메뉴 건너뛰기




Volumn 6, Issue , 2006, Pages

Acceleration of epithelial cell syndecan-1 shedding by anthrax hemolytic virulence factors

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN KINASE SYK; STRESS ACTIVATED PROTEIN KINASE; SYNDECAN 1; UVOMORULIN; VIRULENCE FACTOR; ANTHRAX TOXIN; BACTERIAL ANTIGEN; BACTERIAL TOXIN; CADHERIN; HEMOLYSIN; LACTATE DEHYDROGENASE; PHOSPHATIDYLCHOLINE SPECIFIC PHOSPHOLIPASE C; PHOSPHATIDYLCHOLINE-SPECIFIC PHOSPHOLIPASE C; PHOSPHOLIPASE C; SPHINGOMYELIN PHOSPHODIESTERASE;

EID: 33644648573     PISSN: 14712180     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-6-8     Document Type: Article
Times cited : (45)

References (52)
  • 2
    • 0035799627 scopus 로고    scopus 로고
    • Exploitation of syndecan-1 shedding by Pseudomonas aeruginosa enhances virulence
    • Park PW, Pier GB, Hinkes MT, Bernfield M: Exploitation of syndecan-1 shedding by Pseudomonas aeruginosa enhances virulence. Nature 2001, 411:98-102.
    • (2001) Nature , vol.411 , pp. 98-102
    • Park, P.W.1    Pier, G.B.2    Hinkes, M.T.3    Bernfield, M.4
  • 3
    • 0345791535 scopus 로고    scopus 로고
    • Activation of syndecan-1 ectodomain shedding by Staphylococcus aureus alpha-toxin and beta-toxin
    • Park PW, Foster TJ, Nishi E, Duncan SJ, Klagsbrun M, Chen Y: Activation of syndecan-1 ectodomain shedding by Staphylococcus aureus alpha-toxin and beta-toxin. J Biol Chem 2004, 279:251-258.
    • (2004) J Biol Chem , vol.279 , pp. 251-258
    • Park, P.W.1    Foster, T.J.2    Nishi, E.3    Duncan, S.J.4    Klagsbrun, M.5    Chen, Y.6
  • 5
    • 0034695918 scopus 로고    scopus 로고
    • Shedding of syndecan-1 and -4 ectodomains is regulated by multiple signaling pathways and mediated by a TIMP-3-sensitive metalloproteinase
    • Fitzgerald ML, Wang Z, Park PW, Murphy G, Bernfield M: Shedding of syndecan-1 and -4 ectodomains is regulated by multiple signaling pathways and mediated by a TIMP-3-sensitive metalloproteinase. J Cell Biol 2000, 148:811-824.
    • (2000) J Cell Biol , vol.148 , pp. 811-824
    • Fitzgerald, M.L.1    Wang, Z.2    Park, P.W.3    Murphy, G.4    Bernfield, M.5
  • 9
    • 0031768024 scopus 로고    scopus 로고
    • Matrix metalloproteinases in cerebrovascular disease
    • Mun-Bryce S, Rosenberg GA: Matrix metalloproteinases in cerebrovascular disease. J Cereb Blood Flow Metab 1998, 18:1163-1172.
    • (1998) J Cereb Blood Flow Metab , vol.18 , pp. 1163-1172
    • Mun-Bryce, S.1    Rosenberg, G.A.2
  • 15
    • 0028174030 scopus 로고
    • NIH 3T3 cells stably transfected with the gene encoding phosphatidylcholine-hydrolyzing phospholipase C from Bacillus cereus acquire a transformed phenotype
    • Johansen T, Bjorkoy G, Overvatn A, Diaz-Meco MT, Traavik T, Moscat J: NIH 3T3 cells stably transfected with the gene encoding phosphatidylcholine- hydrolyzing phospholipase C from Bacillus cereus acquire a transformed phenotype. J Mol Cell Biol 1994, 14:646-654.
    • (1994) J Mol Cell Biol , vol.14 , pp. 646-654
    • Johansen, T.1    Bjorkoy, G.2    Overvatn, A.3    Diaz-Meco, M.T.4    Traavik, T.5    Moscat, J.6
  • 16
    • 0034999680 scopus 로고    scopus 로고
    • Exogenous phospholipase C stimulates epithelial cell migration and integrin expression in vitro
    • Firth JD, Putnins EE, Larjava H, Uitto VJ: Exogenous phospholipase C stimulates epithelial cell migration and integrin expression in vitro. Wound Repair Regen 2001, 9:86-94.
    • (2001) Wound Repair Regen , vol.9 , pp. 86-94
    • Firth, J.D.1    Putnins, E.E.2    Larjava, H.3    Uitto, V.J.4
  • 17
    • 1242351553 scopus 로고    scopus 로고
    • The roles of anthrax toxin in pathogenesis
    • Moayeri M, Leppla SH: The roles of anthrax toxin in pathogenesis. Curr Opin Microbiol 2004, 7:19-24.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 19-24
    • Moayeri, M.1    Leppla, S.H.2
  • 19
    • 85047692288 scopus 로고    scopus 로고
    • Bacillus anthracis lethal toxin induces TNF-alpha-independent hypoxia-mediated toxicity in mice
    • Moayeri M, Haines D, Young HA, Leppla SH: Bacillus anthracis lethal toxin induces TNF-alpha-independent hypoxia-mediated toxicity in mice. J Clin Invest 2003, 112:670-682.
    • (2003) J Clin Invest , vol.112 , pp. 670-682
    • Moayeri, M.1    Haines, D.2    Young, H.A.3    Leppla, S.H.4
  • 20
    • 0014127332 scopus 로고
    • Anthrax toxic complex
    • Smith H, Stoner HB: Anthrax toxic complex. Fed Proc 1967, 26:1554-1557.
    • (1967) Fed Proc , vol.26 , pp. 1554-1557
    • Smith, H.1    Stoner, H.B.2
  • 21
    • 19544371576 scopus 로고    scopus 로고
    • Anthrax lethal toxin induces endothelial barrier dysfunction
    • Warfel JM, Steele AD, D'Agnillo F: Anthrax lethal toxin induces endothelial barrier dysfunction. Am J Pathol 2005, 166:1871-1881.
    • (2005) Am J Pathol , vol.166 , pp. 1871-1881
    • Warfel, J.M.1    Steele, A.D.2    D'Agnillo, F.3
  • 23
    • 0346251030 scopus 로고    scopus 로고
    • Anthrax lethal toxin induces human endothelial cell apoptosis
    • Kirby JE: Anthrax lethal toxin induces human endothelial cell apoptosis. Infect Immun 2004, 72:430-439.
    • (2004) Infect Immun , vol.72 , pp. 430-439
    • Kirby, J.E.1
  • 24
    • 13844318262 scopus 로고    scopus 로고
    • Differentiation of human monocytic cell lines confers susceptibility to Bacillus anthracis lethal toxin
    • Kassam A, Der SD, Mogridge J: Differentiation of human monocytic cell lines confers susceptibility to Bacillus anthracis lethal toxin. Cell Microbiol 2005, 7:281-292.
    • (2005) Cell Microbiol , vol.7 , pp. 281-292
    • Kassam, A.1    Der, S.D.2    Mogridge, J.3
  • 25
    • 17844397159 scopus 로고    scopus 로고
    • Endocytosis of the apical junctional complex: Mechanisms and possible roles in regulation of epithelial barriers
    • Ivanov AI, Nusrat A, Parkos CA: Endocytosis of the apical junctional complex: mechanisms and possible roles in regulation of epithelial barriers. Bioessays 2005, 27:356-365.
    • (2005) Bioessays , vol.27 , pp. 356-365
    • Ivanov, A.I.1    Nusrat, A.2    Parkos, C.A.3
  • 26
    • 0036882397 scopus 로고    scopus 로고
    • Protein ectodomain shedding
    • Arribas J, Borroto A: Protein ectodomain shedding. Chem Rev 2002, 102:4627-4638.
    • (2002) Chem Rev , vol.102 , pp. 4627-4638
    • Arribas, J.1    Borroto, A.2
  • 27
    • 1542269021 scopus 로고    scopus 로고
    • Tyrosine kinase inhibitors: A new approach for asthma
    • Wong WS, Leong KP: Tyrosine kinase inhibitors: a new approach for asthma. Biochim Biophys Acta 2004, 1697:53-69.
    • (2004) Biochim Biophys Acta , vol.1697 , pp. 53-69
    • Wong, W.S.1    Leong, K.P.2
  • 28
    • 0037458567 scopus 로고    scopus 로고
    • Syk, a protein-tyrosine kinase, suppresses the cell motility and nuclear factor kappa Bmediated secretion of urokinase type plasminogen activator by inhibiting the phosphatidylinositol 3′-kinase activity in breast cancer cells
    • Mahabeleshwar GH, Kundu GC: Syk, a protein-tyrosine kinase, suppresses the cell motility and nuclear factor kappa Bmediated secretion of urokinase type plasminogen activator by inhibiting the phosphatidylinositol 3′-kinase activity in breast cancer cells. J Biol Chem 2003, 278:6209-6221.
    • (2003) J Biol Chem , vol.278 , pp. 6209-6221
    • Mahabeleshwar, G.H.1    Kundu, G.C.2
  • 29
    • 0031754497 scopus 로고    scopus 로고
    • Receptors for purines and pyrimidines
    • Ralevic V, Burnstock G: Receptors for purines and pyrimidines. Pharmacol Rev 1998, 50:413-92.
    • (1998) Pharmacol Rev , vol.50 , pp. 413-492
    • Ralevic, V.1    Burnstock, G.2
  • 30
    • 0036007414 scopus 로고    scopus 로고
    • Shedding light on sheddases: Role in growth and development
    • Keradmand F, Werb Z: Shedding light on sheddases: role in growth and development. BioEssays 2002, 24:8-12.
    • (2002) BioEssays , vol.24 , pp. 8-12
    • Keradmand, F.1    Werb, Z.2
  • 31
    • 0032524855 scopus 로고    scopus 로고
    • Suramin is an active site-directed, reversible, and tight-binding inhibitor of protein-tyrosine phosphatases
    • Zhang YL, Keng YF, Zhao Y, Wu L, Zhang ZY: Suramin is an active site-directed, reversible, and tight-binding inhibitor of protein-tyrosine phosphatases. J Biol Chem 1998, 15:12281-12287.
    • (1998) J Biol Chem , vol.15 , pp. 12281-12287
    • Zhang, Y.L.1    Keng, Y.F.2    Zhao, Y.3    Wu, L.4    Zhang, Z.Y.5
  • 32
    • 17844403782 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases and signalling
    • Stoker AW: Protein tyrosine phosphatases and signalling. J Endocrinol 2005, 185:19-33.
    • (2005) J Endocrinol , vol.185 , pp. 19-33
    • Stoker, A.W.1
  • 34
    • 11844262784 scopus 로고    scopus 로고
    • Anthrolysin O and other Gram-positive cytolysins are Toll-like receptor agonists
    • Park JM, Ng VH, Maeda S, Rest RF, Karin M: Anthrolysin O and other Gram-positive cytolysins are Toll-like receptor agonists. J Exp Med 2004, 200:1647-1655.
    • (2004) J Exp Med , vol.200 , pp. 1647-1655
    • Park, J.M.1    Ng, V.H.2    Maeda, S.3    Rest, R.F.4    Karin, M.5
  • 37
    • 0036144712 scopus 로고    scopus 로고
    • Mechanical stress regulates syndecan-4 expression and redistribution in vascular smooth muscle cells
    • Li L, Chaikof EL: Mechanical stress regulates syndecan-4 expression and redistribution in vascular smooth muscle cells. Arterioscler Thromb Vasc Biol 2002, 22:61-68.
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , pp. 61-68
    • Li, L.1    Chaikof, E.L.2
  • 38
    • 22744450061 scopus 로고    scopus 로고
    • ADAM-mediated ectodomain shedding of HB-EGF in receptor cross-talk
    • Higashiyama S, Nanba D: ADAM-mediated ectodomain shedding of HB-EGF in receptor cross-talk. Biochim Biophys Acta 2005, 1751:110-117.
    • (2005) Biochim Biophys Acta , vol.1751 , pp. 110-117
    • Higashiyama, S.1    Nanba, D.2
  • 39
    • 19544366809 scopus 로고    scopus 로고
    • Oxidative stress and 8-iso-prostaglandin F(2alpha) induce ectodomain shedding of CD163 and release of tumor necrosis factor-alpha from human monocytes
    • Timmermann M, Hogger P: Oxidative stress and 8-iso-prostaglandin F(2alpha) induce ectodomain shedding of CD163 and release of tumor necrosis factor-alpha from human monocytes. Free Radic Biol Med 2005, 39:98-107.
    • (2005) Free Radic Biol Med , vol.39 , pp. 98-107
    • Timmermann, M.1    Hogger, P.2
  • 40
    • 17844406602 scopus 로고    scopus 로고
    • Bacterial cytotoxins: Targeting eukaryotic switches
    • Aktories K, Barbieri JT: Bacterial cytotoxins: targeting eukaryotic switches. Nat Rev Microbiol 2005, 3:397-410.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 397-410
    • Aktories, K.1    Barbieri, J.T.2
  • 41
    • 0029005076 scopus 로고
    • Loss of cell surface syndecan-1 causes epithelia to transform into anchorageindependent mesenchyme-like cells
    • Kato M, Saunders S, Nguyen H, Bernfield M: Loss of cell surface syndecan-1 causes epithelia to transform into anchorageindependent mesenchyme-like cells. Mol Biol Cell 1995, 6:559-576.
    • (1995) Mol Biol Cell , vol.6 , pp. 559-576
    • Kato, M.1    Saunders, S.2    Nguyen, H.3    Bernfield, M.4
  • 42
    • 0000823104 scopus 로고
    • The chemical basis of the virulence of Bacillus anthracis. V. The specific toxin produced by B. anthracis in vivo
    • Smith H, Keppie J, Stanley JL: The chemical basis of the virulence of Bacillus anthracis. V. The specific toxin produced by B. anthracis in vivo. Br J Exp Pathol 1955, 36:460-472.
    • (1955) Br J Exp Pathol , vol.36 , pp. 460-472
    • Smith, H.1    Keppie, J.2    Stanley, J.L.3
  • 43
    • 0033257307 scopus 로고    scopus 로고
    • Correlation of the virulence of Bacillus anthracis with expression of signs, coded for by chromosomal genes
    • Mikshis NI, Eremin SA, Bolotnikova MF: Correlation of the virulence of Bacillus anthracis with expression of signs, coded for by chromosomal genes. Mol Gen Mikrobiol Virusol 1999, 4:25-28.
    • (1999) Mol Gen Mikrobiol Virusol , vol.4 , pp. 25-28
    • Mikshis, N.I.1    Eremin, S.A.2    Bolotnikova, M.F.3
  • 44
    • 0037767296 scopus 로고    scopus 로고
    • Characterization of anthrolysin O, the Bacillus anthracis cholesterol-dependent cytolysin
    • Shannon JG, Ross CL, Koehler TM, Rest RF: Characterization of anthrolysin O, the Bacillus anthracis cholesterol-dependent cytolysin. Infect Immun 2003, 71:3183-3189.
    • (2003) Infect Immun , vol.71 , pp. 3183-3189
    • Shannon, J.G.1    Ross, C.L.2    Koehler, T.M.3    Rest, R.F.4
  • 46
    • 4143128938 scopus 로고    scopus 로고
    • Role of CaMKII in hydrogen peroxide activation of ERK1/2, p38 MAPK, HSP27 and actin reorganization in endothelial cells
    • Nguyen A, Chen P, Cai H: Role of CaMKII in hydrogen peroxide activation of ERK1/2, p38 MAPK, HSP27 and actin reorganization in endothelial cells. FEBS Lett 2004, 572:307-313.
    • (2004) FEBS Lett , vol.572 , pp. 307-313
    • Nguyen, A.1    Chen, P.2    Cai, H.3
  • 48
    • 20444385832 scopus 로고    scopus 로고
    • Activation of p38 has opposing effects on the proliferation and migration of endothelial cells
    • McMullen ME, Bryant PW, Glembotski CC, Vincent PA, Pumiglia KM: Activation of p38 has opposing effects on the proliferation and migration of endothelial cells. J Biol Chem 2005, 280:20995-21003.
    • (2005) J Biol Chem , vol.280 , pp. 20995-21003
    • McMullen, M.E.1    Bryant, P.W.2    Glembotski, C.C.3    Vincent, P.A.4    Pumiglia, K.M.5
  • 49
    • 3342901591 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways defend against bacterial pore-forming toxins
    • Huffman DL, Abrami L, Sasik R, Corbeil J, Goot F, Aroian R: Mitogen-activated protein kinase pathways defend against bacterial pore-forming toxins. Proc Nat Acad Sci USA 2004, 101:10995-11000.
    • (2004) Proc Nat Acad Sci USA , vol.101 , pp. 10995-11000
    • Huffman, D.L.1    Abrami, L.2    Sasik, R.3    Corbeil, J.4    Goot, F.5    Aroian, R.6
  • 50
    • 0034844097 scopus 로고    scopus 로고
    • The role of p38 MAP kinase in hydrogen peroxide mediated endothelial solute permeability
    • Kevil CG, Oshima T, Alexander JS: The role of p38 MAP kinase in hydrogen peroxide mediated endothelial solute permeability. Endothelium 2001, 8:107-116.
    • (2001) Endothelium , vol.8 , pp. 107-116
    • Kevil, C.G.1    Oshima, T.2    Alexander, J.S.3
  • 51
    • 0142091353 scopus 로고    scopus 로고
    • Toxin-induced resistance in Bacillus anthracis lethal toxin-treated macrophages
    • Salles II, Tucker AE, Voth DE, Ballard JD: Toxin-induced resistance in Bacillus anthracis lethal toxin-treated macrophages. Proc Nat Acad Sci USA 2003, 100:12426-12431.
    • (2003) Proc Nat Acad Sci USA , vol.100 , pp. 12426-12431
    • Salles, I.I.1    Tucker, A.E.2    Voth, D.E.3    Ballard, J.D.4
  • 52
    • 0347994943 scopus 로고    scopus 로고
    • An endogenous pathway to systemic inflammatory response syndrome (SIRS)-like reactions through toll-like receptor 4
    • Johnson GB, Brunn GJ, Platt JL: An endogenous pathway to systemic inflammatory response syndrome (SIRS)-like reactions through toll-like receptor 4. J Immun 2004, 172:20-24.
    • (2004) J Immun , vol.172 , pp. 20-24
    • Johnson, G.B.1    Brunn, G.J.2    Platt, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.