath.2007.11.008
    • Stepińska M, Trafny EA, (2008) Diverse type III secretion phenotypes among Pseudomonas aeruginosa strains upon infection of murine macrophage-like and endothelial cell lines. Microb Pathog 44: 448-458. doi:10.1016/j.micpath.2007.11.008. PubMed: 18221854.
    • (2008) Microb Pathog , vol.44 , pp. 448-458
    • Stepińska, M.1    Trafny, E.A.2
  • 63
    • 0036400645 scopus 로고    scopus 로고
    • Type III secretion-mediated killing of endothelial cells by Pseudomonas aeruginosa
    • Mattos Saliba A, Filloux A, Ball G, Silva ASV, Assis M-C, et al. (2009) Type III secretion-mediated killing of endothelial cells by Pseudomonas aeruginosa. Microb Pathog 33: 153-166.
    • (2009) Microb Pathog , vol.33 , pp. 153-166
    • Mattos Saliba, A.1    Filloux, A.2    Ball, G.3    Silva, A.S.V.4    Assis, M.-C.5
  • 64
    • 0036433010 scopus 로고    scopus 로고
    • Kinetics of thrombomodulin release and endothelial cell injury by neutrophil-derived proteases and oxygen radicals
    • doi:10.1046/j.1365-2567.2002.01469.x
    • Boehme MWJ, Galle P, Stremmel W, (2002) Kinetics of thrombomodulin release and endothelial cell injury by neutrophil-derived proteases and oxygen radicals. Immunology 107: 340-349. doi:10.1046/j.1365-2567.2002.01469.x. PubMed: 12423310.
    • (2002) Immunology , vol.107 , pp. 340-349
    • Boehme, M.W.J.1    Galle, P.2    Stremmel, W.3
  • 65
    • 0021783941 scopus 로고
    • Evidence that Pseudomonas aeruginosa elastase does not inactivate the bronchial inhibitor in the presence of leukocyte elastase
    • Tournier J-M, Jacquot J, Puchelle E, Bieth JG, (1985) Evidence that Pseudomonas aeruginosa elastase does not inactivate the bronchial inhibitor in the presence of leukocyte elastase. Am Rev Respir Dis 132: 524-528. PubMed: 2412473.
    • (1985) Am Rev Respir Dis , vol.132 , pp. 524-528
    • Tournier, J.-M.1    Jacquot, J.2    Puchelle, E.3    Bieth, J.G.4
  • 66
    • 33645746818 scopus 로고    scopus 로고
    • High urokinase expression contributes to the angiogenic properties of endothelial cells derived from circulating progenitors
    • Basire A, Sabatier F, Ravet S, Lamy E, Mialhe A, et al. (2006) High urokinase expression contributes to the angiogenic properties of endothelial cells derived from circulating progenitors. Thromb Haemost 95: 678-688. PubMed: 16601839.
    • (2006) Thromb Haemost , vol.95 , pp. 678-688
    • Basire, A.1    Sabatier, F.2    Ravet, S.3    Lamy, E.4    Mialhe, A.5
  • 67
    • 0027451706 scopus 로고
    • The extracellular matrix as a cell survival factor
    • doi:10.1091/mbc.4.9.953
    • Meredith JE Jr, Fazeli B, Schwartz MA, (1993) The extracellular matrix as a cell survival factor. Mol Biol Cell 4: 953-961. doi:10.1091/mbc.4.9.953. PubMed: 8257797.
    • (1993) Mol Biol Cell , vol.4 , pp. 953-961
    • Meredith Jr., J.E.1    Fazeli, B.2    Schwartz, M.A.3
  • 68
    • 44349186815 scopus 로고    scopus 로고
    • Degradation of circulating von Willebrand factor and its regulator ADAMTS13 implicates secreted Bacillus anthracis metalloproteases in anthrax consumptive coagulopathy
    • doi:10.1074/jbc.M705871200
    • Chung M-C, Popova TG, Jorgensen SC, Dong L, Chandhoke V, et al. (2008) Degradation of circulating von Willebrand factor and its regulator ADAMTS13 implicates secreted Bacillus anthracis metalloproteases in anthrax consumptive coagulopathy. J Biol Chem 283: 9531-9542. doi:10.1074/jbc.M705871200. PubMed: 18263586.
    • (2008) J Biol Chem , vol.283 , pp. 9531-9542
    • Chung, M.-C.1    Popova, T.G.2    Jorgensen, S.C.3    Dong, L.4    Chandhoke, V.5
  • 69
    • 0037853133 scopus 로고    scopus 로고
    • Identification of proteases involved in the proteolysis of vascular endothelium cadherin during neutrophil transmigration
    • doi:10.1074/jbc.M300351200
    • Hermant B, Bibert S, Concord E, Dublet B, Weidenhaupt M, et al V,. (2003) Identification of proteases involved in the proteolysis of vascular endothelium cadherin during neutrophil transmigration. J Biol Chem 278: 14002-14012. doi:10.1074/jbc.M300351200. PubMed: 12584200.
    • (2003) J Biol Chem , vol.278 , pp. 14002-14012
    • Hermant, B.1    Bibert, S.2    Concord, E.3    Dublet, B.4    Weidenhaupt, M.5
  • 70
    • 55849124698 scopus 로고    scopus 로고
    • The interaction of Streptocccus pneumoniae with plasmin mediates transmigration across endothelial and epithelial monolayers by intercellular junction cleavage
    • doi:10.1128/IAI.00184-08
    • Attali C, Durmort C, Vernet T, Di Guilmi A-M, (2008) The interaction of Streptocccus pneumoniae with plasmin mediates transmigration across endothelial and epithelial monolayers by intercellular junction cleavage. Infect Immun 76: 5350-5356. doi:10.1128/IAI.00184-08. PubMed: 18725422.
    • (2008) Infect Immun , vol.76 , pp. 5350-5356
    • Attali, C.1    Durmort, C.2    Vernet, T.3    Di Guilmi, A.-M.4
  • 71
    • 33646908499 scopus 로고    scopus 로고
    • Rhamnolipids are virulence factors that promote early infiltration of primary human airway epithelia by Pseudomonas aeruginosa
    • doi:10.1128/IAI.01772-05
    • Zulianello L, Canard C, Köhler T, Caille D, Lacroix J-S, et al. (2006) Rhamnolipids are virulence factors that promote early infiltration of primary human airway epithelia by Pseudomonas aeruginosa. Infect Immun 74: 3134-3147. doi:10.1128/IAI.01772-05. PubMed: 16714541.
    • (2006) Infect Immun , vol.74 , pp. 3134-3147
    • Zulianello, L.1    Canard, C.2    Köhler, T.3    Caille, D.4    Lacroix, J.-S.5
  • 72
    • 67249164000 scopus 로고    scopus 로고
    • A complex extracellular sphingomyelinase of Pseudomonas aeruginosa inhibits angiogenesis by selective cytotoxicity to endothelial cells
    • Vasil ML, Stonehouse MJ, Vasil AI, Wadsworth SJ, Goldfine H, et al. (2009) A complex extracellular sphingomyelinase of Pseudomonas aeruginosa inhibits angiogenesis by selective cytotoxicity to endothelial cells. PLOS Pathog 5(5):: e1000420. PubMed: 19424430.
    • (2009) PLOS Pathog , vol.5
    • Vasil, M.L.1    Stonehouse, M.J.2    Vasil, A.I.3    Wadsworth, S.J.4    Goldfine, H.5
  • 73
    • 33750335819 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa type III-secreted toxin ExoT inhibits host-cell division by targeting cytokinesis at multiple steps
    • doi:10.1073/pnas.0605949103
    • Shafikhani SH, Engel J, (2006) Pseudomonas aeruginosa type III-secreted toxin ExoT inhibits host-cell division by targeting cytokinesis at multiple steps. Proc Natl Acad Sci U S A 103: 15605-15610. doi:10.1073/pnas.0605949103. PubMed: 17030800.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 15605-15610
    • Shafikhani, S.H.1    Engel, J.2


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