메뉴 건너뛰기




Volumn 339, Issue 1, 2006, Pages 107-114

Inhibition of platelet aggregation by anthrax edema toxin

Author keywords

Bleeding time; Edema toxin; Hemorrhage; Platelet aggregation

Indexed keywords

ANTHRAX TOXIN;

EID: 28144431782     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.11.008     Document Type: Article
Times cited : (18)

References (40)
  • 3
    • 0000947082 scopus 로고
    • Anthrax toxin edema factor: A bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells
    • S.H. Leppla Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells Proc. Natl. Acad. Sci. USA 79 1982 3162 3166
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3162-3166
    • Leppla, S.H.1
  • 5
    • 0027930622 scopus 로고
    • Anthrax edema toxin differentially regulates lipopolysaccharide-induced monocyte production of tumor necrosis factor alpha and interleukin-6 by increasing intracellular cyclic AMP
    • D.L. Hoover, A.M. Friedlander, L.C. Rogers, I.K. Yoon, R.L. Warren, and A.S. Cross Anthrax edema toxin differentially regulates lipopolysaccharide- induced monocyte production of tumor necrosis factor alpha and interleukin-6 by increasing intracellular cyclic AMP Infect. Immun. 62 1994 4432 4439
    • (1994) Infect. Immun. , vol.62 , pp. 4432-4439
    • Hoover, D.L.1    Friedlander, A.M.2    Rogers, L.C.3    Yoon, I.K.4    Warren, R.L.5    Cross, A.S.6
  • 7
    • 0036719095 scopus 로고    scopus 로고
    • Anthrax edema toxin requires influx of calcium for inducing cyclic AMP toxicity in target cells
    • P. Kumar, N. Ahuja, and R. Bhatnagar Anthrax edema toxin requires influx of calcium for inducing cyclic AMP toxicity in target cells Infect. Immun. 70 2002 4997 5007
    • (2002) Infect. Immun. , vol.70 , pp. 4997-5007
    • Kumar, P.1    Ahuja, N.2    Bhatnagar, R.3
  • 8
    • 0242364656 scopus 로고    scopus 로고
    • Anthrax toxin induces hemolysis: An indirect effect through polymorphonuclear cells
    • A.G. Wu, D. Alibek, Y.L. Li, C. Bradburne, C.L. Bailey, and K. Alibek Anthrax toxin induces hemolysis: an indirect effect through polymorphonuclear cells J. Infect. Dis. 188 2003 1138 1141
    • (2003) J. Infect. Dis. , vol.188 , pp. 1138-1141
    • Wu, A.G.1    Alibek, D.2    Li, Y.L.3    Bradburne, C.4    Bailey, C.L.5    Alibek, K.6
  • 13
  • 16
    • 0142151113 scopus 로고    scopus 로고
    • Exposing a killer: Pathologists angle for anthrax
    • S.W. Chensue Exposing a killer: pathologists angle for anthrax Am. J. Pathol. 163 2003 1699 1702
    • (2003) Am. J. Pathol. , vol.163 , pp. 1699-1702
    • Chensue, S.W.1
  • 19
  • 20
  • 21
    • 85047692288 scopus 로고    scopus 로고
    • Bacillus anthracis lethal toxin induces TNF-alpha-independent hypoxia-mediated toxicity in mice
    • M. Moayeri, D. Haines, H.A. Young, and S.H. Leppla Bacillus anthracis lethal toxin induces TNF-alpha-independent hypoxia-mediated toxicity in mice J. Clin. Invest. 112 2003 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
  • 22
    • 0032984192 scopus 로고    scopus 로고
    • Suppression of platelet aggregation by Bordetella pertussis adenylate cyclase toxin
    • M. Iwaki, K. Kamachi, N. Heveker, and T. Konda Suppression of platelet aggregation by Bordetella pertussis adenylate cyclase toxin Infect. Immun. 67 1999 2763 2768
    • (1999) Infect. Immun. , vol.67 , pp. 2763-2768
    • Iwaki, M.1    Kamachi, K.2    Heveker, N.3    Konda, T.4
  • 23
    • 25844500354 scopus 로고    scopus 로고
    • Antiplatelet activities of anthrax lethal toxin are associated with suppressed p42/44 and p38 mitogen-activated protein kinase pathways in the platelets
    • J.H. Kau, D.S. Sun, W.J. Tsai, H.F. Shyu, H.H. Huang, H.C. Lin, and H.H. Chang Antiplatelet activities of anthrax lethal toxin are associated with suppressed p42/44 and p38 mitogen-activated protein kinase pathways in the platelets J. Infect. Dis. 192 2005 1465 1474
    • (2005) J. Infect. Dis. , vol.192 , pp. 1465-1474
    • Kau, J.H.1    Sun, D.S.2    Tsai, W.J.3    Shyu, H.F.4    Huang, H.H.5    Lin, H.C.6    Chang, H.H.7
  • 26
    • 0034816420 scopus 로고    scopus 로고
    • Rapid purification of recombinant anthrax protective antigen under nondenaturing conditions
    • N. Ahuja, P. Kumar, and R. Bhatnagar Rapid purification of recombinant anthrax protective antigen under nondenaturing conditions Biochem. Biophys. Res. Commun. 286 2001 6 11
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 6-11
    • Ahuja, N.1    Kumar, P.2    Bhatnagar, R.3
  • 27
    • 0034833135 scopus 로고    scopus 로고
    • Purification of anthrax edema factor from Escherichia coli and identification of residues required for binding to anthrax protective antigen
    • P. Kumar, N. Ahuja, and R. Bhatnagar Purification of anthrax edema factor from Escherichia coli and identification of residues required for binding to anthrax protective antigen Infect. Immun. 69 2001 6532 6536
    • (2001) Infect. Immun. , vol.69 , pp. 6532-6536
    • Kumar, P.1    Ahuja, N.2    Bhatnagar, R.3
  • 28
    • 0042171523 scopus 로고    scopus 로고
    • Deletion mutants of protective antigen that inhibit anthrax toxin both in vitro and in vivo
    • N. Ahuja, P. Kumar, S. Alam, M. Gupta, and R. Bhatnagar Deletion mutants of protective antigen that inhibit anthrax toxin both in vitro and in vivo Biochem. Biophys. Res. Commun. 307 2003 446 450
    • (2003) Biochem. Biophys. Res. Commun. , vol.307 , pp. 446-450
    • Ahuja, N.1    Kumar, P.2    Alam, S.3    Gupta, M.4    Bhatnagar, R.5
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the Principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the Principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0029914091 scopus 로고    scopus 로고
    • The bioactive phospholipid, lysophosphatidylcholine, induces cellular effects via G-protein-dependent activation of adenylyl cyclase
    • Y. Yuan, S.M. Schoenwaelder, H.H. Salem, and S.P. Jackson The bioactive phospholipid, lysophosphatidylcholine, induces cellular effects via G-protein-dependent activation of adenylyl cyclase J. Biol. Chem. 271 1996 27090 27098
    • (1996) J. Biol. Chem. , vol.271 , pp. 27090-27098
    • Yuan, Y.1    Schoenwaelder, S.M.2    Salem, H.H.3    Jackson, S.P.4
  • 33
    • 0346367328 scopus 로고
    • Aggregation of blood platelets by adenosine diphosphate and its reversal
    • G.V.R. Born Aggregation of blood platelets by adenosine diphosphate and its reversal Nature 194 1962 927 929
    • (1962) Nature , vol.194 , pp. 927-929
    • Born, G.V.R.1
  • 36
    • 0034333365 scopus 로고    scopus 로고
    • Inhibition of agonist-induced p42 and p38 mitogen-activated protein kinase phosphorylation and CD40 ligand/P-selectin expression by cyclic nucleotide-regulated pathways in human platelets
    • U.R. Schwarz, A.L. Kobsar, M. Koksch, U. Walter, and M. Eigenthaler Inhibition of agonist-induced p42 and p38 mitogen-activated protein kinase phosphorylation and CD40 ligand/P-selectin expression by cyclic nucleotide-regulated pathways in human platelets Biochem. Pharmacol. 60 2000 1399 1407
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 1399-1407
    • Schwarz, U.R.1    Kobsar, A.L.2    Koksch, M.3    Walter, U.4    Eigenthaler, M.5
  • 37
    • 0037033024 scopus 로고    scopus 로고
    • Regulation of glycoprotein Ib-IX-von Willebrand factor interaction by cAMP-dependent protein kinase-mediated phosphorylation at Ser 166 of glycoprotein Ib(beta)
    • R.J. Bodnar, X. Xi, Z. Li, M.C. Berndt, and X. Du Regulation of glycoprotein Ib-IX-von Willebrand factor interaction by cAMP-dependent protein kinase-mediated phosphorylation at Ser 166 of glycoprotein Ib(beta) J. Biol. Chem. 277 2002 47080 47087
    • (2002) J. Biol. Chem. , vol.277 , pp. 47080-47087
    • Bodnar, R.J.1    Xi, X.2    Li, Z.3    Berndt, M.C.4    Du, X.5
  • 38
    • 0037108442 scopus 로고    scopus 로고
    • Sequential cytoplasmic calcium signals in a 2-stage platelet activation process induced by the glycoprotein Ibalpha mechanoreceptor
    • M. Mazzucato, P. Pradella, M.R. Cozzi, L. De Marco, and Z.M. Ruggeri Sequential cytoplasmic calcium signals in a 2-stage platelet activation process induced by the glycoprotein Ibalpha mechanoreceptor Blood 100 2002 2793 2800
    • (2002) Blood , vol.100 , pp. 2793-2800
    • Mazzucato, M.1    Pradella, P.2    Cozzi, M.R.3    De Marco, L.4    Ruggeri, Z.M.5
  • 39
    • 1542313912 scopus 로고    scopus 로고
    • Initial accumulation of platelets during arterial thrombus formation in vivo is inhibited by elevation of basal cAMP levels
    • D.S. Sim, G. Merrill-Skoloff, B.C. Furie, B. Furie, and R. Flaumenhaft Initial accumulation of platelets during arterial thrombus formation in vivo is inhibited by elevation of basal cAMP levels Blood 103 2004 2127 2134
    • (2004) Blood , vol.103 , pp. 2127-2134
    • Sim, D.S.1    Merrill-Skoloff, G.2    Furie, B.C.3    Furie, B.4    Flaumenhaft, R.5
  • 40
    • 0026050285 scopus 로고
    • Contribution of individual toxin components to virulence of Bacillus anthracis
    • C. Pezard, P. Berche, and M. Mock Contribution of individual toxin components to virulence of Bacillus anthracis Infect. Immun. 59 1991 3472 3477
    • (1991) Infect. Immun. , vol.59 , pp. 3472-3477
    • Pezard, C.1    Berche, P.2    Mock, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.