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Volumn 45, Issue 2, 2015, Pages 544-550

TFPI inhibits lectin pathway of complement activation by direct interaction with MASP-2

Author keywords

Complement inhibition; Complement coagulation crosstalk; MASP 2; TFPI

Indexed keywords

LECTIN; MANNAN; MBL ASSOCIATED SERINE PROTEASE 2; MONOCLONAL ANTIBODY; SERINE PROTEINASE; TISSUE FACTOR PATHWAY INHIBITOR; UNCLASSIFIED DRUG; CHROMOGENIC SUBSTRATE; COMPLEMENT COMPONENT C1R; COMPLEMENT COMPONENT C1S; COMPLEMENT COMPONENT C4; LIPOPROTEIN; LIPOPROTEIN-ASSOCIATED COAGULATION INHIBITOR; MANNAN BINDING LECTIN ASSOCIATED SERINE PROTEINASE; MASP1 PROTEIN, HUMAN; MASP2 PROTEIN, HUMAN; RECOMBINANT PROTEIN; SERINE PROTEINASE INHIBITOR; SOLUTION AND SOLUBILITY;

EID: 84923031022     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201445070     Document Type: Article
Times cited : (31)

References (24)
  • 1
    • 18644384051 scopus 로고    scopus 로고
    • Gastrointestinal ischemia-reperfusion injury is lectin complement pathway dependent without involving C1q
    • Hart, M. L., Ceonzo, K. A., Shaffer, L. A., Takahashi, K., Rother, R. P., Reenstra, W. R., Buras, J. A. et al., Gastrointestinal ischemia-reperfusion injury is lectin complement pathway dependent without involving C1q. J. Immunol. 2005. 174: 6373-6380.
    • (2005) J. Immunol. , vol.174 , pp. 6373-6380
    • Hart, M.L.1    Ceonzo, K.A.2    Shaffer, L.A.3    Takahashi, K.4    Rother, R.P.5    Reenstra, W.R.6    Buras, J.A.7
  • 2
    • 79959359209 scopus 로고    scopus 로고
    • Mannose-binding lectin deficiency is associated with smaller infarction size and favorable outcome in ischemic stroke patients
    • Osthoff, M., Katan, M., Fluri, F., Schuetz, P., Bingisser, R., Kappos, L., Steck, A. J. et al., Mannose-binding lectin deficiency is associated with smaller infarction size and favorable outcome in ischemic stroke patients. PLoS One 2011. 6: e21338.
    • (2011) PLoS One , vol.6
    • Osthoff, M.1    Katan, M.2    Fluri, F.3    Schuetz, P.4    Bingisser, R.5    Kappos, L.6    Steck, A.J.7
  • 3
    • 79956313936 scopus 로고    scopus 로고
    • Targeting of mannan-binding lectin-associated serine protease-2 confers protection from myocardial and gastrointestinal ischemia/reperfusion injury
    • Schwaeble, W. J., Lynch, N. J., Clark, J. E., Marber, M., Samani, N. J., Ali, Y. M., Dudler, T. et al., Targeting of mannan-binding lectin-associated serine protease-2 confers protection from myocardial and gastrointestinal ischemia/reperfusion injury. Proc. Natl. Acad. Sci. U.S.A. 2011. 108: 7523-7528.
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 7523-7528
    • Schwaeble, W.J.1    Lynch, N.J.2    Clark, J.E.3    Marber, M.4    Samani, N.J.5    Ali, Y.M.6    Dudler, T.7
  • 4
    • 84873475609 scopus 로고    scopus 로고
    • The control of the complement lectin pathway activation revisited: both C1-inhibitor and antithrombin are likely physiological inhibitors, while alpha2-macroglobulin is not
    • Parej, K., Dobo, J., Zavodszky, P. and Gal, P., The control of the complement lectin pathway activation revisited: both C1-inhibitor and antithrombin are likely physiological inhibitors, while alpha2-macroglobulin is not. Mol. Immunol. 2013. 54: 415-422.
    • (2013) Mol. Immunol. , vol.54 , pp. 415-422
    • Parej, K.1    Dobo, J.2    Zavodszky, P.3    Gal, P.4
  • 6
    • 0031752854 scopus 로고    scopus 로고
    • Proteolysis of tissue factor pathway inhibitor (TFPI) by plasmin: effect on TFPI activity
    • Li, A. and Wun, T. C., Proteolysis of tissue factor pathway inhibitor (TFPI) by plasmin: effect on TFPI activity. Thromb. Haemost. 1998. 80: 423-427.
    • (1998) Thromb. Haemost. , vol.80 , pp. 423-427
    • Li, A.1    Wun, T.C.2
  • 7
    • 0034758293 scopus 로고    scopus 로고
    • Structure and biology of tissue factor pathway inhibitor
    • Bajaj, M. S., Birktoft, J. J., Steer, S. A. and Bajaj, S. P., Structure and biology of tissue factor pathway inhibitor. Thromb. Haemost. 2001. 86: 959-972.
    • (2001) Thromb. Haemost. , vol.86 , pp. 959-972
    • Bajaj, M.S.1    Birktoft, J.J.2    Steer, S.A.3    Bajaj, S.P.4
  • 9
    • 84883303777 scopus 로고    scopus 로고
    • Cellular expression and biological activities of alternatively spliced forms of tissue factor pathway inhibitor
    • Maroney, S. A., Hansen, K. G. and Mast, A. E., Cellular expression and biological activities of alternatively spliced forms of tissue factor pathway inhibitor. Curr. Opin. Hematol. 2013. 20: 403-409.
    • (2013) Curr. Opin. Hematol. , vol.20 , pp. 403-409
    • Maroney, S.A.1    Hansen, K.G.2    Mast, A.E.3
  • 10
    • 34548835747 scopus 로고    scopus 로고
    • Sepsis-induced coagulation in the baboon lung is associated with decreased tissue factor pathway inhibitor
    • Tang, H., Ivanciu, L., Popescu, N., Peer, G., Hack, E., Lupu, C., Taylor, F. B., Jr. et al., Sepsis-induced coagulation in the baboon lung is associated with decreased tissue factor pathway inhibitor. Am. J. Pathol. 2007. 171: 1066-1077.
    • (2007) Am. J. Pathol. , vol.171 , pp. 1066-1077
    • Tang, H.1    Ivanciu, L.2    Popescu, N.3    Peer, G.4    Hack, E.5    Lupu, C.6    Taylor, F.B.7
  • 11
    • 84878797556 scopus 로고    scopus 로고
    • Plasma levels of mannan-binding lectin (MBL)-associated serine proteases (MASPs) and MBL-associated protein in cardio- and cerebrovascular diseases
    • Frauenknecht, V., Thiel, S., Storm, L., Meier, N., Arnold, M., Schmid, J. P., Saner, H. et al., Plasma levels of mannan-binding lectin (MBL)-associated serine proteases (MASPs) and MBL-associated protein in cardio- and cerebrovascular diseases. Clin. Exp. Immunol. 2013. 173: 112-120.
    • (2013) Clin. Exp. Immunol. , vol.173 , pp. 112-120
    • Frauenknecht, V.1    Thiel, S.2    Storm, L.3    Meier, N.4    Arnold, M.5    Schmid, J.P.6    Saner, H.7
  • 12
    • 84868201188 scopus 로고    scopus 로고
    • Endogenous and natural complement inhibitor attenuates myocardial injury and arterial thrombogenesis
    • Pavlov, V. I., Skjoedt, M. O., Siow, T. Y., Rosbjerg, A., Garred, P. and Stahl, G. L., Endogenous and natural complement inhibitor attenuates myocardial injury and arterial thrombogenesis. Circulation 2012. 126: 2227-2235.
    • (2012) Circulation , vol.126 , pp. 2227-2235
    • Pavlov, V.I.1    Skjoedt, M.O.2    Siow, T.Y.3    Rosbjerg, A.4    Garred, P.5    Stahl, G.L.6
  • 13
    • 0035146571 scopus 로고    scopus 로고
    • The activity of tissue factor pathway inhibitor in experimental models of superantigen-induced shock and polymicrobial intra-abdominal sepsis
    • Opal, S. M., Palardy, J. E., Parejo, N. A. and Creasey, A. A., The activity of tissue factor pathway inhibitor in experimental models of superantigen-induced shock and polymicrobial intra-abdominal sepsis. Crit. Care Med. 2001. 29: 13-17.
    • (2001) Crit. Care Med. , vol.29 , pp. 13-17
    • Opal, S.M.1    Palardy, J.E.2    Parejo, N.A.3    Creasey, A.A.4
  • 14
    • 0033556648 scopus 로고    scopus 로고
    • The effect of tissue factor pathway inhibitor on hepatic ischemic reperfusion injury of the rat
    • Yoshimura, N., Kobayashi, Y., Nakamura, K., Yamagishi, H. and Oka, T., The effect of tissue factor pathway inhibitor on hepatic ischemic reperfusion injury of the rat. Transplantation 1999. 67: 45-53.
    • (1999) Transplantation , vol.67 , pp. 45-53
    • Yoshimura, N.1    Kobayashi, Y.2    Nakamura, K.3    Yamagishi, H.4    Oka, T.5
  • 15
    • 0038690407 scopus 로고    scopus 로고
    • Efficacy and safety of tifacogin (recombinant tissue factor pathway inhibitor) in severe sepsis: a randomized controlled trial
    • Abraham, E., Reinhart, K., Opal, S., Demeyer, I., Doig, C., Rodriguez, A. L., Beale, R. et al., Efficacy and safety of tifacogin (recombinant tissue factor pathway inhibitor) in severe sepsis: a randomized controlled trial. JAMA 2003. 290: 238-247.
    • (2003) JAMA , vol.290 , pp. 238-247
    • Abraham, E.1    Reinhart, K.2    Opal, S.3    Demeyer, I.4    Doig, C.5    Rodriguez, A.L.6    Beale, R.7
  • 16
    • 0035159740 scopus 로고    scopus 로고
    • Assessment of the safety of recombinant tissue factor pathway inhibitor in patients with severe sepsis: a multicenter, randomized, placebo-controlled, single-blind, dose escalation study
    • Abraham, E., Reinhart, K., Svoboda, P., Seibert, A., Olthoff, D., Dal, N. A., Postier, R. et al., Assessment of the safety of recombinant tissue factor pathway inhibitor in patients with severe sepsis: a multicenter, randomized, placebo-controlled, single-blind, dose escalation study. Crit. Care Med. 2001. 29: 2081-2089.
    • (2001) Crit. Care Med. , vol.29 , pp. 2081-2089
    • Abraham, E.1    Reinhart, K.2    Svoboda, P.3    Seibert, A.4    Olthoff, D.5    Dal, N.A.6    Postier, R.7
  • 17
    • 84907200730 scopus 로고    scopus 로고
    • Mannan-binding lectin-associated serine protease 2 is critical for the development of renal ischemia reperfusion injury and mediates tissue injury in the absence of complement C4
    • Asgari, E., Farrar, C. A., Lynch, N., Ali, Y. M., Roscher, S., Stover, C., Zhou, W. et al., Mannan-binding lectin-associated serine protease 2 is critical for the development of renal ischemia reperfusion injury and mediates tissue injury in the absence of complement C4. FASEB J. 2014. 28: 3996-4003.
    • (2014) FASEB J , vol.28 , pp. 3996-4003
    • Asgari, E.1    Farrar, C.A.2    Lynch, N.3    Ali, Y.M.4    Roscher, S.5    Stover, C.6    Zhou, W.7
  • 18
    • 33846804076 scopus 로고    scopus 로고
    • Deficiency of functional mannose-binding lectin is not associated with infections in patients with systemic lupus erythematosus
    • Bultink, I. E., Hamann, D., Seelen, M. A., Hart, M. H., Dijkmans, B. A., Daha, M. R. and Voskuyl, A. E., Deficiency of functional mannose-binding lectin is not associated with infections in patients with systemic lupus erythematosus. Arthritis Res. Ther. 2006. 8: R183.
    • (2006) Arthritis Res. Ther. , vol.8 , pp. R183
    • Bultink, I.E.1    Hamann, D.2    Seelen, M.A.3    Hart, M.H.4    Dijkmans, B.A.5    Daha, M.R.6    Voskuyl, A.E.7
  • 19
    • 0027179963 scopus 로고
    • Application of a monoclonal antibody against a neoepitope on activated C4 in an ELISA for the quantification of complement activation via the classical pathway
    • Wolbink, G. J., Bollen, J., Baars, J. W., ten Berge, R. J., Swaak, A. J., Paardekooper, J. and Hack, C. E., Application of a monoclonal antibody against a neoepitope on activated C4 in an ELISA for the quantification of complement activation via the classical pathway. J. Immunol. Methods 1993. 163: 67-76.
    • (1993) J. Immunol. Methods , vol.163 , pp. 67-76
    • Wolbink, G.J.1    Bollen, J.2    Baars, J.W.3    ten Berge, R.J.4    Swaak, A.J.5    Paardekooper, J.6    Hack, C.E.7
  • 21
    • 64849114540 scopus 로고    scopus 로고
    • Polymorphisms in mannan-binding lectin (MBL)-associated serine protease 2 affect stability, binding to MBL, and enzymatic activity
    • Thiel, S., Kolev, M., Degn, S., Steffensen, R., Hansen, A. G., Ruseva, M. and Jensenius, J. C., Polymorphisms in mannan-binding lectin (MBL)-associated serine protease 2 affect stability, binding to MBL, and enzymatic activity. J. Immunol. 2009. 182: 2939-2947.
    • (2009) J. Immunol. , vol.182 , pp. 2939-2947
    • Thiel, S.1    Kolev, M.2    Degn, S.3    Steffensen, R.4    Hansen, A.G.5    Ruseva, M.6    Jensenius, J.C.7
  • 22
    • 70349254225 scopus 로고    scopus 로고
    • Mannose-binding lectin (MBL) substitution: recovery of opsonic function in vivo lags behind MBL serum levels
    • Brouwer, N., Frakking, F. N., van de Wetering, M. D., van, H. M., Hart, M., Budde, I. K., Strengers, P. F. et al., Mannose-binding lectin (MBL) substitution: recovery of opsonic function in vivo lags behind MBL serum levels. J. Immunol. 2009. 183: 3496-3504.
    • (2009) J. Immunol. , vol.183 , pp. 3496-3504
    • Brouwer, N.1    Frakking, F.N.2    van de Wetering, M.D.3    van, H.M.4    Hart, M.5    Budde, I.K.6    Strengers, P.F.7
  • 24
    • 0347915527 scopus 로고    scopus 로고
    • Differential substrate and inhibitor profiles for human MASP-1 and MASP-2
    • Presanis, J. S., Hajela, K., Ambrus, G., Gal, P. and Sim, R. B., Differential substrate and inhibitor profiles for human MASP-1 and MASP-2. Mol. Immunol. 2004. 40: 921-929.
    • (2004) Mol. Immunol. , vol.40 , pp. 921-929
    • Presanis, J.S.1    Hajela, K.2    Ambrus, G.3    Gal, P.4    Sim, R.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.