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Volumn 5, Issue 5, 1998, Pages 309-313

Fibrinolysis and the plasma carboxypeptidase

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYPEPTIDASE; ENZYME PRECURSOR; FIBRIN; LYSINE; THROMBIN; THROMBOMODULIN;

EID: 0031696875     PISSN: 10656251     EISSN: None     Source Type: Journal    
DOI: 10.1097/00062752-199809000-00001     Document Type: Review
Times cited : (27)

References (40)
  • 1
    • 0026337077 scopus 로고
    • The coagulation cascade: Initiation, maintenance, and regulation
    • Davie EW, Fujikawa K, Kisiel W: The coagulation cascade: initiation, maintenance, and regulation. Biochemistry 1991, 30:10363-10370.
    • (1991) Biochemistry , vol.30 , pp. 10363-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 2
    • 0004791737 scopus 로고
    • Molecular and cellular basis of fibrinolysis
    • Edited by Hoffman R, Benz E, Shattil S, Furie B, Cohen H. New York: Churchill Livingstone
    • Collen D, Lijnen HR: Molecular and cellular basis of fibrinolysis. In Hematology: Basic Principles and Practice. Edited by Hoffman R, Benz E, Shattil S, Furie B, Cohen H. New York: Churchill Livingstone; 1991:1232-1242.
    • (1991) Hematology: Basic Principles and Practice , pp. 1232-1242
    • Collen, D.1    Lijnen, H.R.2
  • 3
    • 0027161205 scopus 로고
    • Molecular events that control the protein C anticoagulant pathway
    • Esmon CT: Molecular events that control the protein C anticoagulant pathway. Thromb Haemost 1993, 70:29-35.
    • (1993) Thromb Haemost , vol.70 , pp. 29-35
    • Esmon, C.T.1
  • 4
    • 0028300767 scopus 로고
    • The specific roles of finger and kringle 2 domains of tissue-type plasminogen activator during the in vitro fibrinolysis
    • Horrevoets AJG, Smilde A, de Vries C, Pannekoek H: The specific roles of finger and kringle 2 domains of tissue-type plasminogen activator during the in vitro fibrinolysis. J Biol Chem 1994, 269:12639-12644.
    • (1994) J Biol Chem , vol.269 , pp. 12639-12644
    • Horrevoets, A.J.G.1    Smilde, A.2    De Vries, C.3    Pannekoek, H.4
  • 5
    • 0025667113 scopus 로고
    • The dissociation constants and stoichiometries of the interactions of Lys-plasminogen and chloromethyl ketone derivatives of tissue plasminogen activator and the variant dFEIX with intact fibrin
    • Nesheim ME, Fredenburgh JC, Larsen GR: The dissociation constants and stoichiometries of the interactions of Lys-plasminogen and chloromethyl ketone derivatives of tissue plasminogen activator and the variant dFEIX with intact fibrin. J Biol Chem 1990, 265:21541-21548.
    • (1990) J Biol Chem , vol.265 , pp. 21541-21548
    • Nesheim, M.E.1    Fredenburgh, J.C.2    Larsen, G.R.3
  • 6
    • 0023941054 scopus 로고
    • Plasminogen receptors: Ubiquitous sites for cellular regulation of fibrinolysis
    • Miles LA, Plow EF: Plasminogen receptors: ubiquitous sites for cellular regulation of fibrinolysis. Fibrinolysis 1988, 2:61-71.
    • (1988) Fibrinolysis , vol.2 , pp. 61-71
    • Miles, L.A.1    Plow, E.F.2
  • 7
    • 0015866290 scopus 로고
    • Studies on the conformational changes of plasminogen induced during activation to plasmin and by 6-aminohexanoic acid
    • Sjoholm I: Studies on the conformational changes of plasminogen induced during activation to plasmin and by 6-aminohexanoic acid. Eur J Biochem 1973, 39:471-479.
    • (1973) Eur J Biochem , vol.39 , pp. 471-479
    • Sjoholm, I.1
  • 8
    • 0002538356 scopus 로고
    • Alpha 2-antiplasmin
    • Edited by Barrett AJ, Salvesen G. New York: Elsevier Science Publishers BV
    • Lijnen HR, Collen D: Alpha 2-antiplasmin. In Proteinase Inhibitors. Edited by Barrett AJ, Salvesen G. New York: Elsevier Science Publishers BV; 1986:457-476.
    • (1986) Proteinase Inhibitors , pp. 457-476
    • Lijnen, H.R.1    Collen, D.2
  • 9
    • 0025852042 scopus 로고
    • Kinetic characterization of tissue-type plasminogen activator (t-PA) and t-PA deletion mutants
    • de Vries C, Veerman H, Nesheim ME, Pannekoek H: Kinetic characterization of tissue-type plasminogen activator (t-PA) and t-PA deletion mutants. Thromb Haemost 1991, 65:280-285.
    • (1991) Thromb Haemost , vol.65 , pp. 280-285
    • De Vries, C.1    Veerman, H.2    Nesheim, M.E.3    Pannekoek, H.4
  • 10
    • 0025819231 scopus 로고
    • Role of cell-surface lysines in plasminogen binding to cells: Identification of alpha-enolase as a candidate plasminogen receptor
    • Miles LA, Dahlberg CM, Plescia J, Felez J, Kato K, Plow EF: Role of cell-surface lysines in plasminogen binding to cells: identification of alpha-enolase as a candidate plasminogen receptor. Biochemistry 1991, 30:1682-1691.
    • (1991) Biochemistry , vol.30 , pp. 1682-1691
    • Miles, L.A.1    Dahlberg, C.M.2    Plescia, J.3    Felez, J.4    Kato, K.5    Plow, E.F.6
  • 11
    • 0025938614 scopus 로고
    • The effect of the carboxy-terminal lysine of urokinase on the catalysis of plasminogen activation
    • Lenich C, Pannell R, Gurewich V: The effect of the carboxy-terminal lysine of urokinase on the catalysis of plasminogen activation. Thromb Res 1991, 64:69-80.
    • (1991) Thromb Res , vol.64 , pp. 69-80
    • Lenich, C.1    Pannell, R.2    Gurewich, V.3
  • 12
    • 0025718644 scopus 로고
    • Characterization of the binding of plasminogen to fibrin surfaces: The role of carboxy-terminal lysines
    • Fleury V, Angles-Cano E: Characterization of the binding of plasminogen to fibrin surfaces: the role of carboxy-terminal lysines. Biochemistry 1991, 30:7630-7638.
    • (1991) Biochemistry , vol.30 , pp. 7630-7638
    • Fleury, V.1    Angles-Cano, E.2
  • 13
    • 0023840635 scopus 로고
    • Complementary modes of action of tissue-type plasminogen activator and pro-urokinase by which their synergistic effect on clot lysis may be explained
    • Pannell R, Black J, Gurewich V: Complementary modes of action of tissue-type plasminogen activator and pro-urokinase by which their synergistic effect on clot lysis may be explained. J Clin Invest 1988, 81:853-859.
    • (1988) J Clin Invest , vol.81 , pp. 853-859
    • Pannell, R.1    Black, J.2    Gurewich, V.3
  • 15
    • 0025748556 scopus 로고
    • Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma
    • Eaton DL, Malloy BE, Tsai SP, Henzel W, Drayna D: Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. J Biol Chem 1991, 269:21833-21838.
    • (1991) J Biol Chem , vol.269 , pp. 21833-21838
    • Eaton, D.L.1    Malloy, B.E.2    Tsai, S.P.3    Henzel, W.4    Drayna, D.5
  • 16
    • 0029023651 scopus 로고
    • Activation and characterization of procarboxypeptidase B from human plasma
    • Tan AK, Eaton DL: Activation and characterization of procarboxypeptidase B from human plasma. Biochemistry 1995, 34:5811-5816.
    • (1995) Biochemistry , vol.34 , pp. 5811-5816
    • Tan, A.K.1    Eaton, D.L.2
  • 17
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin activatable fibrinolysis inhibitor
    • Bajzar L, Manuel R, Nesheim ME: Purification and characterization of TAFI, a thrombin activatable fibrinolysis inhibitor. J Biol Chem 1995, 270:14477-14484.
    • (1995) J Biol Chem , vol.270 , pp. 14477-14484
    • Bajzar, L.1    Manuel, R.2    Nesheim, M.E.3
  • 18
    • 10544253848 scopus 로고    scopus 로고
    • Coagulation-dependent inhibition of fibrinolysis: Role of carboxypeptidase-U and the premature lysis of clots from hemophilic plasma
    • Broze GJ Jr, Higuchi DA: Coagulation-dependent inhibition of fibrinolysis: role of carboxypeptidase-U and the premature lysis of clots from hemophilic plasma. Blood 1996, 88:3815-3823.
    • (1996) Blood , vol.88 , pp. 3815-3823
    • Broze Jr., G.J.1    Higuchi, D.A.2
  • 19
    • 0030962331 scopus 로고    scopus 로고
    • Thrombin mediated activation of factor XI in a TAFI (thrombin activatable fibrinolysis inhibitor) dependent inhibition of fibrinolysis
    • von dem Borne PA, Bajzar L, Meijers JCM, Nesheim ME, Bouma BN: • Thrombin mediated activation of factor XI in a TAFI (thrombin activatable fibrinolysis inhibitor) dependent inhibition of fibrinolysis. J Clin Invest 1997, 99:2323-2327. Demonstrates that the intrinsic pathway mediates inhibition of fibrinolysis and that the process is dependent on TAFI.
    • (1997) J Clin Invest , vol.99 , pp. 2323-2327
    • Von Dem Borne, P.A.1    Bajzar, L.2    Meijers, J.C.M.3    Nesheim, M.E.4    Bouma, B.N.5
  • 20
    • 0029895009 scopus 로고    scopus 로고
    • TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex
    • Bajzar L, Morser J, Nesheim M: TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. J Biol Chem 1996, 271:16603-16608.
    • (1996) J Biol Chem , vol.271 , pp. 16603-16608
    • Bajzar, L.1    Morser, J.2    Nesheim, M.3
  • 21
    • 0028815556 scopus 로고
    • Plasma carboxypeptidases as regulators of the plasminogen system
    • Redlitz A, Tan AK, Eaton DL, Plow EF: Plasma carboxypeptidases as regulators of the plasminogen system. J Clin Invest 1995, 96:2534-2538.
    • (1995) J Clin Invest , vol.96 , pp. 2534-2538
    • Redlitz, A.1    Tan, A.K.2    Eaton, D.L.3    Plow, E.F.4
  • 22
    • 0030742896 scopus 로고    scopus 로고
    • Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis
    • Nesheim M, Wang W, Boffa M, Nagashima M, Morser J, Bajzar L: • Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis. Thromb Haemost 1997, 78:386-391. A recent review of the properties and role of the plasma carboxypeptidase.
    • (1997) Thromb Haemost , vol.78 , pp. 386-391
    • Nesheim, M.1    Wang, W.2    Boffa, M.3    Nagashima, M.4    Morser, J.5    Bajzar, L.6
  • 23
    • 0028222563 scopus 로고
    • Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen
    • Wang W, Hendriks DF, Scharpe SS: Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen. J Biol Chem 1994, 269:15937-15944.
    • (1994) J Biol Chem , vol.269 , pp. 15937-15944
    • Wang, W.1    Hendriks, D.F.2    Scharpe, S.S.3
  • 24
    • 0027419521 scopus 로고
    • The effect of activated protein C on fibrinolysis in cell-free plasma can be attributed specifically to attenuation of prothrombin activation
    • Bajzar L, Nesheim M: The effect of activated protein C on fibrinolysis in cell-free plasma can be attributed specifically to attenuation of prothrombin activation. J Biol Chem 1993, 268:8608-8616.
    • (1993) J Biol Chem , vol.268 , pp. 8608-8616
    • Bajzar, L.1    Nesheim, M.2
  • 26
    • 0029793068 scopus 로고    scopus 로고
    • The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent
    • Bajzar L, Nesheim ME, Tracy PB: The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent. Blood 1996, 88:2093-2100.
    • (1996) Blood , vol.88 , pp. 2093-2100
    • Bajzar, L.1    Nesheim, M.E.2    Tracy, P.B.3
  • 27
    • 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
    • Boffa MB, Wang W, Bajzar L, Nesheim ME: 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 1998, 273:2127-2135. Provides a comparison of plasma and recombinant TAFI and characterizes the intrinsic instability of TAFIa.
    • (1998) J Biol Chem , vol.273 , pp. 2127-2135
    • Boffa, M.B.1    Wang, W.2    Bajzar, L.3    Nesheim, M.E.4
  • 28
    • 0030589619 scopus 로고    scopus 로고
    • The gene for human carboxypeptidase U (CPU): A proposed novel regulator of plasminogen activation-maps to 13q14.11
    • Vanhoof G, Wauters J, Schatteman K, Hendriks D, Goossens F, Bossuyt P, Scharpe S: The gene for human carboxypeptidase U (CPU): a proposed novel regulator of plasminogen activation-maps to 13q14.11. Genomics 1996, 38:454-455.
    • (1996) Genomics , vol.38 , pp. 454-455
    • Vanhoof, G.1    Wauters, J.2    Schatteman, K.3    Hendriks, D.4    Goossens, F.5    Bossuyt, P.6    Scharpe, S.7
  • 29
    • 0030920922 scopus 로고    scopus 로고
    • On the mechanism of the antifibrinolytic activity of plasma carboxypeptidase B
    • Sakharov DV, Plow EF, Rijken DC: On the mechanism of the antifibrinolytic • activity of plasma carboxypeptidase B. J Biol Chem 1997, 272:14477-14482. Analyzes the mechanism of inhibition of fibrinolysis by the plasma carboxypeptidase. The authors also show inhibition of fibrinolysis even at high levels of tissue plasminogen activator, such as those achieved in therapeutic thrombolysis.
    • (1997) J Biol Chem , vol.272 , pp. 14477-14482
    • Sakharov, D.V.1    Plow, E.F.2    Rijken, D.C.3
  • 30
    • 33846677222 scopus 로고    scopus 로고
    • A study of the mechanism of inhibition of tPA-mediated fibrinolysis by activated TAFI
    • abstract 278
    • Wang W, Boffa MB, Walker J, Nesheim ME: A study of the mechanism of inhibition of tPA-mediated fibrinolysis by activated TAFI [abstract]. Fibrinolysis 1996, 10 (abstract 278):82.
    • (1996) Fibrinolysis , vol.10 , pp. 82
    • Wang, W.1    Boffa, M.B.2    Walker, J.3    Nesheim, M.E.4
  • 31
    • 7844220411 scopus 로고
    • A study of the mechanism of inhibition of fibrinolysis by activated TAFI
    • in press
    • Wang W, Boffa MB, Bajzar L, Walker JB, Nesheim ME: A study of the • mechanism of inhibition of fibrinolysis by activated TAFI. J Biol Chem 1988, in press. Provides a quantitative analysis of the mechanism of inhibition of fibrinolysis by TAFIa.
    • (1988) J Biol Chem
    • Wang, W.1    Boffa, M.B.2    Bajzar, L.3    Walker, J.B.4    Nesheim, M.E.5
  • 32
    • 17544370936 scopus 로고    scopus 로고
    • Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha 2 macroglobulin and pregnancy zone protein
    • Valnickova Z, Thogersen IB, Christensen S, Chu CT, Pizzo SV, Enghild JJ: Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha 2 macroglobulin and pregnancy zone protein. J Biol Chem 1996, 271:12937-12943.
    • (1996) J Biol Chem , vol.271 , pp. 12937-12943
    • Valnickova, Z.1    Thogersen, I.B.2    Christensen, S.3    Chu, C.T.4    Pizzo, S.V.5    Enghild, J.J.6
  • 33
    • 0032579276 scopus 로고    scopus 로고
    • Both cellular and soluble forms of thrombomodulin inhibit fibrinolysis by potentiating the activation of thrombin-activable fibrinolysis inhibitor
    • Bajzar L, Nesheim ME, Morser J, Tracy PB: Both cellular and soluble forms • of thrombomodulin inhibit fibrinolysis by potentiating the activation of thrombin-activable fibrinolysis inhibitor. J Biol Chem 1998, 273:2792-2798. Endothelial cell thrombomodulin promotes TAFI activation and suppression of fibrinolysis.
    • (1998) J Biol Chem , vol.273 , pp. 2792-2798
    • Bajzar, L.1    Nesheim, M.E.2    Morser, J.3    Tracy, P.B.4
  • 35
    • 0031974703 scopus 로고    scopus 로고
    • Enhancement of jugular vein thrombolysis by neutralization of factor XI: In vivo evidence for a role of factor XI as an antifibrinolytic factor
    • Minnema MC, Friedrich PW, Levi M, von dem Borne PAK, Mosnier LQ, • Meijers JCM, Biemond BJ, Hack CE, Bouma BN, ten Cate H: Enhancement of jugular vein thrombolysis by neutralization of factor XI: in vivo evidence for a role of factor XI as an antifibrinolytic factor. J Clin Invest 1998, 101:1-5. This article shows factor XI-dependent inhibition of fibrinolysis in vivo, and that inhibition of factor XI enhances endogenous lysis of jugular vein clots in rabbits.
    • (1998) J Clin Invest , vol.101 , pp. 1-5
    • Minnema, M.C.1    Friedrich, P.W.2    Levi, M.3    Von Dem Borne, P.A.K.4    Mosnier, L.Q.5    Meijers, J.C.M.6    Biemond, B.J.7    Hack, C.E.8    Bouma, B.N.9    Ten Cate, H.10
  • 36
    • 0030944354 scopus 로고    scopus 로고
    • Thrombosis: Theoretical considerations
    • Mann KG: Thrombosis: Theoretical considerations. Am J Clin Nutr 1997, 65(suppl):1657S-1664S.
    • (1997) Am J Clin Nutr , vol.65 , Issue.SUPPL.
    • Mann, K.G.1
  • 37
    • 0029294604 scopus 로고
    • Molecular genetics of thrombophilia: Factor V gene mutation causing resistance to activated protein C as a basis of the hypercoagulable state
    • Dahlback B: Molecular genetics of thrombophilia: factor V gene mutation causing resistance to activated protein C as a basis of the hypercoagulable state. J Lab Clin Med 1995, 125:566-571.
    • (1995) J Lab Clin Med , vol.125 , pp. 566-571
    • Dahlback, B.1
  • 38
  • 39
    • 1642530216 scopus 로고    scopus 로고
    • Increased tissue factor-initiated prothrombin activation as a result of the Arg 506 → Gln mutation in factor V Leiden
    • van't Veer C, Kalafatis M, Bertina RM, Simioni P, Mann KG: Increased • tissue factor-initiated prothrombin activation as a result of the Arg 506 → Gln mutation in factor V Leiden. J Biol Chem 1997, 272:20721-20729. Provides a definitive analysis of the kinetic defect in factor V Leiden.
    • (1997) J Biol Chem , vol.272 , pp. 20721-20729
    • Van't Veer, C.1    Kalafatis, M.2    Bertina, R.M.3    Simioni, P.4    Mann, K.G.5
  • 40
    • 0029810712 scopus 로고    scopus 로고
    • An antifibrinolytic mechanism describing the prothrombotic effect associated with factor V Leiden
    • Bajzar L, Kalafatis M, Simioni P, Tracy PB: An antifibrinolytic mechanism describing the prothrombotic effect associated with factor V Leiden. J Biol Chem 1996, 271:22949-22952
    • (1996) J Biol Chem , vol.271 , pp. 22949-22952
    • Bajzar, L.1    Kalafatis, M.2    Simioni, P.3    Tracy, P.B.4


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