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Volumn 9, Issue 10, 2009, Pages 1165-1173

Recent developments in thrombin-activatable fibrinolysis inhibitor research

Author keywords

Carboxypeptidase B; Carboxypeptidase R; Carboxypeptidase U; Fibrinolysis; Inflammation; TAFI

Indexed keywords

ANTIFIBRINOLYTIC AGENT; ARGININE CARBOXYPEPTIDASE; CARBOXYPEPTIDASE; ENZYME PRECURSOR; METALLOCARBOXYPEPTIDASE; THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR; THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR A; THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR A INHIBITOR; UNCLASSIFIED DRUG;

EID: 70450212621     PISSN: 13895575     EISSN: None     Source Type: Journal    
DOI: 10.2174/138955709789055216     Document Type: Review
Times cited : (12)

References (122)
  • 1
    • 42149166603 scopus 로고    scopus 로고
    • Which carboxypeptidase determines the antifibrinolytic potential?
    • Gils, A. Which carboxypeptidase determines the antifibrinolytic potential? J. Thromb. Haemost., 2008, 6, 846-847
    • (2008) J. Thromb. Haemost. , vol.6 , pp. 846-847
    • Gils, A.1
  • 2
    • 33947585401 scopus 로고    scopus 로고
    • Curiouser and curiouser: Recent advances in measurement of thrombin-activatable fibrinolysis inhibitor (TAFI) and in understanding its molecular genetics, gene regulation, and biological roles
    • Boffa, M. B.; Koschinsky, M. L. Curiouser and curiouser: recent advances in measurement of thrombin-activatable fibrinolysis inhibitor (TAFI) and in understanding its molecular genetics, gene regulation, and biological roles. Clin. Biochem., 2007, 40, 431-442
    • (2007) Clin. Biochem. , vol.40 , pp. 431-442
    • Boffa, M.B.1    Koschinsky, M.L.2
  • 3
    • 33749257998 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor (TAFI) - How does thrombin regulate fibrinolysis?
    • DOI 10.1080/07853890600852898, PII X4576337755P7877
    • Bouma, B. N.; Mosnier, L. O. Thrombin activatable fibrinolysis inhibitor (TAFI)-how does thrombin regulate fibrinolysis? Ann. Med., 2006, 38, 378-388 (Pubitemid 44484876)
    • (2006) Annals of Medicine , vol.38 , Issue.6 , pp. 378-388
    • Bouma, B.N.1    Mosnier, L.O.2
  • 4
    • 34147159934 scopus 로고    scopus 로고
    • A role for procarboxypepidase U (TAFI) in thrombosis
    • Willemse, J. L.; Hendriks, D. F. A role for procarboxypepidase U (TAFI) in thrombosis. Front Biosci., 2007, 12, 1973-1987
    • (2007) Front Biosci. , vol.12 , pp. 1973-1987
    • Willemse, J.L.1    Hendriks, D.F.2
  • 5
    • 33750222459 scopus 로고    scopus 로고
    • Regulation of fibrinolysis by thrombin activatable fibrinolysis inhibitor, an unstable carboxypeptidase B that unites the pathways of coagulation and fibrinolysis
    • Mosnier, L. O.; Bouma, B. N. Regulation of fibrinolysis by thrombin activatable fibrinolysis inhibitor, an unstable carboxypeptidase B that unites the pathways of coagulation and fibrinolysis. Arterioscler. Thromb. Vasc. Biol., 2006, 26, 2445-2453
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 2445-2453
    • Mosnier, L.O.1    Bouma, B.N.2
  • 6
    • 24944454291 scopus 로고    scopus 로고
    • Carboxypeptidase U (TAFIa): A metallocarboxypeptidase with a distinct role in haemostasis and a possible risk factor for thrombotic disease
    • Leurs, J.; Hendriks, D. Carboxypeptidase U (TAFIa): a metallocarboxypeptidase with a distinct role in haemostasis and a possible risk factor for thrombotic disease. Thromb. Haemost., 2005, 94, 471-487
    • (2005) Thromb. Haemost. , vol.94 , pp. 471-487
    • Leurs, J.1    Hendriks, D.2
  • 7
    • 14044259258 scopus 로고    scopus 로고
    • Thrombin Activatable Fibrinolysis Inhibitor (TAFI) at the interface between coagulation and fibrinolysis
    • DOI 10.1159/000083832
    • Bouma, B. N.; Mosnier, L. O. Thrombin activatable fibrinolysis inhibitor (TAFI) at the interface between coagulation and fibrinolysis. Pathophysiol. Haemost. Thromb., 2003, 33, 375-381 (Pubitemid 40278711)
    • (2003) Pathophysiology of Haemostasis and Thrombosis , vol.33 , Issue.5-6 , pp. 375-381
    • Bouma, B.N.1    Mosnier, L.O.2
  • 8
    • 4444287314 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor
    • Marx, P. F. Thrombin-activatable fibrinolysis inhibitor. Curr. Med. Chem., 2004, 11, 2311-2324
    • (2004) Curr. Med. Chem. , vol.11 , pp. 2311-2324
    • Marx, P.F.1
  • 9
    • 67349254675 scopus 로고    scopus 로고
    • New insights into the molecular mechanisms of the fibrinolytic system
    • Rijken, D. C.; Lijnen, H. R. New insights into the molecular mechanisms of the fibrinolytic system. J. Thromb. Haemost., 2008.
    • (2008) J. Thromb. Haemost.
    • Rijken, D.C.1    Lijnen, H.R.2
  • 10
    • 58149328581 scopus 로고    scopus 로고
    • Regulation of tissue inflammation by thrombin-activatable carboxypeptidase B (or TAFI)
    • Leung, L. L.; Nishimura, T.; Myles, T. Regulation of tissue inflammation by thrombin-activatable carboxypeptidase B (or TAFI). Adv. Exp. Med. Biol., 2008, 632, 61-69
    • (2008) Adv. Exp. Med. Biol. , vol.632 , pp. 61-69
    • Leung, L.L.1    Nishimura, T.2    Myles, T.3
  • 11
    • 36148996511 scopus 로고    scopus 로고
    • Thrombin-thrombomodulin connects coagulation and fibrinolysis: More than an in vitro phenomenon
    • DOI 10.1182/blood-2007-03-078824
    • Binette, T. M.; Taylor, F. B., Jr.; Peer, G.; Bajzar, L. Thrombin-thrombomodulin connects coagulation and fibrinolysis: more than an in vitro phenomenon. Blood, 2007, 110, 3168-3175 (Pubitemid 350106308)
    • (2007) Blood , vol.110 , Issue.9 , pp. 3168-3175
    • Binette, T.M.1    Taylor Jr., F.B.2    Peer, G.3    Bajzar, L.4
  • 12
    • 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
  • 13
    • 0025748556 scopus 로고
    • Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma
    • Eaton, D. L.; Malloy, B. E.; Tsai, S. P.; Henzel, W.; Drayna, D. Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. J. Biol. Chem., 1991, 266, 21833-21838 (Pubitemid 121000257)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.32 , pp. 21833-21838
    • Eaton, D.L.1    Malloy, B.E.2    Tsai, S.P.3    Henzel, W.4    Drayna, D.5
  • 14
    • 0033521034 scopus 로고    scopus 로고
    • Characterization of plasmin-mediated activation of plasma procarboxypeptidase B - Modulation by glycosaminoglycans
    • Mao, S. S.; Cooper, C. M.; Wood, T.; Shafer, J. A.; Gardell, S. J. Characterization of plasmin-mediated activation of plasma procarboxypeptidase B - modulation by glycosaminoglycans. J. Biol. Chem., 1999, 274, 35046-35052
    • (1999) J. Biol. Chem. , vol.274 , pp. 35046-35052
    • Mao, S.S.1    Cooper, C.M.2    Wood, T.3    Shafer, J.A.4    Gardell, S.J.5
  • 15
    • 0037188376 scopus 로고    scopus 로고
    • Plasmin-mediated activation and inactivation of thrombin-activatable fibrinolysis inhibitor
    • DOI 10.1021/bi015982e
    • Marx, P. F.; Dawson, P. E.; Bouma, B. N.; Meijers, J. C. Plasmin-mediated activation and inactivation of thrombin-activatable fibrinolysis inhibitor. Biochemistry, 2002, 41, 6688-6696 (Pubitemid 34547359)
    • (2002) Biochemistry , vol.41 , Issue.21 , pp. 6688-6696
    • Marx, P.F.1    Dawson, P.E.2    Bouma, B.N.3    Meijers, J.C.M.4
  • 16
    • 0036221061 scopus 로고    scopus 로고
    • Elastase from activated human neutrophils activates procarboxypeptidase R
    • Kawamura, T.; Okada, N.; Okada, H. Elastase from activated human neutronpils activates procarboxypeptidase R. Microbiol. Immunol., 2002, 46, 225-230 (Pubitemid 34289020)
    • (2002) Microbiology and Immunology , vol.46 , Issue.3 , pp. 225-230
    • Kawamura, T.1    Okada, N.2    Okada, H.3
  • 17
    • 0034725047 scopus 로고    scopus 로고
    • Inactivation of activated thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage
    • Marx, P. F.; Hackeng, T. M.; Dawson, P. E.; Griffin, J. H.; Meijers, J. C. M.; Bouma, B. N. Inactivation of activated thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage. J. Biol. Chem., 2000, 275, 12410-12415
    • (2000) J. Biol. Chem. , vol.275 , pp. 12410-12415
    • Marx, P.F.1    Hackeng, T.M.2    Dawson, P.E.3    Griffin, J.H.4    Meijers, J.C.M.5    Bouma, B.N.6
  • 18
    • 0034725120 scopus 로고    scopus 로고
    • Roles of thermal instability and proteolytic cleavage in regulation of activated thrombin-activable fibrinolysis inhibitor
    • Boffa, M. B.; Bell, R.; Stevens, W. K.; Nesheim, M. E. Roles of thermal instability and proteolytic cleavage in regulation of activated thrombin-activable fibrinolysis inhibitor. J. Biol. Chem., 2000, 275, 12868-12878
    • (2000) J. Biol. Chem. , vol.275 , pp. 12868-12878
    • Boffa, M.B.1    Bell, R.2    Stevens, W.K.3    Nesheim, M.E.4
  • 19
    • 0037192169 scopus 로고    scopus 로고
    • Role of zinc ions in activation and inactivation of thrombin-activatable fibrinolysis inhibitor
    • DOI 10.1021/bi0115683
    • Marx, P. F.; Bouma, B. N.; Meijers, J. C. Role of zinc ions in activation and inactivation of thrombin-activatable fibrinolysis inhibitor. Biochemistry, 2002, 41, 1211-1216 (Pubitemid 34083773)
    • (2002) Biochemistry , vol.41 , Issue.4 , pp. 1211-1216
    • Marx, P.F.1    Bouma, B.N.2    Meijers, J.C.M.3
  • 20
    • 70450138147 scopus 로고    scopus 로고
    • The activation peptide of thrombin-activatable fibrinolysis inhibitor: A role in activity and stability of the enzyme?
    • Marx, P. F.; Plug, T.; Havik, S. R.; Morgelin, M.; Meijers, J. C. The activation peptide of thrombin-activatable fibrinolysis inhibitor: a role in activity and stability of the enzyme? J. Thromb. Haemost., 2008,
    • (2008) J. Thromb. Haemost.
    • Marx, P.F.1    Plug, T.2    Havik, S.R.3    Morgelin, M.4    Meijers, J.C.5
  • 21
    • 1342346593 scopus 로고    scopus 로고
    • Generation and characterization of a highly stable form of activated thrombin-activable fibrinolysis inhibitor
    • Marx, P. F.; Havik, S. R.; Marquart, J. A.; Bouma, B. N.; Meijers, J. C. M. Generation and characterization of a highly stable form of activated thrombin-activable fibrinolysis inhibitor. J. Biol. Chem., 2004, 279, 6620-6628
    • (2004) J. Biol. Chem. , vol.279 , pp. 6620-6628
    • Marx, P.F.1    Havik, S.R.2    Marquart, J.A.3    Bouma, B.N.4    Meijers, J.C.M.5
  • 22
    • 24944454310 scopus 로고    scopus 로고
    • Role of isoleucine residues 182 and 183 in thrombin-activatable fibrinolysis inhibitor
    • Marx, P. F.; Havik, S. R.; Bouma, B. N.; Meijers, J. C. M. Role of isoleucine residues 182 and 183 in thrombin-activatable fibrinolysis inhibitor. J. Thromb. Haemost., 2005, 3, 1293-1300
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 1293-1300
    • Marx, P.F.1    Havik, S.R.2    Bouma, B.N.3    Meijers, J.C.M.4
  • 23
    • 33644952604 scopus 로고    scopus 로고
    • Limited mutagenesis increases the stability of human carboxypeptidase U (TAFIa) and demonstrates the importance of CPU stability over proCPU concentration in down-regulating fibrinolysis
    • Knecht, W.; Willemse, J.; Stenhamre, H.; Andersson, M.; Berntsson, P.; Furebring, C.; Harrysson, A.; Hager, A. C.; Wissing, B. M.; Hendriks, D.; Cronet, P. Limited mutagenesis increases the stability of human carboxypeptidase U (TAFIa) and demonstrates the importance of CPU stability over proCPU concentration in down-regulating fibrinolysis. FEBS J., 2006, 273, 778-792
    • (2006) FEBS J. , vol.273 , pp. 778-792
    • Knecht, W.1    Willemse, J.2    Stenhamre, H.3    Andersson, M.4    Berntsson, P.5    Furebring, C.6    Harrysson, A.7    Hager, A.C.8    Wissing, B.M.9    Hendriks, D.10    Cronet, P.11
  • 24
    • 34548840834 scopus 로고    scopus 로고
    • Comparative evaluation of stable TAFIa variants: Importance of alpha-helix 9 and beta-sheet 11 for TAFIa (in)stability
    • DOI 10.1111/j.1538-7836.2007.02720.x
    • Ceresa, E.; De Maeyer, M.; Jonckheer, A.; Peeters, M.; Engelborghs, Y.; Declerck, P. J.; Gils, A. Comparative evaluation of stable TAFIa variants: importance of alpha-helix 9 and beta-sheet 11 for TAFIa (in)stability. J. Thromb. Haemost., 2007, 5, 2105-2112 (Pubitemid 47450030)
    • (2007) Journal of Thrombosis and Haemostasis , vol.5 , Issue.10 , pp. 2105-2112
    • Ceresa, E.1    De Maeyer, M.2    Jonckheer, A.3    Peeters, M.4    Engelborghs, Y.5    Declerck, P.J.6    Gils, A.7
  • 25
    • 33846444017 scopus 로고    scopus 로고
    • Announcing a TAFIa mutant with a 180-fold increased half-life and concomitantly a strongly increased antifibrinolytic potential [4]
    • DOI 10.1111/j.1538-7836.2007.02322.x
    • Ceresa, E.; Peeters, M.; Declerck, P. J.; Gils, A. Announcing a TAFIa mutant with a 180-fold increased half-life and concomitantly a strongly increased antifibrinolytic potential. J. Thromb. Haemost., 2007, 5, 418-420 (Pubitemid 46139471)
    • (2007) Journal of Thrombosis and Haemostasis , vol.5 , Issue.2 , pp. 418-420
    • Ceresa, E.1    Peeters, M.2    Declerck, P.J.3    Gils, A.4
  • 27
    • 53449101060 scopus 로고    scopus 로고
    • Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI; a novel mechanism for enzyme auto-regulation
    • Marx, P. F.; Brondijk, T. H.; Plug, T.; Romijn, R. A.; Hemrika, W.; Meijers, J. C.; Huizinga, E. G. Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI; A novel mechanism for enzyme auto-regulation. Blood, 2008, 112, 2803-2809
    • (2008) Blood , vol.112 , pp. 2803-2809
    • Marx, P.F.1    Brondijk, T.H.2    Plug, T.3    Romijn, R.A.4    Hemrika, W.5    Meijers, J.C.6    Huizinga, E.G.7
  • 31
    • 0025977159 scopus 로고
    • Three-dimensional structure of porcine procarboxypeptidase B: A structural basis of its inactivity
    • Coll, M.; Guasch, A.; Avilés, F. X.; Huber, R. Three-dimensional structure of pocine procarboxypeptidase B: a structural basis of its inactivity. EMBO J., 1991, 10, 1-9. (Pubitemid 21905260)
    • (1991) EMBO Journal , vol.10 , Issue.1 , pp. 1-9
    • Coll, M.1    Guasch, A.2    Aviles, F.X.3    Huber, R.4
  • 32
    • 0026548881 scopus 로고
    • Three-dimensional structure of procine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation
    • Guasch, A.; Coll, M.; Aviles, F. X.; Huber, R. Three-dimensional structure of procine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation. J. Mol. Biol., 1992, 224, 141-157
    • (1992) J. Mol. Biol. , vol.224 , pp. 141-157
    • Guasch, A.1    Coll, M.2    Aviles, F.X.3    Huber, R.4
  • 33
    • 0040974381 scopus 로고    scopus 로고
    • The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen
    • Garcia-Saez, I.; Reverter, D.; Vendrell, J.; Aviles, F. X.; Coll, M. The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen. EMBO J., 1997, 16, 6906-6913 (Pubitemid 27520791)
    • (1997) EMBO Journal , vol.16 , Issue.23 , pp. 6906-6913
    • Garcia-Saez, I.1    Reverter, D.2    Vendrell, J.3    Aviles, F.X.4    Coll, M.5
  • 34
    • 0029114209 scopus 로고
    • The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C
    • Gomis-Ruth, F. X.; Gomez, M.; Bode, W.; Huber, R.; Aviles, F. X. The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C. EMBO J., 1995, 14, 4387-4394
    • (1995) EMBO J. , vol.14 , pp. 4387-4394
    • Gomis-Ruth, F.X.1    Gomez, M.2    Bode, W.3    Huber, R.4    Aviles, F.X.5
  • 35
    • 32244438306 scopus 로고    scopus 로고
    • Post-translational modifications of human thrombin-activatable fibrinolysis inhibitor (TAFI): Evidence for a large shift in the isoelectric point and reduced solubility upon activation
    • Valnickova, Z.; Christensen, T.; Skottrup, P.; Thogersen, I. B.; Hojrup, P.; Enghild, J. J. Post-translational modifications of human thrombin-activatable fibrinolysis inhibitor (TAFI): evidence for a large shift in the isoelectric point and reduced solubility upon activation. Biochemistry, 2006, 45, 1525-1535
    • (2006) Biochemistry , vol.45 , pp. 1525-1535
    • Valnickova, Z.1    Christensen, T.2    Skottrup, P.3    Thogersen, I.B.4    Hojrup, P.5    Enghild, J.J.6
  • 36
    • 39449126006 scopus 로고    scopus 로고
    • Biochemical importance of glycosylation in thrombin activatable fibrinolysis inhibitor
    • DOI 10.1161/CIRCRESAHA.107.157099
    • Buelens, K.; Hillmayer, K.; Compernolle, G.; Declerck, P. J.; Gils, A. Biochemical importance of glycosylation in thrombin activatable fibrinolysis inhibitor. Circ. Res., 2008, 102, 295-301. (Pubitemid 351271649)
    • (2008) Circulation Research , vol.102 , Issue.3 , pp. 295-301
    • Buelens, K.1    Hillmayer, K.2    Compernolle, G.3    Declerck, P.J.4    Gils, A.5
  • 37
    • 34047264612 scopus 로고    scopus 로고
    • Thrombin-activable fibrinolysis inhibitor (TAFI) zymogen is an active carboxypeptidase
    • Valnickova, Z.; Thogersen, I. B.; Potempa, J.; Enghild, J. J. Thrombin-activable fibrinolysis inhibitor (TAFI) zymogen is an active carboxypeptidase. J. Biol. Chem., 2007, 282, 3066-3076
    • (2007) J. Biol. Chem. , vol.282 , pp. 3066-3076
    • Valnickova, Z.1    Thogersen, I.B.2    Potempa, J.3    Enghild, J.J.4
  • 38
    • 33747165030 scopus 로고    scopus 로고
    • The intrinsic enzymatic activity of plasma procarboxypeptidase U (TAFI) can interfere with plasma carboxypeptidase N assays
    • willemse, J. L.; Polla, M.; Hendriks, D. F. The intrinsic enzymatic activity of plasma procarboxypeptidase U (TAFI) can interfere with plasma carboxypeptidase N assays. Anal. Biochem., 2006, 356, 157-159
    • (2006) Anal. Biochem. , vol.356 , pp. 157-159
    • Willemse, J.L.1    Polla, M.2    Hendriks, D.F.3
  • 39
    • 44049087406 scopus 로고    scopus 로고
    • Thrombin-activable fibrinolysis inhibitor zymogen does not play a significant role in the attenuation of fibrinolysis
    • Foley, J. H.; Kim, P.; Nesheim, M. E. Thrombin-activable fibrinolysis inhibitor zymogen does not play a significant role in the attenuation of fibrinolysis. J. Biol. Chem., 2008, 283, 8863-8867
    • (2008) J. Biol. Chem. , vol.283 , pp. 8863-8867
    • Foley, J.H.1    Kim, P.2    Nesheim, M.E.3
  • 40
    • 34250176224 scopus 로고    scopus 로고
    • The intrinsic enzymatic activity of procarboxypeptidase U (TAFI) does not significantly influence the fibrinolysis rate: A rebuttal [7]
    • DOI 10.1111/j.1538-7836.2007.02539.x
    • Willemse, J. L.; Heylen, E.; Hendriks, D. F. The intrinsic enzymatic activity of procarboxypeptidase U (TAFI) does not significantly influence the fibrinolysis rate: a rebuttal. J. Thromb. Haemost., 2007, 5, 1334-1336 (Pubitemid 46902143)
    • (2007) Journal of Thrombosis and Haemostasis , vol.5 , Issue.6 , pp. 1334-1336
    • Willemse, J.L.1    Heylen, E.2    Hendriks, D.F.3
  • 45
    • 46749103227 scopus 로고    scopus 로고
    • TAFIa inhibitors in the treatment of thrombosis
    • Bunnage, M. E.; Owen, D. R. TAFIa inhibitors in the treatment of thrombosis. Curr. Opin. Drug Discov. Dev., 2008, 11, 480-486
    • (2008) Curr. Opin. Drug Discov. Dev. , vol.11 , pp. 480-486
    • Bunnage, M.E.1    Owen, D.R.2
  • 48
    • 33645563991 scopus 로고    scopus 로고
    • Murine model of ferric chloride-induced vena cava thrombosis: Evidence for effect of potato carboxypeptidase inhibitor
    • Wang, X.; Smith, P. L.; Hsu, M. Y.; Ogletree, M. L.; Schumacher, W. A. Murine model of ferric chloride-induced vena cava thrombosis: evidence for effect of potato carboxypeptidase inhibitor. J. Thromb. Haemost., 2006, 4, 403-410
    • (2006) J. Thromb. Haemost. , vol.4 , pp. 403-410
    • Wang, X.1    Smith, P.L.2    Hsu, M.Y.3    Ogletree, M.L.4    Schumacher, W.A.5
  • 49
    • 29244465865 scopus 로고    scopus 로고
    • Modulation of TAFI function through different pathways -implications for the development of TAFI inhibitors
    • Gils, A.; Ceresa, E.; Macovei, A. M.; Marx, P. F.; Peeters, M.; Compernolle, G.; Declerck, P. J. Modulation of TAFI function through different pathways - implications for the development of TAFI inhibitors. J. Thromb. Haemost., 2005, 3, 2745-2753
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 2745-2753
    • Gils, A.1    Ceresa, E.2    Macovei, A.M.3    Marx, P.F.4    Peeters, M.5    Compernolle, G.6    Declerck, P.J.7
  • 50
    • 0141484363 scopus 로고    scopus 로고
    • Reversible inhibitors of TAFIa can both promote and inhibit fibrinolysis
    • Schneider, M.; Nesheim, M. Reversible inhibitors of TAFIa can both promote and inhibit fibrinolysis. J. Thromb. Haemost., 2003, 1, 147-154
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 147-154
    • Schneider, M.1    Nesheim, M.2
  • 51
    • 0037646413 scopus 로고    scopus 로고
    • Stabilization versus inhibition of TAFIa by competitive inhibitors in vitro
    • DOI 10.1074/jbc.M205006200
    • Walker, J. B.; Hughes, B.; James, I.; Haddock, P.; Kluft, C.; Bajzar, L. Stabilization versus inhibition of TAFIa by competitive inhibitors in vitro. J. Biol. Chem., 2003, 278, 8913-8921 (Pubitemid 36800367)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.11 , pp. 8913-8921
    • Walker, J.B.1    Hughes, B.2    James, I.3    Haddock, P.4    Kluft, C.5    Bajzar, L.6
  • 52
    • 3142584783 scopus 로고    scopus 로고
    • Carboxypeptidase U (TAFIa) prevents lysis from proceeding into the propagation phase through a threshold-dependent mechanism
    • Leurs, J.; Nerme, V.; Sim, Y.; Hendriks, D. Carboxypeptidase U (TAFIa) prevents lysis from proceeding into the propagation phase through a threshold-dependent mechanism. J. Thromb. Haemost., 2004, 2, 416-423
    • (2004) J. Thromb. Haemost. , vol.2 , pp. 416-423
    • Leurs, J.1    Nerme, V.2    Sim, Y.3    Hendriks, D.4
  • 53
    • 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
    • DOI 10.1074/jbc.M401027200
    • Walker, J. B.; Bajzar, L. The intrinsic threshold of the fibriolytic 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., 2004, 279, 27896-27904 (Pubitemid 38900058)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 27896-27904
    • Walker, J.B.1    Bajzar, L.2
  • 54
    • 0035885942 scopus 로고    scopus 로고
    • A novel, possibly functional, single nucleotide polymorphism in the coding region of the thrombin-activatable fibrinolysis inhibitor (TAFI) gene is also associated with TAFI levels
    • Brouwers, G. J.; Vos, H. L.; Leebeek, F. W.; Bulk, S.; Schneider, M.; Boffa, M.; Koschinsky, M. L.; Van Tilburg, N. H.; Nesheim, M.; Bertina, R. M.; Gomez-Garcia, E. B. A novel, possibly functional, single nucleotide polymorphism in the coding region of the thrombin-activatable fibrinolysis inhibitor (TAFI) gene is also associated with TAFI levels. Blood, 2001, 98, 1992-1993
    • (2001) Blood , vol.98 , pp. 1992-1993
    • Brouwers, G.J.1    Vos, H.L.2    Leebeek, F.W.3    Bulk, S.4    Schneider, M.5    Boffa, M.6    Koschinsky, M.L.7    Van Tilburg, N.H.8    Nesheim, M.9    Bertina, R.M.10    Gomez-Garcia, E.B.11
  • 55
    • 0037059828 scopus 로고    scopus 로고
    • Two naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme
    • DOI 10.1074/jbc.M104444200
    • Schneider, M.; Boffa, M.; Stewart, R. J.; Rahman, N. L.; Koschinsky, M. L.; Nesheim, M. Two naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme. J. Biol. Chem., 2002, 277, 1021-1030 (Pubitemid 34968847)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.2 , pp. 1021-1030
    • Schneider, M.1    Boffa, M.2    Stewart, R.3    Rahman, M.4    Koschinsky, M.5    Nesheim, M.6
  • 56
    • 0035313252 scopus 로고    scopus 로고
    • Identification of polymorphisms in the promoter and the 3′ region of the TAFI gene: Evidence that plasma TAFI antigen levels are strongly genetically controlled
    • DOI 10.1182/blood.V97.7.2053
    • Henry, M.; Aubert, H.; Morange, P. E.; Nanni, I.; Alessi, M. C.; Tiret, L.; Juhan-Vague, I. Identification of polymorphisms in the promoter and the 3′ region of the TAFI gene: evidence that plasma TAFI antigen levels are strongly genetically controlled. Blood, 2001, 97, 2053-2058 (Pubitemid 32239086)
    • (2001) Blood , vol.97 , Issue.7 , pp. 2053-2058
    • Henry, M.1    Aubert, H.2    Morange, P.E.3    Nanni, I.4    Alessi, M.-C.5    Tiret, L.6    Juhan-Vague, I.7
  • 58
    • 0035179379 scopus 로고    scopus 로고
    • Association of a single nucleotide polymorphism in CPB2 encoding the thrombin-activable fibrinolysis inhibitor (TAF1) with blood pressure
    • Koschinsky, M. L.; Boffa, M. B.; Nesheim, M. E.; Zinman, B.; Hanley, A. J.; Harris, S. B.; Cao, H.; Hegele, R. A. Association of a single nucleotide polymorphism in CPB2 encoding the thrombin-activable fibrinolysis inhibitor (TAF1) with blood pressure. Clin. Genet., 2001, 60, 345-349
    • (2001) Clin. Genet. , vol.60 , pp. 345-349
    • Koschinsky, M.L.1    Boffa, M.B.2    Nesheim, M.E.3    Zinman, B.4    Hanley, A.J.5    Harris, S.B.6    Cao, H.7    Hegele, R.A.8
  • 60
    • 4444246103 scopus 로고    scopus 로고
    • A functional single nucleotide polymorphisms in the thrombin-activatable fibrinolysis inhibitor (TAFI) gene associates with outcome of meningococcal disease
    • DOI 10.1111/j.1538-7836.2004.00557.x
    • Kremer Hovinga, J. A.; Franco, R. F.; Zago, M. A.; Ten, C. H.; Westendorp, R. G.; Reitsma, P. H. A functional single nucleotide polymorphism in the thrombin-activatable fibrinolysis inhibitor (TAFI) gene associates with outcome of meningococcal disease. J. Thromb. Haemost., 2004, 2, 54-57 (Pubitemid 40185619)
    • (2004) Journal of Thrombosis and Haemostasis , vol.2 , Issue.1 , pp. 54-57
    • Kremer Hovinga, J.A.1    Franco, R.F.2    Zago, M.A.3    Ten Cate, H.4    Westendorp, R.G.J.5    Reitsma, P.H.6
  • 62
    • 34548062846 scopus 로고    scopus 로고
    • Influence of thrombin-activatable fibrinolysis inhibitor and plasminogen activator inhibitor-1 gene polymorphisms on tissue-type plasminogen activator-induced recanalization in ischemic stroke patients
    • Fernandez-Cadenas, I.; varez-Sabin, J.; Ribo, M.; Rubiera, M.; Mendioroz, M.; Molina, C. A.; Rosell, A.; Montaner, J. Influence of thrombin-activatable fibrinolysis inhibitor and plasminogen activator inhibitor-1 gene polymorphisms on tissue-type plasminogen activator-induced recanalization in ischemic stroke patients. J. Thromb. Haemost., 2007, 5, 1862-1868
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 1862-1868
    • Fernandez-Cadenas, I.1    Varez-Sabin, J.2    Ribo, M.3    Rubiera, M.4    Mendioroz, M.5    Molina, C.A.6    Rosell, A.7    Montaner, J.8
  • 64
    • 0030589619 scopus 로고    scopus 로고
    • The gene for human carboxypeptidase U (CPU) - A proposed novel regulator of plasminogen activation - Maps to 13q14.11
    • DOI 10.1006/geno.1996.0656
    • Vanhoof, G.; Wauters, J.; Schatteman, K.; Hendriks, D.; Goossens, F.; Bossuyt, P.; Scharpé, S. The gene for human carboxypeptidase U (CPU)- a proposed novel regulator of plasminogen activation-maps to 13q14.11. Genomics, 1996, 38, 454-455 (Pubitemid 27030141)
    • (1996) Genomics , vol.38 , Issue.3 , pp. 454-455
    • Vanhoof, G.1    Wauters, J.2    Schatteman, K.3    Hendriks, D.4    Goossens, F.5    Bossuyt, P.6    Scharpe, S.7
  • 65
    • 0026464017 scopus 로고
    • The gene encoding human plasma carboxypeptidase B (CPB2) resides on chromosome 13
    • Tsai, S. P.; Drayna, D. The gene encoding human plasma carboxypeptidase B (CPB2) resides on chromosome 13. Genomics, 1992, 14, 549-550
    • (1992) Genomics , vol.14 , pp. 549-550
    • Tsai, S.P.1    Drayna, D.2
  • 66
    • 0033580640 scopus 로고    scopus 로고
    • Characterization of the gene encoding human TAFI (thrombin-activable fibrinolysis inhibitor; plasma procarboxypeptidase B)
    • Boffa, M.; Reid, S. T.; Joo, E.; Nesheim, M.; Koschinsky, M. L. Characterization of the gene encoding human TAFI (Thrombin-activable fibrinolysis inhibitor; plasma procarboxypeptidas B). Biochem., 1999, 38, 6547-6558 (Pubitemid 129514953)
    • (1999) Biochemistry , vol.38 , Issue.20 , pp. 6547-6558
    • Boffa, M.B.1    Reid, T.S.2    Joo, E.3    Nesheim, M.E.4    Koschinsky, M.L.5
  • 67
    • 34250884059 scopus 로고    scopus 로고
    • Molecular analysis of the human thrombin-activatable fibrinolysis inhibitor gene promoter
    • DOI 10.1111/j.1365-2141.2007.06640.x
    • Garand, M.; Bastajian, N.; Nesheim, M. E.; Boffa, M. B.; Koschinsky, M. L. Molecular analysis of the human thrombin-activatable fibrinolysis inhibitor gene promoter. Br. J. Haematol., 2007, 138, 231-244 (Pubitemid 46976324)
    • (2007) British Journal of Haematology , vol.138 , Issue.2 , pp. 231-244
    • Garand, M.1    Bastajian, N.2    Nesheim, M.E.3    Boffa, M.B.4    Koschinsky, M.L.5
  • 69
    • 0038454527 scopus 로고    scopus 로고
    • Identification of thrombin activatable fibrinolysis inhibitor (TAFI) in human platelets
    • Mosnier, L. O.; Buijtenhuijs, P.; Marx, P. F.; Meijers, J. C. M.; Bouma, B. N. Identification of Thrombin Activatable Fibrinolysis Inhibitor (TAFI) in human platelets. Blood, 2003, 101, 4844-4846 (Pubitemid 36857744)
    • (2003) Blood , vol.101 , Issue.12 , pp. 4844-4846
    • Mosnier, L.O.1    Buijtenhuijs, P.2    Marx, P.F.3    Meijers, J.C.M.4    Bouma, B.N.5
  • 70
    • 0029793068 scopus 로고    scopus 로고
    • The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent
    • Bajzar, L.; Nesheim, M. E.; Tracy, P. B. The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent. Blood, 1996, 88, 2093-2100 (Pubitemid 26307911)
    • (1996) Blood , vol.88 , Issue.6 , pp. 2093-2100
    • Bajzar, L.1    Nesheim, M.E.2    Tracy, P.B.3
  • 71
    • 0031775510 scopus 로고    scopus 로고
    • Plasma TAFI levels determine the clot lysis time in healthy individuals in the presence of an intact intrinsic pathway of coagulation
    • Mosnier, L. O.; Von dem Borne, P. A.; Meijers, J. C.; Bouma, B. N. Plasma TAFI levels determine the clot lysis time in healthy individuals in the presence of an intact intrinsic pathway of coagulation. Thromb. Haemost., 1998, 80, 829-835
    • (1998) Thromb. Haemost. , vol.80 , pp. 829-835
    • Mosnier, L.O.1    Von Dem Borne, P.A.2    Meijers, J.C.3    Bouma, B.N.4
  • 72
    • 0034192129 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis
    • Van Tilburg, N. H.; Rosendaal, F. R.; Bertina, R. M. Thrombin-activatable fibrinolysis inhibitor and the risk for deep vein thrombosis. Blood, 2000, 95, 2855-2859 (Pubitemid 30235895)
    • (2000) Blood , vol.95 , Issue.9 , pp. 2855-2859
    • Van Tilburg, N.H.1    Rosendaal, F.R.2    Bertina, R.M.3
  • 74
    • 23644433169 scopus 로고    scopus 로고
    • Quantification of thrombin activatable fibrinolysis inhibitor (TAFI) gene polymorphism effects on plasma levels of TAFI measured with assays insensitive to isoform-dependent artefact
    • Frere, C.; Morange, P. E.; Saut, N.; Tregouet, D. A.; Grosley, M.; Beltran, J.; Juhan-Vague, I.; Alessi, M. C. Quantification of thrombin activatable fibrinolysis inhibitor (TAFI) gene polymorphism effects on plasma levels of TAFI measured with assays insensitive to isoform-dependent artefact. Thromb. Haemost., 2005, 94, 373-379
    • (2005) Thromb. Haemost. , vol.94 , pp. 373-379
    • Frere, C.1    Morange, P.E.2    Saut, N.3    Tregouet, D.A.4    Grosley, M.5    Beltran, J.6    Juhan-Vague, I.7    Alessi, M.C.8
  • 75
    • 0038660605 scopus 로고    scopus 로고
    • Acute phase mediators modulate Thrombin-activable Fibrinolysis Inhibitor (TAFI) gene expression in HepG2 cells
    • Boffa, M. B.; Hamill, J. D.; Maret, D.; Brown, D.; Scott, M. L.; Nesheim, M. E.; Koschinsky, M. L. Acute phase mediators modulate Thrombin-activable Fibrinolysis Inhibitor (TAFI) gene expression in HepG2 cells. J. Biol. Chem., 2003, 278, 9250-9257
    • (2003) J. Biol. Chem. , vol.278 , pp. 9250-9257
    • Boffa, M.B.1    Hamill, J.D.2    Maret, D.3    Brown, D.4    Scott, M.L.5    Nesheim, M.E.6    Koschinsky, M.L.7
  • 77
    • 34147172386 scopus 로고    scopus 로고
    • Influence of the Thr325Ile polymorphism on procarboxypeptidase U (thrombin-activable fibrinolysis inhibitor) activity-based assays
    • Willemse, J. L.; Matus, V.; Heylen, E.; Mezzano, D.; Hendriks, D. F. Influence of the Thr325Ile polymorphism on procarboxypeptidase U (thrombin-activable fibrinolysis inhibitor) activity-based assays. J. Thromb. Haemost., 2007, 5, 872-875
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 872-875
    • Willemse, J.L.1    Matus, V.2    Heylen, E.3    Mezzano, D.4    Hendriks, D.F.5
  • 78
    • 15544373731 scopus 로고    scopus 로고
    • Development of a fast kinetic method for the determination of carboxypeptidase U (TAFIa) using C-terminal arginine containing peptides as substrate
    • DOI 10.1016/j.ab.2005.01.039
    • Willemse, J.; Leurs, J.; Verkerk, R.; Hendriks, D. Development of a fast kinetic method for the determination of carboxypeptidase U (TAFIa) using C-terminal arginine containing peptides as substrate. Anal. Biochem., 2005, 340, 106-112 (Pubitemid 40404106)
    • (2005) Analytical Biochemistry , vol.340 , Issue.1 , pp. 106-112
    • Willemse, J.1    Leurs, J.2    Verkerk, R.3    Hendriks, D.4
  • 79
    • 28444441566 scopus 로고    scopus 로고
    • Fast kinetic assay for the determination of procarboxypeptidase U (TAFI) in human plasma
    • Willemse, J. L.; Leurs, J. R.; Hendriks, D. F. Fast kinetic assay for the determination of procarboxypeptidase U (TAFI) in human plasma. J. Thromb. Haemost., 2005, 3, 2353-2355
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 2353-2355
    • Willemse, J.L.1    Leurs, J.R.2    Hendriks, D.F.3
  • 80
    • 36048964941 scopus 로고    scopus 로고
    • An assay for measuring functional activated thrombin-activatable fibrinolysis inhibitor in plasma
    • Kim, P. Y.; Foley, J.; Hsu, G.; Kim, P. Y.; Nesheim, M. E. An assay for measuring functional activated thrombin-activatable fibrinolysis inhibitor in plasma. Anal. Biochem., 2008, 372, 32-40.
    • (2008) Anal. Biochem. , vol.372 , pp. 32-40
    • Kim, P.Y.1    Foley, J.2    Hsu, G.3    Kim, P.Y.4    Nesheim, M.E.5
  • 82
    • 33750079554 scopus 로고    scopus 로고
    • Characterization of rat thrombin-activatable fibrinolysis inhibitor (TAFI) - A comparative study assessing the biological equivalence of rat, murine and human TAFI
    • DOI 10.1111/j.1538-7836.2006.02224.x
    • Hillmayer, K.; Macovei, A.; Pauwels, D.; Compernolle, G.; Declerck, P. J.; Gils, A. Characterization of rat thrombin-activatable fibrinolysis inhibitor (TAFI) - a comparative study assessing the biological equivalence of rat, murine and human TAFI. J. Thromb. Haemost., 2006, 4, 2470-2477 (Pubitemid 44575443)
    • (2006) Journal of Thrombosis and Haemostasis , vol.4 , Issue.11 , pp. 2470-2477
    • Hillmayer, K.1    Macovei, A.2    Pauwels, D.3    Compernolle, G.4    Declerck, P.J.5    Gils, A.6
  • 83
    • 37549034248 scopus 로고    scopus 로고
    • Development of sandwich-type ELISAs for the quantification of rat and murine thrombin activatable fibrinolysis inhibitor in plasma
    • Hillmayer, K.; Brouwers, E.; Leon-Tamariz, F.; Meijers, J. C.; Marx, P. F.; Declerck, P. J.; Gils, A. Development of sandwich-type ELISAs for the quantification of rat and murine thrombin activatable fibrinolysis inhibitor in plasma. J. Thromb. Haemost., 2008, 6, 132-138
    • (2008) J. Thromb. Haemost. , vol.6 , pp. 132-138
    • Hillmayer, K.1    Brouwers, E.2    Leon-Tamariz, F.3    Meijers, J.C.4    Marx, P.F.5    Declerck, P.J.6    Gils, A.7
  • 85
    • 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)
    • Guimaraes, A. H.; Barrett-Bergshoeff, M. M.; Criscuoli, M.; Evangelista, S.; Rijken, D. C. 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., 2006, 96, 325-330
    • (2006) Thromb. Haemost. , vol.96 , pp. 325-330
    • Guimaraes, A.H.1    Barrett-Bergshoeff, M.M.2    Criscuoli, M.3    Evangelista, S.4    Rijken, D.C.5
  • 86
    • 24944488122 scopus 로고    scopus 로고
    • A new functional assay of thrombin activatable fibrinolysis inhibitor
    • DOI 10.1111/j.1538-7836.2005.01388.x
    • Guimaraes, A. H.; Bertina, R. M.; Rijken, D. C. A new functional assay of thrombin activatable fibrinolysis inhibitor. J. Thromb. Haemost., 2005, 3, 1284-1292 (Pubitemid 41725254)
    • (2005) Journal of Thrombosis and Haemostasis , vol.3 , Issue.6 , pp. 1284-1292
    • Guimaraes, A.H.C.1    Bertina, R.M.2    Rijken, D.C.3
  • 88
    • 35748983545 scopus 로고    scopus 로고
    • Comparative substrate specificity study of carboxypeptidase U (TAFIa) and carboxypeptidase N: Development of highly selective CPU substrates as useful tools for assay development
    • Willemse, J. L.; Polla, M.; Olsson, T.; Hendriks, D. F. Comparative substrate specificity study of carboxypeptidase U (TAFIa) and carboxypeptidase N: development of highly selective CPU substrates as useful tools for assay development. Clin. Chim. Acta, 2008, 387, 158-160
    • (2008) Clin. Chim. Acta , vol.387 , pp. 158-160
    • Willemse, J.L.1    Polla, M.2    Olsson, T.3    Hendriks, D.F.4
  • 90
    • 0032700758 scopus 로고    scopus 로고
    • Activation of plasma procarboxypeptidase U in different mammalian species points to a conserved pathway of inhibition of fibrinolysis
    • Schatteman, K. A.; Goossens, F. J.; Scharpe, S. S.; Hendriks, D. F. Activation of plasma procarboxypeptidase U in different mammalian species points to a conserved pathway of inhibition of fibrinolysis. Thromb. Haemost., 1999, 82, 1718-1721
    • (1999) Thromb. Haemost. , vol.82 , pp. 1718-1721
    • Schatteman, K.A.1    Goossens, F.J.2    Scharpe, S.S.3    Hendriks, D.F.4
  • 91
    • 12244252240 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor (TAFI) levels in patients with coronary artery disease investigated by angiography
    • Schroeder, V.; Chatterjee, T.; Mehta, H.; Windecker, S.; Pham, T.; Devantay, N.; Meier, B.; Kohler, H. P. Thrombin activatable fibrinolysis inhibitor (TAFI) levels in patients with coronary artery disease investigated by angiography. Thromb. Haemost., 2002, 88, 1020-1025
    • (2002) Thromb. Haemost. , vol.88 , pp. 1020-1025
    • Schroeder, V.1    Chatterjee, T.2    Mehta, H.3    Windecker, S.4    Pham, T.5    Devantay, N.6    Meier, B.7    Kohler, H.P.8
  • 92
    • 33747087775 scopus 로고    scopus 로고
    • TAFI activity in coronary artery disease: A contribution to the current discussion on TAFI assays
    • Schroeder, V.; Wilmer, M.; Buehler, B.; Kohler, H. P. TAFI activity in coronary artery disease: a contribution to the current discussion on TAFI assays. Thromb. Haemost., 2006, 96, 236-237
    • (2006) Thromb. Haemost. , vol.96 , pp. 236-237
    • Schroeder, V.1    Wilmer, M.2    Buehler, B.3    Kohler, H.P.4
  • 95
    • 0036636770 scopus 로고    scopus 로고
    • Association between plasma thrombin-activatable fibrinolysis inhibitor levels and acti vated protein C in normotensive type 2 diabetic patients
    • Yano, Y.; Gabazza, E. C.; Hori, Y.; Kitagawa, N.; Katsuki, A.; raki-Sasaki, R.; Sumida, Y.; Adachi, Y. Association between plasma thrombin-activatable fibrinolysis inhibitor levels and acti vated protein C in normotensive type 2 diabetic patients. Diabetes Care, 2002, 25, 1245-1246
    • (2002) Diabetes Care , vol.25 , pp. 1245-1246
    • Yano, Y.1    Gabazza, E.C.2    Hori, Y.3    Kitagawa, N.4    Katsuki, A.5    Raki-Sasaki, R.6    Sumida, Y.7    Adachi, Y.8
  • 96
    • 0036172375 scopus 로고    scopus 로고
    • Insulin resistance is associated with increased circulating level of thrombin-activatable fibrinolysis inhibitor in type 2 diabetic patients
    • DOI 10.1210/jc.87.2.660
    • Hori, Y.; Gabazza, E. C.; Yano, Y.; Katsuki, A.; Suzuki, K.; Adachi, Y.; Sumida, Y. Insulin resistance is associated with increased circulating level of thrombin-activatable fibrinolysis inhibitor in type 2 diabetic patients. J. Clin. Endocrinol. Metab, 2002, 87, 660-665 (Pubitemid 34158234)
    • (2002) Journal of Clinical Endocrinology and Metabolism , vol.87 , Issue.2 , pp. 660-665
    • Hori, Y.1    Gabazza, E.C.2    Yano, Y.3    Katsuki, A.4    Suzuki, K.5    Adachi, Y.6    Sumida, Y.7
  • 97
    • 39849095427 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor and other hemostatic parameters in patients with essential arterial hypertension
    • Malyszko, J.; Tymcio, J. Thrombin activatable fibrinolysis inhibitor and other hemostatic parameters in patients with essential arterial hypertension. Pol. Arch. Med. Wewn., 2008, 118, 36-41. (Pubitemid 351316526)
    • (2008) Polskie Archiwum Medycyny Wewnetrznej , vol.118 , Issue.1-2 , pp. 36-41
    • Malyszko, J.1    Tymcio, J.2
  • 98
    • 33644507447 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor in hypertensive kidney transplant recipients
    • DOI 10.1016/j.transproceed.2005.11.072, PII S0041134505014326
    • Malyszko, J.; Malyszko, J. S.; Hryszko, T.; Mysliwiec, M. Thrombin activatable fibrinolysis inhibitor in hypertensive kidney transplant recipients. Transplant. Proc., 2006, 38, 105-107 (Pubitemid 43303610)
    • (2006) Transplantation Proceedings , vol.38 , Issue.1 , pp. 105-107
    • Malyszko, J.1    Malyszko, J.S.2    Hryszko, T.3    Mysliwiec, M.4
  • 99
    • 33748741980 scopus 로고    scopus 로고
    • Decrements in the thrombin activatable fibrinolysis inhibitor (TAFI) levels in association with orlistat treatment in obesity
    • DOI 10.1177/1076029606291403
    • Guven, G. S.; Kilicaslan, A.; Oz, S. G.; Haznedaroglu, I. C.; Kirazli, S.; Aslan, D.; Sozen, T. Decrements in the thrombin activatable fibrinolysis inhibitor (TAFI) levels in association with orlistat treatment in obesity. Clin. Appl. Thromb. Hemost., 2006, 12, 364-368 (Pubitemid 44400850)
    • (2006) Clinical and Applied Thrombosis/Hemostasis , vol.12 , Issue.3 , pp. 364-368
    • Guven, G.S.1    Kilicaslan, A.2    Oz, S.G.3    Haznedaroglu, I.C.4    Kirazli, S.5    Aslan, D.6    Sozen, T.7
  • 100
    • 34247891640 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor and its relationship to fibrinolysis and inflammation during the acute and convalescent phase of ischemic stroke
    • DOI 10.1097/MBC.0b013e3281139c34, PII 0000172120070600000012
    • Rooth, E.; Wallen, H.; Antovic, A.; von, A. M.; Kaponides, G.; Wahlgren, N.; Blomback, M.; Antovic, J. Thrombin activatable fibrinolysis inhibitor and its relationship to fibrinolysis and inflammation during the acute and convalescent phase of ischemic stroke. Blood Coagul. Fibrinolysis, 2007, 18, 365-370 (Pubitemid 46699415)
    • (2007) Blood Coagulation and Fibrinolysis , vol.18 , Issue.4 , pp. 365-370
    • Rooth, E.1    Wallen, H.2    Antovic, A.3    Von Arbin, M.4    Kaponides, G.5    Wahlgren, N.6    Blomback, M.7    Antovic, J.8
  • 101
    • 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
    • DOI 10.1161/01.ATV.0000259354.93789.a6
    • Ladenvall, C.; Gils, A.; Jood, K.; Blomstrand, C.; Declerck, P. J.; Jern, C. Thrombin activatable fibrinolysis inhibitor activation peptide shows association with all major subtypes of ischemic stroke and with TAFI gene variation. Arterioscler. Thromb. Vasc. Biol., 2007, 27, 955-962 (Pubitemid 46606731)
    • (2007) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.27 , Issue.4 , pp. 955-962
    • Ladenvall, C.1    Gils, A.2    Jood, K.3    Blomstrand, C.4    Declerck, P.J.5    Jern, C.6
  • 102
    • 28444480174 scopus 로고    scopus 로고
    • High functional levels of thrombin-activatable fibrinolysis inhibitor are associated with an increased risk of first ischemic stroke
    • Leebeek, F. W.; Goor, M. P.; Guimaraes, A. H.; Brouwers, G. J.; Maat, M. P.; Dippel, D. W.; Rijken, D. C. High functional levels of thrombin-activatable fibrinolysis inhibitor are associated with an increased risk of first ischemic stroke. J. Thromb. Haemost., 2005, 3, 2211-2218
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 2211-2218
    • Leebeek, F.W.1    Goor, M.P.2    Guimaraes, A.H.3    Brouwers, G.J.4    Maat, M.P.5    Dippel, D.W.6    Rijken, D.C.7
  • 103
    • 14044261178 scopus 로고    scopus 로고
    • Plasma thrombin-activatable fibrinolytic inhibitor (TAFI) among healthy subjects and patients with vascular diseases: A validation study
    • DOI 10.1159/000083833
    • Monasterio, J.; Bermudez, P.; Quiroga, D.; Francisco, E.; Meneses, B.; Montaner, J. Plasma thrombin-activatable fibrinolytic inhibitor (TAFI) among healthy subjects and patients with vascular diseases: a validation study. Pathophysiol. Haemost. Thromb., 2003, 33, 382-386 (Pubitemid 40278712)
    • (2003) Pathophysiology of Haemostasis and Thrombosis , vol.33 , Issue.5-6 , pp. 382-386
    • Monasterio, J.1    Bermudez, P.2    Quiroga, D.3    Francisco, E.4    Meneses, B.5    Montaner, J.6
  • 104
    • 4344618873 scopus 로고    scopus 로고
    • Admission fibrinolytic profile is associated with symptomatic hemorrhagic transformation in stroke patients treated with tissue plasminogen activator
    • Ribo, M.; Montaner, J.; Molina, C. A.; Arenillas, J. F.; Santamarina, E.; Quintana, M.; varez-Sabin, J. Admission fibrinolytic profile is associated with symptomatic hemorrhagic transformation in stroke patients treated with tissue plasminogen activator. Stroke, 2004, 35, 2123-2127
    • (2004) Stroke , vol.35 , pp. 2123-2127
    • Ribo, M.1    Montaner, J.2    Molina, C.A.3    Arenillas, J.F.4    Santamarina, E.5    Quintana, M.6    Varez-Sabin, J.7
  • 105
    • 17644434948 scopus 로고    scopus 로고
    • Risk of ischemic stroke associated with functional thrombin-activatable fibrinolysis inhibitor plasma levels
    • DOI 10.1161/01.STR.0000088642.07691.15
    • Santamaria, A.; Oliver, A.; Borrell, M.; Mateo, J.; Belvis, R.; Marti-Fabregas, J.; Ortin, R.; Tirado, I.; Souto, J. C.; Fontcuberta, J. Risk of ischemic stroke associated with functional thrombin-activatable fibrinolysis inhibitor plasma levels. Stroke, 2003, 34, 2387-2391 (Pubitemid 37229070)
    • (2003) Stroke , vol.34 , Issue.10 , pp. 2387-2391
    • Santamaria, A.1    Oliver, A.2    Borrell, M.3    Mateo, J.4    Belvis, R.5    Marti-Fabregas, J.6    Ortin, R.7    Tirado, I.8    Souto, J.C.9    Fontcuberta, J.10
  • 106
    • 0037383184 scopus 로고    scopus 로고
    • Thrombin-activable fibrinolysis inhibitor levels in the acute phase of ischemic stroke
    • DOI 10.1161/01.STR.0000063139.06585.45
    • Montaner, J.; Ribo, M.; Monasterio, J.; Molina, C. A.; Alvarez-Sabin, J. Thrombin-Activable Fibrinolysis Inhibitor levels in the acute phase of ischemic stroke. Stroke, 2003, 1038-1040 (Pubitemid 36402986)
    • (2003) Stroke , vol.34 , Issue.4 , pp. 1038-1040
    • Montaner, J.1    Ribo, M.2    Monasterio, J.3    Molina, C.A.4    Alvarez-Sabin, J.5
  • 109
    • 0035479232 scopus 로고    scopus 로고
    • Activity and antigen levels of thrombin-activatable fibrinolysis inhibitor in plasma of patients with disseminated intravascular coagulation
    • DOI 10.1016/S0049-3848(01)00331-0, PII S0049384801003310
    • Watanabe, R.; Wada, H.; Watanabe, Y.; Sakakura, M.; Nakasaki, T.; Mori, Y.; Nishikawa, M.; Gabazza, E. C.; Nobori, T.; Shiku, H. Activity and antigen levels of thrombin-activatable fibrinolysis inhibitor in plasma of patients with disseminated intravascular coagulation. Thromb. Res., 2001, 104, 1-6. (Pubitemid 32918249)
    • (2001) Thrombosis Research , vol.104 , Issue.1 , pp. 1-6
    • Watanabe, R.1    Wada, H.2    Watanabe, Y.3    Sakakura, M.4    Nakasaki, T.5    Mori, Y.6    Nishikawa, M.7    Gabazza, E.C.8    Nobori, T.9    Shiku, H.10
  • 112
    • 33749543001 scopus 로고    scopus 로고
    • Postprandial thrombin activatable fibrinolysis inhibitor and markers of endothelial dysfunction in type 2 diabetic patients
    • DOI 10.1016/j.metabol.2005.11.010, PII S0026049505004439
    • Rigla, M.; Wagner, A. M.; Borrell, M.; Mateo, J.; Foncuberta, J.; de, L. A.; Ordonez-Llanos, J.; Perez, A. Postprandial thrombin activatable fibrinolysis inhibitor and markers of endothelial dysfunction in type 2 diabetic patients. Metabolism, 2006, 55, 1437-1442 (Pubitemid 44537340)
    • (2006) Metabolism: Clinical and Experimental , vol.55 , Issue.11 , pp. 1437-1442
    • Rigla, M.1    Wagner, A.M.2    Borrell, M.3    Mateo, J.4    Foncuberta, J.5    De Leiva, A.6    Ordonez-Llanos, J.7    Perez, A.8
  • 113
    • 3042619676 scopus 로고    scopus 로고
    • Admission fibrinolytic profile predicts clot lysis resistance in stroke patients treated with tissue plasminogen activator
    • Ribo, M.; Montaner, J.; Molina, C. A.; Arenillas, J. F.; Santamarina, E.; varez-Sabin, J. Admission fibrinolytic profile predicts clot lysis resistance in stroke patients treated with tissue plasminogen activator. Thromb. Haemost., 2004, 91, 1146-1151 (Pubitemid 38821271)
    • (2004) Thrombosis and Haemostasis , vol.91 , Issue.6 , pp. 1146-1151
    • Ribo, M.1    Montaner, J.2    Molina, C.A.3    Arenillas, J.F.4    Santamarina, E.5    Alvarez-Sabin, J.6
  • 115
    • 4644336103 scopus 로고    scopus 로고
    • Absence of procarboxypeptidase R induces complement-mediated lethal inflammation in lipopolysaccharide-primed mice
    • Asai, S.; Sato, T.; Tada, T.; Miyamoto, T.; Kimbara, N.; Motoyama, N.; Okada, H.; Okada, N. Absence of procarboxypeptidase R induces complement-mediated lethal inflammation in lipopolysaccharide-primed mice. J. Immunol., 2004, 173, 4669-4674 (Pubitemid 39280701)
    • (2004) Journal of Immunology , vol.173 , Issue.7 , pp. 4669-4674
    • Asai, S.1    Sato, T.2    Tada, T.3    Miyamoto, T.4    Kimbara, N.5    Motoyama, N.6    Okada, H.7    Okada, N.8
  • 116
    • 33846951195 scopus 로고    scopus 로고
    • Deficiency in thrombin-activatable fibrinolysis inhibitor (TAFI) protected mice from ferric chloride-induced vena cava thrombosis
    • Wang, X.; Smith, P. L.; Hsu, M. Y.; Tamasi, J. A.; Bird, E.; Schumacher, W. A. Deficiency in thrombin-activatable fibrinolysis inhibitor (TAFI) protected mice from ferric chloride-induced vena cava thrombosis. J. Thromb. Thrombolysis., 2007, 23, 41-49
    • (2007) J. Thromb. Thrombolysis. , vol.23 , pp. 41-49
    • Wang, X.1    Smith, P.L.2    Hsu, M.Y.3    Tamasi, J.A.4    Bird, E.5    Schumacher, W.A.6
  • 117
    • 24044500304 scopus 로고    scopus 로고
    • Demonstration of enhanced endogenous fibrinolysis in thrombin activatable fibrinolysis inhibitor-deficient mice
    • Mao, S. S.; Holahan, M. A.; Bailey, C.; Wu, G.; Colussi, D.; Carroll, S. S.; Cook, J. J. Demonstration of enhanced endogenous fibrinolysis in thrombin activatable fibrinolysis inhibitor-deficient mice. Blood Coagul. Fibrinolysis, 2005, 16, 407-415
    • (2005) Blood Coagul. Fibrinolysis , vol.16 , pp. 407-415
    • Mao, S.S.1    Holahan, M.A.2    Bailey, C.3    Wu, G.4    Colussi, D.5    Carroll, S.S.6    Cook, J.J.7
  • 118
    • 0036843274 scopus 로고    scopus 로고
    • In vivo regulation of plasminogen function by plasma carboxypeptidase B
    • Swaisgood, C. M.; Schmitt, D.; Eaton, D. L.; Plow, E. F. In vivo regulation of plasminogen function by plasma carboxypeptidase B. J. Clin. Invest., 2002, 110, 1275-1282
    • (2002) J. Clin. Invest. , vol.110 , pp. 1275-1282
    • Swaisgood, C.M.1    Schmitt, D.2    Eaton, D.L.3    Plow, E.F.4
  • 120
    • 34548307247 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor binds to Streptococcus pyogenes by interacting with collagen-like proteins a and B
    • DOI 10.1074/jbc.M610015200
    • Pahlman, L. I.; Marx, P. F.; Morgelin, M.; Lukomski, S.; Meijers, J. C.; Herwald, H. Thrombin-activatable fibrinolysis inhibitor binds to Streptococcus pyogenes by interacting with collagen-like proteins A and B. J. Biol. Chem., 2007, 282, 24873-24881 (Pubitemid 47347522)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.34 , pp. 24873-24881
    • Pahlman, L.I.1    Marx, P.F.2    Morgelin, M.3    Lukomski, S.4    Meijers, J.C.M.5    Herwald, H.6
  • 121
    • 62249101697 scopus 로고    scopus 로고
    • Activation of TAFI on the Surface of Streptococcus pyogenes Evokes Inflammatory Reactions by Modulating the Kallikrein/Kinin System
    • Bengtson, S.; Sadén, C.; Mörgelin, M.; Marx, P. F.; Olin, A.; Leeb- Lundberg, L.; Meijers, J. C. M.; Herwald, H. Activation of TAFI on the Surface of Streptococcus pyogenes Evokes Inflammatory Reactions by Modulating the Kallikrein/Kinin System. J. Innate Immun., 2009, 1, 18-28.
    • (2009) J. Innate Immun. , vol.1 , pp. 18-28
    • Bengtson, S.1    Sadén, C.2    Mörgelin, M.3    Marx, P.F.4    Olin, A.5    Leeb-Lundberg, L.6    Meijers, J.C.M.7    Herwald, H.8
  • 122
    • 35148845916 scopus 로고    scopus 로고
    • TAFI and pancreatic carboxypeptidase B modulate in vitro capillary tube formation by human microvascular endothelial cells
    • Guimaraes, A. H.; Laurens, N.; Weijers, E. M.; Koolwijk, P.; van, H., V; Rijken, D. C. TAFI and pancreatic carboxypeptidase B modulate in vitro capillary tube formation by human microvascular endothelial cells. Arterioscler. Thromb. Vasc. Biol., 2007, 27, 2157-2162
    • (2007) Arterioscler. Thromb. Vasc. Biol. , vol.27 , pp. 2157-2162
    • Guimaraes, A.H.1    Laurens, N.2    Weijers, E.M.3    Koolwijk, P.4    Van, H.V.5    Rijken, D.C.6


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