메뉴 건너뛰기




Volumn 35, Issue 3, 2011, Pages 247-252

The tissue factor pathway inhibitor 1 of Sciaenops ocellatus possesses antimicrobial activity and is involved in the immune response against bacterial infection

Author keywords

Antibacterial; Sciaenops ocellatus; Serine protease inhibitor; Tissue factor pathway inhibitor 1

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; SYNTHETIC PEPTIDE; TISSUE FACTOR PATHWAY INHIBITOR; TISSUE FACTOR PATHWAY INHIBITOR 1; UNCLASSIFIED DRUG;

EID: 79151482655     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2010.10.006     Document Type: Article
Times cited : (36)

References (40)
  • 1
    • 0034758293 scopus 로고    scopus 로고
    • Structure and biology of tissue factor pathway inhibitor
    • Bajaj M.S., Birktoft J.J., Steer S.A., Bajaj S.P. Structure and biology of tissue factor pathway inhibitor. Thromb. Haemost. 2001, 86(4):959-972.
    • (2001) Thromb. Haemost. , vol.86 , Issue.4 , pp. 959-972
    • Bajaj, M.S.1    Birktoft, J.J.2    Steer, S.A.3    Bajaj, S.P.4
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0029039574 scopus 로고
    • Tissue factor pathway inhibitor and the current concept of blood coagulation
    • Broze G.J. Tissue factor pathway inhibitor and the current concept of blood coagulation. Blood. Coagul. Fibrinolysis 1995, 6(suppl. 1):S7-S13.
    • (1995) Blood. Coagul. Fibrinolysis , vol.6 , Issue.SUPPL. 1
    • Broze, G.J.1
  • 4
    • 0031934850 scopus 로고    scopus 로고
    • Delayed treatment with recombinant human tissue factor pathway inhibitor improves survival in rabbits with gram-negative peritonitis
    • Camerota A.J., Creasey A.A., Patla V., Larkin V.A., Fink M.P. Delayed treatment with recombinant human tissue factor pathway inhibitor improves survival in rabbits with gram-negative peritonitis. J. Infect. Dis. 1998, 177(3):668-676.
    • (1998) J. Infect. Dis. , vol.177 , Issue.3 , pp. 668-676
    • Camerota, A.J.1    Creasey, A.A.2    Patla, V.3    Larkin, V.A.4    Fink, M.P.5
  • 5
    • 1642459321 scopus 로고    scopus 로고
    • The effect of human tissue factor pathway inhibitor-2 on the growth and metastasis of fibrosarcoma tumors in athymic mice
    • Chand H.S., Du X., Ma D., Inzunza H.D., Kamei S., Foster D., et al. The effect of human tissue factor pathway inhibitor-2 on the growth and metastasis of fibrosarcoma tumors in athymic mice. Blood 2004, 103(3):1069-1077.
    • (2004) Blood , vol.103 , Issue.3 , pp. 1069-1077
    • Chand, H.S.1    Du, X.2    Ma, D.3    Inzunza, H.D.4    Kamei, S.5    Foster, D.6
  • 6
    • 0027319678 scopus 로고
    • Tissue factor pathway inhibitor reduces mortality from Escherichia coli septic shock
    • Creasey A.A., Chang A.C., Feigen L., Wun T.C., Taylor F.B., Hinshaw L.B. Tissue factor pathway inhibitor reduces mortality from Escherichia coli septic shock. J. Clin. Invest. 1993, 91(6):2850-2860.
    • (1993) J. Clin. Invest. , vol.91 , Issue.6 , pp. 2850-2860
    • Creasey, A.A.1    Chang, A.C.2    Feigen, L.3    Wun, T.C.4    Taylor, F.B.5    Hinshaw, L.B.6
  • 7
    • 0037108733 scopus 로고    scopus 로고
    • Structural and functional characterization of tissue factor pathway inhibitor following degradation by matrix metalloproteinase-8
    • Cunningham A.C., Hasty K.A., Enghild J.J., Mast A.E. Structural and functional characterization of tissue factor pathway inhibitor following degradation by matrix metalloproteinase-8. Biochem. J. 2002, 367(Pt2):451-458.
    • (2002) Biochem. J. , vol.367 , Issue.PART 2 , pp. 451-458
    • Cunningham, A.C.1    Hasty, K.A.2    Enghild, J.J.3    Mast, A.E.4
  • 8
    • 77954953808 scopus 로고    scopus 로고
    • Differential regulation of Sciaenops ocellatus viperin expression by intracellular and extracellular bacterial pathogens
    • Dang W., Zhang M., Hu Y.H., Sun L. Differential regulation of Sciaenops ocellatus viperin expression by intracellular and extracellular bacterial pathogens. Fish. Shellfish Immunol. 2010, 29(2):264-270.
    • (2010) Fish. Shellfish Immunol. , vol.29 , Issue.2 , pp. 264-270
    • Dang, W.1    Zhang, M.2    Hu, Y.H.3    Sun, L.4
  • 9
    • 33644801469 scopus 로고    scopus 로고
    • The interactions between inflammation and coagulation
    • Esmon C.T. The interactions between inflammation and coagulation. Br. J. Haematol. 2005, 131(4):417-430.
    • (2005) Br. J. Haematol. , vol.131 , Issue.4 , pp. 417-430
    • Esmon, C.T.1
  • 10
    • 0033407494 scopus 로고    scopus 로고
    • The role of the C-terminal domain in the inhibitory functions of tissue factor pathway inhibitor
    • Ettelaie C., Adam J.M., James N.J., Oke A.O., Harrison J.A., Bunce T.D., et al. The role of the C-terminal domain in the inhibitory functions of tissue factor pathway inhibitor. FEBS Lett. 1999, 463(3):341-344.
    • (1999) FEBS Lett. , vol.463 , Issue.3 , pp. 341-344
    • Ettelaie, C.1    Adam, J.M.2    James, N.J.3    Oke, A.O.4    Harrison, J.A.5    Bunce, T.D.6
  • 11
    • 0024543984 scopus 로고
    • Functional significance of the Kuntiz type inhibitor domains of the lipoprotein-associated coagulation inhibitor
    • Girard T.J., Warren L.A., Novonty W.F., Likert K.M., Brown S.G., Miletich J.B., et al. Functional significance of the Kuntiz type inhibitor domains of the lipoprotein-associated coagulation inhibitor. Nature 1989, 338(6215):518-520.
    • (1989) Nature , vol.338 , Issue.6215 , pp. 518-520
    • Girard, T.J.1    Warren, L.A.2    Novonty, W.F.3    Likert, K.M.4    Brown, S.G.5    Miletich, J.B.6
  • 12
    • 0036037340 scopus 로고    scopus 로고
    • Comprehensive analysis of blood coagulation pathways in teleostei: evolution of coagulation factor genes and identification of zebrafish factor VIIi
    • Hanumanthaiah R., Day K., Jagadeeswaran P. Comprehensive analysis of blood coagulation pathways in teleostei: evolution of coagulation factor genes and identification of zebrafish factor VIIi. Blood Cells Mol. Dis. 2002, 29(1):57-68.
    • (2002) Blood Cells Mol. Dis. , vol.29 , Issue.1 , pp. 57-68
    • Hanumanthaiah, R.1    Day, K.2    Jagadeeswaran, P.3
  • 13
    • 0026594204 scopus 로고
    • The effect of leukocyte elastase on tissue factor pathway inhibitor
    • Higuchi D.A., Wun T.C., Likert K.M., Broze G.J. The effect of leukocyte elastase on tissue factor pathway inhibitor. Blood 1992, 79(7):1712-1719.
    • (1992) Blood , vol.79 , Issue.7 , pp. 1712-1719
    • Higuchi, D.A.1    Wun, T.C.2    Likert, K.M.3    Broze, G.J.4
  • 14
    • 0027477119 scopus 로고
    • Antithrombotic properties of a truncated recombinant tissue factor pathway inhibitor in an experimental venous thrombosis model
    • Holst J., Lindblad B., Bergqvist D., Nordfang O., Ostergaard P.B., Petersen J.L., et al. Antithrombotic properties of a truncated recombinant tissue factor pathway inhibitor in an experimental venous thrombosis model. Haemostasis 1993, 23(suppl. 1):112-117.
    • (1993) Haemostasis , vol.23 , Issue.SUPPL.. 1 , pp. 112-117
    • Holst, J.1    Lindblad, B.2    Bergqvist, D.3    Nordfang, O.4    Ostergaard, P.B.5    Petersen, J.L.6
  • 15
    • 67649600437 scopus 로고    scopus 로고
    • Identification, characterization, and molecular application of a virulence-associated autotransporter from a pathogenic Pseudomonas fluorescens strain
    • Hu Y., Liu C., Hou J., Sun L. Identification, characterization, and molecular application of a virulence-associated autotransporter from a pathogenic Pseudomonas fluorescens strain. Appl. Environ. Microbiol. 2009, 75(13):4333-4340.
    • (2009) Appl. Environ. Microbiol. , vol.75 , Issue.13 , pp. 4333-4340
    • Hu, Y.1    Liu, C.2    Hou, J.3    Sun, L.4
  • 16
    • 77949917657 scopus 로고    scopus 로고
    • Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus)
    • Hu Y.H., Zheng W.J., Sun L. Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus). Fish. Shellfish Immunol. 2010, 28(4):678-686.
    • (2010) Fish. Shellfish Immunol. , vol.28 , Issue.4 , pp. 678-686
    • Hu, Y.H.1    Zheng, W.J.2    Sun, L.3
  • 17
    • 33750630284 scopus 로고    scopus 로고
    • Restoration of tissue factor pathway inhibitor (TFPI) inhibits invasion and tumor growth in vitro and in vivo in a malignant meningioma cell line
    • Kondraganti S., Gondi C.S., Gujrati M., McCutcheon I., Dinh D.H., Rao J.S., et al. Restoration of tissue factor pathway inhibitor (TFPI) inhibits invasion and tumor growth in vitro and in vivo in a malignant meningioma cell line. Int. J. Oncol. 2006, 29(1):25-32.
    • (2006) Int. J. Oncol. , vol.29 , Issue.1 , pp. 25-32
    • Kondraganti, S.1    Gondi, C.S.2    Gujrati, M.3    McCutcheon, I.4    Dinh, D.H.5    Rao, J.S.6
  • 18
    • 14344262864 scopus 로고    scopus 로고
    • Expression and characterization of the first kunitz domain of human tissue factor pathway inhibitor-2
    • Kong D., Ma D., Bai H., Guo H., Cai X., Mo W., et al. Expression and characterization of the first kunitz domain of human tissue factor pathway inhibitor-2. Biochem. Biophys. Res. Commun. 2004, 324(4):1179-1185.
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , Issue.4 , pp. 1179-1185
    • Kong, D.1    Ma, D.2    Bai, H.3    Guo, H.4    Cai, X.5    Mo, W.6
  • 19
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak M. An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 1987, 15(20):8125-8148.
    • (1987) Nucleic Acids Res. , vol.15 , Issue.20 , pp. 8125-8148
    • Kozak, M.1
  • 20
    • 2942545798 scopus 로고    scopus 로고
    • Bidirectional relation between inflammation and coagulation
    • Levi M., van der Poll T., Büller H.R. Bidirectional relation between inflammation and coagulation. Circulation 2004, 109(22):2698-2704.
    • (2004) Circulation , vol.109 , Issue.22 , pp. 2698-2704
    • Levi, M.1    van der Poll, T.2    Büller, H.R.3
  • 21
    • 0029148567 scopus 로고
    • Kinetics of the inhibitor of tissue factor-factor VIIa by tissue factor pathway inhibitor
    • Lindhout T., Franssen J.O., Willems G. Kinetics of the inhibitor of tissue factor-factor VIIa by tissue factor pathway inhibitor. Thromb. Haemost. 1995, 74(3):910-915.
    • (1995) Thromb. Haemost. , vol.74 , Issue.3 , pp. 910-915
    • Lindhout, T.1    Franssen, J.O.2    Willems, G.3
  • 22
    • 77955054192 scopus 로고    scopus 로고
    • Identification and analysis of a Sciaenops ocellatus ISG15 homologue that is involved in host immune defense against bacterial infection
    • Liu C.S., Sun Y., Zhang M., Sun L. Identification and analysis of a Sciaenops ocellatus ISG15 homologue that is involved in host immune defense against bacterial infection. Fish. Shellfish Immunol. 2010, 29(1):167-174.
    • (2010) Fish. Shellfish Immunol. , vol.29 , Issue.1 , pp. 167-174
    • Liu, C.S.1    Sun, Y.2    Zhang, M.3    Sun, L.4
  • 23
    • 32244438720 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor: structure, biology and involvement in disease
    • Lwaleed B.A., Bass P.S. Tissue factor pathway inhibitor: structure, biology and involvement in disease. J. Pathol. 2006, 208(3):327-339.
    • (2006) J. Pathol. , vol.208 , Issue.3 , pp. 327-339
    • Lwaleed, B.A.1    Bass, P.S.2
  • 24
    • 0034884867 scopus 로고    scopus 로고
    • Extremely low doses of tissue factor pathway inhibitor decrease mortality in a rabbit model of septic shock
    • Matyal R., Vin Y., Delude R.L., Lee C., Creasey A.A., Fink M.P. Extremely low doses of tissue factor pathway inhibitor decrease mortality in a rabbit model of septic shock. Intensive Care Med. 2001, 27(8):1274-1280.
    • (2001) Intensive Care Med. , vol.27 , Issue.8 , pp. 1274-1280
    • Matyal, R.1    Vin, Y.2    Delude, R.L.3    Lee, C.4    Creasey, A.A.5    Fink, M.P.6
  • 25
    • 2442724586 scopus 로고
    • Interleukin 1 induces endothelial cell procoagulant while suppressing cell-surface anticoagulant activity
    • Nawroth P.P., Handley D.A., Esmon C.T., Stern D.M. Interleukin 1 induces endothelial cell procoagulant while suppressing cell-surface anticoagulant activity. Proc. Natl. Acad. Sci. U.S.A. 1986, 83(10):3460-3464.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , Issue.10 , pp. 3460-3464
    • Nawroth, P.P.1    Handley, D.A.2    Esmon, C.T.3    Stern, D.M.4
  • 26
    • 0027494426 scopus 로고
    • Factor VII autoactivation proceeds via interaction of distinct protease-cofactor and zymogen-cofactor complexes. Implications of a two-dimensional enzyme kinetic mechanism
    • Neuenschwander P.F., Fiore M.M., Morrissey J.H. Factor VII autoactivation proceeds via interaction of distinct protease-cofactor and zymogen-cofactor complexes. Implications of a two-dimensional enzyme kinetic mechanism. J. Biol. Chem. 1993, 268(29):21489-21492.
    • (1993) J. Biol. Chem. , vol.268 , Issue.29 , pp. 21489-21492
    • Neuenschwander, P.F.1    Fiore, M.M.2    Morrissey, J.H.3
  • 27
    • 0025851449 scopus 로고
    • Plasma antigen levels of the lipoprotein-associated coagulation inhibitor in patient samples
    • Novotny W.F., Brown S.G., Miletich J.P., Rader D.J., Broze G.J. Plasma antigen levels of the lipoprotein-associated coagulation inhibitor in patient samples. Blood 1991, 78(2):387-393.
    • (1991) Blood , vol.78 , Issue.2 , pp. 387-393
    • Novotny, W.F.1    Brown, S.G.2    Miletich, J.P.3    Rader, D.J.4    Broze, G.J.5
  • 28
    • 0017639138 scopus 로고
    • Activation of factor IX by the reaction product of tissue factor and factor VII: additional pathway for initiating blood coagulation
    • Osterud B., Rapaport S.I. Activation of factor IX by the reaction product of tissue factor and factor VII: additional pathway for initiating blood coagulation. Proc. Natl. Acad. Sci. U.S.A. 1977, 74(12):5260-5264.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , Issue.12 , pp. 5260-5264
    • Osterud, B.1    Rapaport, S.I.2
  • 29
    • 0030926515 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor blocks cellular effects of endotoxin by binding to endotoxin and interfering with transfer to CD14
    • Park C.T., Creasey A.A., Wright S.D. Tissue factor pathway inhibitor blocks cellular effects of endotoxin by binding to endotoxin and interfering with transfer to CD14. Blood 1997, 89(12):4268-4274.
    • (1997) Blood , vol.89 , Issue.12 , pp. 4268-4274
    • Park, C.T.1    Creasey, A.A.2    Wright, S.D.3
  • 30
    • 10044255324 scopus 로고    scopus 로고
    • Role for the Kunitz-3 domain of tissue factor pathway inhibitor-alpha in cell surface binding
    • Piro O., Broze G.J. Role for the Kunitz-3 domain of tissue factor pathway inhibitor-alpha in cell surface binding. Circulation 2004, 110(23):3567-3572.
    • (2004) Circulation , vol.110 , Issue.23 , pp. 3567-3572
    • Piro, O.1    Broze, G.J.2
  • 31
    • 2342625416 scopus 로고    scopus 로고
    • Tissue factor and tissue factor pathway inhibitor
    • Price G.C., Thompson S.A., Kam P.C. Tissue factor and tissue factor pathway inhibitor. Anaesthesia 2004, 59(5):483-492.
    • (2004) Anaesthesia , vol.59 , Issue.5 , pp. 483-492
    • Price, G.C.1    Thompson, S.A.2    Kam, P.C.3
  • 33
    • 67650446288 scopus 로고    scopus 로고
    • Fragmented tissue factor pathway inhibitor (TFPI) and TFPI C-terminal peptides eliminate serum-resistant Escherichia coli from blood cultures
    • Schirm S., Liu X., Jennings L.L., Jedrzejewski P., Dai Y., Hardy S. Fragmented tissue factor pathway inhibitor (TFPI) and TFPI C-terminal peptides eliminate serum-resistant Escherichia coli from blood cultures. J. Infect. Dis. 2009, 199(12):1807-1815.
    • (2009) J. Infect. Dis. , vol.199 , Issue.12 , pp. 1807-1815
    • Schirm, S.1    Liu, X.2    Jennings, L.L.3    Jedrzejewski, P.4    Dai, Y.5    Hardy, S.6
  • 34
    • 36349029749 scopus 로고    scopus 로고
    • The role of tissue factor pathway inhibitor-2 in cancer biology
    • Sierko E., Wojtukiewicz M.Z., Kisiel W. The role of tissue factor pathway inhibitor-2 in cancer biology. Semin. Thromb. Hemost. 2007, 33(7):653-659.
    • (2007) Semin. Thromb. Hemost. , vol.33 , Issue.7 , pp. 653-659
    • Sierko, E.1    Wojtukiewicz, M.Z.2    Kisiel, W.3
  • 36
    • 67349237092 scopus 로고    scopus 로고
    • Construction of an attenuated Pseudomonas fluorescens strain and evaluation of its potential as a cross-protective vaccine
    • Wang H., Hu Y., Zhang W., Sun L. Construction of an attenuated Pseudomonas fluorescens strain and evaluation of its potential as a cross-protective vaccine. Vaccine 2009, 27(30):4047-4055.
    • (2009) Vaccine , vol.27 , Issue.30 , pp. 4047-4055
    • Wang, H.1    Hu, Y.2    Zhang, W.3    Sun, L.4
  • 37
    • 0028969172 scopus 로고
    • The carboxy-terminus of tissue factor pathway inhibitor is required for interacting with hepatoma cell in vitro and in vivo
    • Warshawsky I., Bu G., Mast A., Saffitz J.E., Broze G.J., Schwartz A.L. The carboxy-terminus of tissue factor pathway inhibitor is required for interacting with hepatoma cell in vitro and in vivo. J. Clin. Invest. 1995, 95(4):1773-1781.
    • (1995) J. Clin. Invest. , vol.95 , Issue.4 , pp. 1773-1781
    • Warshawsky, I.1    Bu, G.2    Mast, A.3    Saffitz, J.E.4    Broze, G.J.5    Schwartz, A.L.6
  • 38
    • 0026668480 scopus 로고
    • Tissue factor pathway inhibitor: the carboxy-terminus is required for optimal inhibition of factor Xa
    • Wesselschmidt R., Likert K., Girard T., Wun T.C., Broze G.J. Tissue factor pathway inhibitor: the carboxy-terminus is required for optimal inhibition of factor Xa. Blood 1992, 79(8):2004-2010.
    • (1992) Blood , vol.79 , Issue.8 , pp. 2004-2010
    • Wesselschmidt, R.1    Likert, K.2    Girard, T.3    Wun, T.C.4    Broze, G.J.5
  • 39
    • 67149118092 scopus 로고    scopus 로고
    • Attenuation of Edwardsiella tarda virulence by small peptides that interfere with LuxS/autoinducer type 2 quorum sensing
    • Zhang M., Jiao X., Hu Y., Sun L. Attenuation of Edwardsiella tarda virulence by small peptides that interfere with LuxS/autoinducer type 2 quorum sensing. Appl. Environ. Microbiol. 2009, 75(12):3882-3890.
    • (2009) Appl. Environ. Microbiol. , vol.75 , Issue.12 , pp. 3882-3890
    • Zhang, M.1    Jiao, X.2    Hu, Y.3    Sun, L.4
  • 40
    • 77951101672 scopus 로고    scopus 로고
    • Cloning and analysis of a ferritin subunit from turbot (Scophthalmus maximus)
    • Zheng W.J., Hu Y.H., Sun L. Cloning and analysis of a ferritin subunit from turbot (Scophthalmus maximus). Fish. Shellfish Immunol. 2010, 28(5-6):829-836.
    • (2010) Fish. Shellfish Immunol. , vol.28 , Issue.5-6 , pp. 829-836
    • Zheng, W.J.1    Hu, Y.H.2    Sun, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.