메뉴 건너뛰기




Volumn 133, Issue 1, 2014, Pages 80-87

Ambivalent roles of carboxypeptidase B in the lytic susceptibility of fibrin

Author keywords

Carboxypeptidase; Fibrin; Fibrinolysis; Plasmin; tPA

Indexed keywords

ARGININE; CARBOXYPEPTIDASE B; FIBRIN; FIBRINOGEN; PLASMIN; TISSUE PLASMINOGEN ACTIVATOR;

EID: 84890562915     PISSN: 00493848     EISSN: 18792472     Source Type: Journal    
DOI: 10.1016/j.thromres.2013.09.017     Document Type: Article
Times cited : (18)

References (49)
  • 2
    • 84868149988 scopus 로고    scopus 로고
    • Regulation of fibrinolysis by C-terminal lysines operates through plasminogen and plasmin but not tissue plasminogen activator (tPA)
    • M.M. Silva, C. Thelwell, S.C. Williams, and C. Longstaff Regulation of fibrinolysis by C-terminal lysines operates through plasminogen and plasmin but not tissue plasminogen activator (tPA) J Thromb Haemost 10 2012 2354 2360
    • (2012) J Thromb Haemost , vol.10 , pp. 2354-2360
    • Silva, M.M.1    Thelwell, C.2    Williams, S.C.3    Longstaff, C.4
  • 4
    • 0031915389 scopus 로고    scopus 로고
    • Plasma and recombinant thrombin-activable fibrinolysis inhibitor (TAFI) and activated TAFI compared with respect to glycosylation, thrombin/ thrombomodulin-dependent activation, thermal stability, and enzymatic properties
    • M.B. Boffa, W. Wang, L. Bajzar, and M.E. Nesheim Plasma and recombinant thrombin-activable fibrinolysis inhibitor (TAFI) and activated TAFI compared with respect to glycosylation, thrombin/thrombomodulin-dependent activation, thermal stability, and enzymatic properties J Biol Chem 273 1998 2127 2135
    • (1998) J Biol Chem , vol.273 , pp. 2127-2135
    • Boffa, M.B.1    Wang, W.2    Bajzar, L.3    Nesheim, M.E.4
  • 5
  • 6
    • 0028222563 scopus 로고
    • Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen
    • W. Wang, D.F. Hendriks, and S.S. Scharpé Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen J Biol Chem 269 1994 15937 15944
    • (1994) J Biol Chem , vol.269 , pp. 15937-15944
    • Wang, W.1    Hendriks, D.F.2    Scharpé, S.S.3
  • 8
  • 10
    • 0028815556 scopus 로고
    • Plasma carboxypeptidases as regulators of the plasminogen system
    • A. Redlitz, A.K. Tan, D.L. Eaton, and E.F. Plow Plasma carboxypeptidases as regulators of the plasminogen system J Clin Invest 96 1995 2534 2538
    • (1995) J Clin Invest , vol.96 , pp. 2534-2538
    • Redlitz, A.1    Tan, A.K.2    Eaton, D.L.3    Plow, E.F.4
  • 11
    • 48249152233 scopus 로고    scopus 로고
    • The biochemical and physical process of fibrinolysis and effects of clot structure and stability on the lysis rate
    • J.W. Weisel, and R.I. Litvinov The biochemical and physical process of fibrinolysis and effects of clot structure and stability on the lysis rate Cardiovasc Hematol Agents Med Chem 6 2008 161 180
    • (2008) Cardiovasc Hematol Agents Med Chem , vol.6 , pp. 161-180
    • Weisel, J.W.1    Litvinov, R.I.2
  • 12
    • 78751560568 scopus 로고    scopus 로고
    • The interplay between tissue plasminogen activator domains and fibrin structures in the regulation of fibrinolysis: Kinetic and microscopic studies
    • C. Longstaff, C. Thelwell, S.C. Williams, M.M. Silva, L. Szabó, and K. Kolev The interplay between tissue plasminogen activator domains and fibrin structures in the regulation of fibrinolysis: kinetic and microscopic studies Blood 117 2011 661 668
    • (2011) Blood , vol.117 , pp. 661-668
    • Longstaff, C.1    Thelwell, C.2    Williams, S.C.3    Silva, M.M.4    Szabó, L.5    Kolev, K.6
  • 13
    • 25144516748 scopus 로고    scopus 로고
    • TAFI gene haplotypes, TAFI plasma levels and future risk of coronary heart disease: The PRIME Study
    • P.E. Morange, D.A. Tregouet, C. Frere, G. Luc, D. Arveiler, and J. Ferrieres TAFI gene haplotypes, TAFI plasma levels and future risk of coronary heart disease: the PRIME Study J Thromb Haemost 3 2005 1503 1510
    • (2005) J Thromb Haemost , vol.3 , pp. 1503-1510
    • Morange, P.E.1    Tregouet, D.A.2    Frere, C.3    Luc, G.4    Arveiler, D.5    Ferrieres, J.6
  • 14
    • 34247275973 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor activation peptide shows association with all major subtypes of ischemic stroke and with TAFI gene variation
    • C. Ladenvall, A. Gils, K. Jood, C. Blomstrand, P.J. Declerck, and C. Jern Thrombin activatable fibrinolysis inhibitor activation peptide shows association with all major subtypes of ischemic stroke and with TAFI gene variation Arterioscler Thromb Vasc Biol 27 2007 955 962
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 955-962
    • Ladenvall, C.1    Gils, A.2    Jood, K.3    Blomstrand, C.4    Declerck, P.J.5    Jern, C.6
  • 15
    • 2342571555 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor and the risk for recurrent venous thromboembolism
    • S. Eichinger, V. Schönauer, A. Weltermann, E. Minar, C. Bialonczyk, and M. Hirschl Thrombin-activatable fibrinolysis inhibitor and the risk for recurrent venous thromboembolism Blood 103 2004 3773 3776
    • (2004) Blood , vol.103 , pp. 3773-3776
    • Eichinger, S.1    Schönauer, V.2    Weltermann, A.3    Minar, E.4    Bialonczyk, C.5    Hirschl, M.6
  • 16
    • 77955874727 scopus 로고    scopus 로고
    • Venous thrombosis risk associated with plasma hypofibrinolysis is explained by elevated plasma levels of TAFI and PAI-1
    • M.E. Meltzer, T. Lisman, P.G. de Groot, J.C. Meijers, S. le Cessie, and C.J. Doggen Venous thrombosis risk associated with plasma hypofibrinolysis is explained by elevated plasma levels of TAFI and PAI-1 Blood 116 2010 113 121
    • (2010) Blood , vol.116 , pp. 113-121
    • Meltzer, M.E.1    Lisman, T.2    De Groot, P.G.3    Meijers, J.C.4    Le Cessie, S.5    Doggen, C.J.6
  • 17
    • 0037383184 scopus 로고    scopus 로고
    • Thrombin-activable fibrinolysis inhibitor levels in the acute phase of ischemic stroke
    • J. Montaner, M. Ribó, J. Monasterio, C.A. Molina, and J. Alvarez-Sabín Thrombin-activable fibrinolysis inhibitor levels in the acute phase of ischemic stroke Stroke 34 2003 1038 1040
    • (2003) Stroke , vol.34 , pp. 1038-1040
    • Montaner, J.1    Ribó, M.2    Monasterio, J.3    Molina, C.A.4    Alvarez-Sabín, J.5
  • 18
    • 46749108013 scopus 로고    scopus 로고
    • Absolute risk of venous and arterial thromboembolism in thrombophilic families is not increased by high thrombin-activatable fibrinolysis inhibitor (TAFI) levels
    • N. Folkeringa, M. Coppens, N.J. Veeger, V.J. Bom, S. Middeldorp, and K. Hamulyak Absolute risk of venous and arterial thromboembolism in thrombophilic families is not increased by high thrombin-activatable fibrinolysis inhibitor (TAFI) levels Thromb Haemost 100 2008 38 44
    • (2008) Thromb Haemost , vol.100 , pp. 38-44
    • Folkeringa, N.1    Coppens, M.2    Veeger, N.J.3    Bom, V.J.4    Middeldorp, S.5    Hamulyak, K.6
  • 19
    • 1542297149 scopus 로고    scopus 로고
    • Very high TAFI antigen levels are associated with a lower risk of hard coronary events: The PRIME Study
    • I. Juhan-Vague, P.E. Morange, and PRIME Study Group Very high TAFI antigen levels are associated with a lower risk of hard coronary events: the PRIME Study J Thromb Haemost 1 2003 2243 2244
    • (2003) J Thromb Haemost , vol.1 , pp. 2243-2244
    • Juhan-Vague, I.1    Morange, P.E.2    Study Group, P.3
  • 20
    • 80052437004 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor
    • P.J. Declerck Thrombin activatable fibrinolysis inhibitor Hamostaseologie 31 2011 165 173
    • (2011) Hamostaseologie , vol.31 , pp. 165-173
    • Declerck, P.J.1
  • 21
    • 3142579973 scopus 로고    scopus 로고
    • The intrinsic threshold of the fibrinolytic system is modulated by basic carboxypeptidases, but the magnitude of the antifibrinolytic effect of activated thrombin-activable fibrinolysis inhibitor is masked by its instability
    • J.B. Walker, and L. Bajzar The intrinsic threshold of the fibrinolytic system is modulated by basic carboxypeptidases, but the magnitude of the antifibrinolytic effect of activated thrombin-activable fibrinolysis inhibitor is masked by its instability J Biol Chem 279 2004 27896 27904
    • (2004) J Biol Chem , vol.279 , pp. 27896-27904
    • Walker, J.B.1    Bajzar, L.2
  • 22
    • 0038029888 scopus 로고    scopus 로고
    • Identification of amino acids in antiplasmin involved in its noncovalent 'lysine-binding-site'-dependent interaction with plasmin
    • H. Wang, A. Yu, B. Wiman, and S. Pap Identification of amino acids in antiplasmin involved in its noncovalent 'lysine-binding-site'-dependent interaction with plasmin Eur J Biochem 270 2003 2023 2029
    • (2003) Eur J Biochem , vol.270 , pp. 2023-2029
    • Wang, H.1    Yu, A.2    Wiman, B.3    Pap, S.4
  • 23
    • 0036143120 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor (TAFI) deficiency is compatible with murine life
    • M. Nagashima, Z.F. Yin, L. Zhao, K. White, Y. Zhu, and N. Lasky Thrombin-activatable fibrinolysis inhibitor (TAFI) deficiency is compatible with murine life J Clin Invest 109 2002 101 110
    • (2002) J Clin Invest , vol.109 , pp. 101-110
    • Nagashima, M.1    Yin, Z.F.2    Zhao, L.3    White, K.4    Zhu, Y.5    Lasky, N.6
  • 25
    • 0027211110 scopus 로고
    • An international collaborative study to investigate standardisation of hirudin potency
    • C. Longstaff, M.Y. Wong, and P.J. Gaffney An international collaborative study to investigate standardisation of hirudin potency Thromb Haemost 69 1993 430 435
    • (1993) Thromb Haemost , vol.69 , pp. 430-435
    • Longstaff, C.1    Wong, M.Y.2    Gaffney, P.J.3
  • 26
    • 0014932863 scopus 로고
    • Plasminogen purification from human plasma by affinity chromatography
    • D.G. Deutsch, and E.T. Mertz Plasminogen purification from human plasma by affinity chromatography Science 170 1970 1095 1096
    • (1970) Science , vol.170 , pp. 1095-1096
    • Deutsch, D.G.1    Mertz, E.T.2
  • 27
    • 0028360109 scopus 로고
    • Regulation of fibrinolytic activity of neutrophil leukocyte elastase, plasmin, and miniplasmin by plasma protease inhibitors
    • K. Kolev, I. Léránt, K. Tenekejiev, and R. Machovich Regulation of fibrinolytic activity of neutrophil leukocyte elastase, plasmin, and miniplasmin by plasma protease inhibitors J Biol Chem 269 1994 17030 17034
    • (1994) J Biol Chem , vol.269 , pp. 17030-17034
    • Kolev, K.1    Léránt, I.2    Tenekejiev, K.3    Machovich, R.4
  • 28
    • 0030051895 scopus 로고    scopus 로고
    • Quantitative comparison of fibrin degradation with plasmin, miniplasmin, neurophil leukocyte elastase and cathepsin G
    • K. Kolev, E. Komorowicz, W.G. Owen, and R. Machovich Quantitative comparison of fibrin degradation with plasmin, miniplasmin, neurophil leukocyte elastase and cathepsin G Thromb Haemost 75 1996 140 146
    • (1996) Thromb Haemost , vol.75 , pp. 140-146
    • Kolev, K.1    Komorowicz, E.2    Owen, W.G.3    Machovich, R.4
  • 29
    • 0030997702 scopus 로고    scopus 로고
    • Functional evaluation of the structural features of proteases and their substrate in fibrin surface degradation
    • K. Kolev, K. Tenekedjiev, E. Komorowicz, and R. Machovich Functional evaluation of the structural features of proteases and their substrate in fibrin surface degradation J Biol Chem 272 1997 13666 13675
    • (1997) J Biol Chem , vol.272 , pp. 13666-13675
    • Kolev, K.1    Tenekedjiev, K.2    Komorowicz, E.3    Machovich, R.4
  • 30
    • 34250692159 scopus 로고    scopus 로고
    • Structure of fibrin: Impact on clot stability
    • J.W. Weisel Structure of fibrin: impact on clot stability J Thromb Haemost 5 Suppl. 1 2007 116 124
    • (2007) J Thromb Haemost , vol.5 , Issue.SUPPL. 1 , pp. 116-124
    • Weisel, J.W.1
  • 31
  • 32
    • 0019987224 scopus 로고
    • Studies on the kinetics of plasminogen activation by tissue plasminogen activator
    • M. Rånby Studies on the kinetics of plasminogen activation by tissue plasminogen activator Biochim Biophys Acta 704 1982 461 469
    • (1982) Biochim Biophys Acta , vol.704 , pp. 461-469
    • Rånby, M.1
  • 33
    • 40349098341 scopus 로고    scopus 로고
    • Suppressed catalytic efficiency of plasmin in the presence of long-chain fatty acids. Identification of kinetic parameters from continuous enzymatic assay with Monte Carlo simulation
    • A. Tanka-Salamon, K. Tenekedjiev, R. Machovich, and K. Kolev Suppressed catalytic efficiency of plasmin in the presence of long-chain fatty acids. Identification of kinetic parameters from continuous enzymatic assay with Monte Carlo simulation FEBS J 275 2008 1274 1282
    • (2008) FEBS J , vol.275 , pp. 1274-1282
    • Tanka-Salamon, A.1    Tenekedjiev, K.2    Machovich, R.3    Kolev, K.4
  • 34
    • 4544232604 scopus 로고    scopus 로고
    • A proposed reference method for plasminogen activators that enables calculation of enzyme activities in SI units
    • C. Longstaff, and C.M. Whitton A proposed reference method for plasminogen activators that enables calculation of enzyme activities in SI units J Thromb Haemost 2 2004 1416 1421
    • (2004) J Thromb Haemost , vol.2 , pp. 1416-1421
    • Longstaff, C.1    Whitton, C.M.2
  • 36
    • 0032538557 scopus 로고    scopus 로고
    • A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor
    • W. Wang, M.B. Boffa, L. Bajzar, J.B. Walker, and M.E. Nesheim A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor J Biol Chem 273 1998 27176 27181
    • (1998) J Biol Chem , vol.273 , pp. 27176-27181
    • Wang, W.1    Boffa, M.B.2    Bajzar, L.3    Walker, J.B.4    Nesheim, M.E.5
  • 37
    • 33646886617 scopus 로고    scopus 로고
    • Arginine, arginine analogs and nitric oxide production in chronic kidney disease
    • C. Baylis Arginine, arginine analogs and nitric oxide production in chronic kidney disease Nat Clin Pract Nephrol 2 2006 209 220
    • (2006) Nat Clin Pract Nephrol , vol.2 , pp. 209-220
    • Baylis, C.1
  • 38
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor
    • L. Bajzar, R. Manuel, and M.E. Nesheim Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor J Biol Chem 270 1995 14477 14484
    • (1995) J Biol Chem , vol.270 , pp. 14477-14484
    • Bajzar, L.1    Manuel, R.2    Nesheim, M.E.3
  • 39
    • 1842728323 scopus 로고    scopus 로고
    • Activated thrombin-activatable fibrinolysis inhibitor reduces the ability of high molecular weight fibrin degradation products to protect plasmin from antiplasmin
    • M. Schneider, N. Brufatto, E. Neill, and M. Nesheim Activated thrombin-activatable fibrinolysis inhibitor reduces the ability of high molecular weight fibrin degradation products to protect plasmin from antiplasmin J Biol Chem 279 2004 13340 13345
    • (2004) J Biol Chem , vol.279 , pp. 13340-13345
    • Schneider, M.1    Brufatto, N.2    Neill, E.3    Nesheim, M.4
  • 40
    • 0035071928 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor (TAFI) does not inhibit in vitro thrombolysis by pharmacological concentrations of t-PA
    • M. Colucci, A.M. D'Aprile, A. Italia, P. Gresele, J. Morser, and N. Semeraro Thrombin activatable fibrinolysis inhibitor (TAFI) does not inhibit in vitro thrombolysis by pharmacological concentrations of t-PA Thromb Haemost 85 2001 661 666
    • (2001) Thromb Haemost , vol.85 , pp. 661-666
    • Colucci, M.1    D'Aprile, A.M.2    Italia, A.3    Gresele, P.4    Morser, J.5    Semeraro, N.6
  • 41
    • 33748589984 scopus 로고    scopus 로고
    • Fibrinolytic efficacy of Amediplase, Tenecteplase and scu-PA in different external plasma clot lysis models: Sensitivity to the inhibitory action of thrombin activatable fibrinolysis inhibitor (TAFI)
    • A.H. Guimarães, M.M. Barrett-Bergshoeff, M. Criscuoli, S. Evangelista, and D.C. Rijken Fibrinolytic efficacy of Amediplase, Tenecteplase and scu-PA in different external plasma clot lysis models: sensitivity to the inhibitory action of thrombin activatable fibrinolysis inhibitor (TAFI) Thromb Haemost 96 2006 325 330
    • (2006) Thromb Haemost , vol.96 , pp. 325-330
    • Guimarães, A.H.1    Barrett-Bergshoeff, M.M.2    Criscuoli, M.3    Evangelista, S.4    Rijken, D.C.5
  • 42
    • 1642398603 scopus 로고    scopus 로고
    • Thrombus lysis by uPA, scuPA and tPA is regulated by plasma TAFI
    • N.J. Mutch, N.R. Moore, E. Wang, and N.A. Booth Thrombus lysis by uPA, scuPA and tPA is regulated by plasma TAFI J Thromb Haemost 1 2003 2000 2007
    • (2003) J Thromb Haemost , vol.1 , pp. 2000-2007
    • Mutch, N.J.1    Moore, N.R.2    Wang, E.3    Booth, N.A.4
  • 43
    • 84897585583 scopus 로고    scopus 로고
    • Modelling fibrinolysis: A 3D stochastic multiscale model
    • 10.1093/imammb/dqs029 [in press]
    • B.E. Bannish, J.P. Keener, and A.L. Fogelson Modelling fibrinolysis: a 3D stochastic multiscale model Math Med Biol 2013 10.1093/imammb/dqs029 [in press]
    • (2013) Math Med Biol
    • Bannish, B.E.1    Keener, J.P.2    Fogelson, A.L.3
  • 44
    • 26044469358 scopus 로고    scopus 로고
    • Active carboxypeptidase B is present in free form in serum from patients with acute pancreatitis
    • A. Borgström, and S. Regnér Active carboxypeptidase B is present in free form in serum from patients with acute pancreatitis Pancreatology 5 2005 530 536
    • (2005) Pancreatology , vol.5 , pp. 530-536
    • Borgström, A.1    Regnér, S.2
  • 45
    • 0035046942 scopus 로고    scopus 로고
    • Amino acid kinetics in patients with sepsis
    • W. Druml, G. Heinzel, and G. Kleinberger Amino acid kinetics in patients with sepsis Am J Clin Nutr 73 2001 908 913
    • (2001) Am J Clin Nutr , vol.73 , pp. 908-913
    • Druml, W.1    Heinzel, G.2    Kleinberger, G.3
  • 47
    • 77449151896 scopus 로고    scopus 로고
    • Carboxypeptidase U (TAFIa): A new drug target for fibrinolytic therapy?
    • J.L. Willemse, E. Heylen, M.E. Nesheim, and D.F. Hendriks Carboxypeptidase U (TAFIa): a new drug target for fibrinolytic therapy? J Thromb Haemost 7 2009 1962 1971
    • (2009) J Thromb Haemost , vol.7 , pp. 1962-1971
    • Willemse, J.L.1    Heylen, E.2    Nesheim, M.E.3    Hendriks, D.F.4
  • 48
    • 84878311772 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor: A putative target to enhance fibrinolysis
    • E. Vercauteren, A. Gils, and P.J. Declerck Thrombin activatable fibrinolysis inhibitor: a putative target to enhance fibrinolysis Semin Thromb Hemost 39 2013 365 372
    • (2013) Semin Thromb Hemost , vol.39 , pp. 365-372
    • Vercauteren, E.1    Gils, A.2    Declerck, P.J.3
  • 49
    • 42149166603 scopus 로고    scopus 로고
    • Which carboxypeptidase determines the antifibrinolytic potential?
    • A. Gils Which carboxypeptidase determines the antifibrinolytic potential? J Thromb Haemost 6 2008 846 847
    • (2008) J Thromb Haemost , vol.6 , pp. 846-847
    • Gils, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.