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Volumn 10, Issue 1, 2009, Pages

Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; THROMBIN; THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR; TRYPSIN; ISOENZYME; PEPTIDE FRAGMENT; POLYSACCHARIDE;

EID: 66149139135     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-10-13     Document Type: Article
Times cited : (7)

References (58)
  • 1
    • 0024558753 scopus 로고
    • A labile enzyme in fresh human serum interferes with the assay of carboxypeptidase N
    • 2910562
    • A labile enzyme in fresh human serum interferes with the assay of carboxypeptidase N. D Hendriks S Scharpe M van Sande MP Lommaert, Clin Chem 1989 35 1 177 2910562
    • (1989) Clin Chem , vol.35 , Issue.1 , pp. 177
    • Hendriks, D.1    Scharpe, S.2    Van Sande, M.3    Lommaert, M.P.4
  • 2
    • 84945736607 scopus 로고
    • Characterisation of a carboxypeptidase in human serum distinct from carboxypeptidase N
    • 2760564
    • Characterisation of a carboxypeptidase in human serum distinct from carboxypeptidase N. D Hendriks S Scharpe M van Sande MP Lommaert, J Clin Chem Clin Biochem 1989 27 5 277 285 2760564
    • (1989) J Clin Chem Clin Biochem , vol.27 , Issue.5 , pp. 277-285
    • Hendriks, D.1    Scharpe, S.2    Van Sande, M.3    Lommaert, M.P.4
  • 3
    • 0025255189 scopus 로고
    • Purification and characterization of a new arginine carboxypeptidase in human serum
    • 2328266
    • Purification and characterization of a new arginine carboxypeptidase in human serum. D Hendriks W Wang S Scharpe MP Lommaert M van Sande, Biochim Biophys Acta 1990 1034 1 86 92 2328266
    • (1990) Biochim Biophys Acta , vol.1034 , Issue.1 , pp. 86-92
    • Hendriks, D.1    Wang, W.2    Scharpe, S.3    Lommaert, M.P.4    Van Sande, M.5
  • 4
    • 0025748556 scopus 로고
    • Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma
    • 1939207
    • Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. DL Eaton BE Malloy SP Tsai W Henzel D Drayna, J Biol Chem 1991 266 32 21833 21838 1939207
    • (1991) J Biol Chem , 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
  • 5
    • 0028815556 scopus 로고
    • Plasma carboxypeptidases as regulators of the plasminogen system
    • 7593646 10.1172/JCI118315
    • Plasma carboxypeptidases as regulators of the plasminogen system. A Redlitz AK Tan DL Eaton EF Plow, J Clin Invest 1995 96 5 2534 2538 7593646 10.1172/JCI118315
    • (1995) J Clin Invest , vol.96 , Issue.5 , pp. 2534-2538
    • Redlitz, A.1    Tan, A.K.2    Eaton, D.L.3    Plow, E.F.4
  • 6
    • 0028222563 scopus 로고
    • Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen
    • 8195249
    • Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen. W Wang DF Hendriks SS Scharpe, J Biol Chem 1994 269 22 15937 15944 8195249
    • (1994) J Biol Chem , vol.269 , Issue.22 , pp. 15937-15944
    • Wang, W.1    Hendriks, D.F.2    Scharpe, S.S.3
  • 7
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor
    • 10.1074/jbc.270.24.14477 7782309
    • Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor. L Bajzar R Manuel ME Nesheim, J Biol Chem 1995 270 24 14477 14484 10.1074/jbc.270.24.14477 7782309
    • (1995) J Biol Chem , vol.270 , Issue.24 , pp. 14477-14484
    • Bajzar, L.1    Manuel, R.2    Nesheim, M.E.3
  • 8
    • 0030920922 scopus 로고    scopus 로고
    • On the mechanism of the antifibrinolytic activity of plasma carboxypeptidase B
    • 10.1074/jbc.272.22.14477 9162090
    • On the mechanism of the antifibrinolytic activity of plasma carboxypeptidase B. DV Sakharov EF Plow DC Rijken, J Biol Chem 1997 272 22 14477 14482 10.1074/jbc.272.22.14477 9162090
    • (1997) J Biol Chem , vol.272 , Issue.22 , pp. 14477-14482
    • Sakharov, D.V.1    Plow, E.F.2    Rijken, D.C.3
  • 9
    • 0035173479 scopus 로고    scopus 로고
    • Regulation of fibrinolysis in plasma by TAFI and protein C is dependent on the concentration of thrombomodulin
    • 11204587
    • Regulation of fibrinolysis in plasma by TAFI and protein C is dependent on the concentration of thrombomodulin. LO Mosnier JC Meijers BN Bouma, Thromb Haemost 2001 85 1 5 11 11204587
    • (2001) Thromb Haemost , vol.85 , Issue.1 , pp. 5-11
    • Mosnier, L.O.1    Meijers, J.C.2    Bouma, B.N.3
  • 10
    • 0141498145 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor (TAFI, plasma procarboxypeptidase B, procarboxypeptidase R, procarboxypeptidase U)
    • 10.1046/j.1538-7836.2003.00329.x 12871292
    • Thrombin-activatable fibrinolysis inhibitor (TAFI, plasma procarboxypeptidase B, procarboxypeptidase R, procarboxypeptidase U). BN Bouma JC Meijers, J Thromb Haemost 2003 1 7 1566 1574 10.1046/j.1538-7836.2003.00329.x 12871292
    • (2003) J Thromb Haemost , vol.1 , Issue.7 , pp. 1566-1574
    • Bouma, B.N.1    Meijers, J.C.2
  • 11
    • 34047264612 scopus 로고    scopus 로고
    • Thrombin-activable fibrinolysis inhibitor (TAFI) zymogen is an active carboxypeptidase
    • 10.1074/jbc.M606559200 17138567
    • Thrombin-activable fibrinolysis inhibitor (TAFI) zymogen is an active carboxypeptidase. Z Valnickova IB Thogersen J Potempa JJ Enghild, J Biol Chem 2007 282 5 3066 3076 10.1074/jbc.M606559200 17138567
    • (2007) J Biol Chem , vol.282 , Issue.5 , pp. 3066-3076
    • Valnickova, Z.1    Thogersen, I.B.2    Potempa, J.3    Enghild, J.J.4
  • 12
    • 33747165030 scopus 로고    scopus 로고
    • The intrinsic enzymatic activity of plasma procarboxypeptidase U (TAFI) can interfere with plasma carboxypeptidase N assays
    • 10.1016/j.ab.2006.05.020 16797476
    • The intrinsic enzymatic activity of plasma procarboxypeptidase U (TAFI) can interfere with plasma carboxypeptidase N assays. JL Willemse M Polla DF Hendriks, Anal Biochem 2006 356 1 157 159 10.1016/j.ab.2006.05.020 16797476
    • (2006) Anal Biochem , vol.356 , Issue.1 , pp. 157-159
    • Willemse, J.L.1    Polla, M.2    Hendriks, D.F.3
  • 13
    • 0032538447 scopus 로고    scopus 로고
    • Human procarboxypeptidase U, or thrombin-activable fibrinolysis inhibitor, is a substrate for transglutaminases. Evidence for transglutaminase-catalyzed cross-linking to fibrin
    • 10.1074/jbc.273.42.27220 9765243
    • Human procarboxypeptidase U, or thrombin-activable fibrinolysis inhibitor, is a substrate for transglutaminases. Evidence for transglutaminase-catalyzed cross-linking to fibrin. Z Valnickova JJ Enghild, J Biol Chem 1998 273 42 27220 27224 10.1074/jbc.273.42.27220 9765243
    • (1998) J Biol Chem , vol.273 , Issue.42 , pp. 27220-27224
    • Valnickova, Z.1    Enghild, J.J.2
  • 14
    • 0029895009 scopus 로고    scopus 로고
    • TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex
    • 10.1074/jbc.271.28.16603 8663147
    • TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. L Bajzar J Morser M Nesheim, J Biol Chem 1996 271 28 16603 16608 10.1074/jbc.271.28.16603 8663147
    • (1996) J Biol Chem , vol.271 , Issue.28 , pp. 16603-16608
    • Bajzar, L.1    Morser, J.2    Nesheim, M.3
  • 15
    • 0029023651 scopus 로고
    • Activation and characterization of procarboxypeptidase B from human plasma
    • 10.1021/bi00017a012 7727441
    • Activation and characterization of procarboxypeptidase B from human plasma. AK Tan DL Eaton, Biochemistry 1995 34 17 5811 5816 10.1021/bi00017a012 7727441
    • (1995) Biochemistry , vol.34 , Issue.17 , pp. 5811-5816
    • Tan, A.K.1    Eaton, D.L.2
  • 16
    • 0033521034 scopus 로고    scopus 로고
    • Characterization of plasmin-mediated activation of plasma procarboxypeptidase B. Modulation by glycosaminoglycans
    • 10.1074/jbc.274.49.35046 10574983
    • Characterization of plasmin-mediated activation of plasma procarboxypeptidase B. Modulation by glycosaminoglycans. SS Mao CM Cooper T Wood JA Shafer SJ Gardell, J Biol Chem 1999 274 49 35046 35052 10.1074/jbc.274.49. 35046 10574983
    • (1999) J Biol Chem , vol.274 , Issue.49 , pp. 35046-35052
    • Mao, S.S.1    Cooper, C.M.2    Wood, T.3    Shafer, J.A.4    Gardell, S.J.5
  • 17
    • 0037188376 scopus 로고    scopus 로고
    • Plasmin-mediated activation and inactivation of thrombin-activatable fibrinolysis inhibitor
    • 10.1021/bi015982e 12022872
    • Plasmin-mediated activation and inactivation of thrombin-activatable fibrinolysis inhibitor. PF Marx PE Dawson BN Bouma JC Meijers, Biochemistry 2002 41 21 6688 6696 10.1021/bi015982e 12022872
    • (2002) Biochemistry , vol.41 , Issue.21 , pp. 6688-6696
    • Marx, P.F.1    Dawson, P.E.2    Bouma, B.N.3    Meijers, J.C.4
  • 18
    • 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
    • 10.1021/bi051956v 16445295
    • Post-translational modifications of human thrombin-activatable fibrinolysis inhibitor (TAFI): evidence for a large shift in the isoelectric point and reduced solubility upon activation. Z Valnickova T Christensen P Skottrup IB Thogersen P Hojrup JJ Enghild, Biochemistry 2006 45 5 1525 1535 10.1021/bi051956v 16445295
    • (2006) Biochemistry , vol.45 , Issue.5 , pp. 1525-1535
    • Valnickova, Z.1    Christensen, T.2    Skottrup, P.3    Thogersen, I.B.4    Hojrup, P.5    Enghild, J.J.6
  • 19
    • 17544370936 scopus 로고    scopus 로고
    • Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone protein
    • 10.1074/jbc.271.22.12937 8662763
    • Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone protein. Z Valnickova IB Thogersen S Christensen CT Chu SV Pizzo JJ Enghild, J Biol Chem 1996 271 22 12937 12943 10.1074/jbc.271.22.12937 8662763
    • (1996) J Biol Chem , vol.271 , Issue.22 , 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
  • 20
    • 0032538557 scopus 로고    scopus 로고
    • A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor
    • 10.1074/jbc.273.42.27176 9765237
    • A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor. W Wang MB Boffa L Bajzar JB Walker ME Nesheim, J Biol Chem 1998 273 42 27176 27181 10.1074/jbc.273.42.27176 9765237
    • (1998) J Biol Chem , vol.273 , Issue.42 , pp. 27176-27181
    • Wang, W.1    Boffa, M.B.2    Bajzar, L.3    Walker, J.B.4    Nesheim, M.E.5
  • 21
    • 0034725120 scopus 로고    scopus 로고
    • Roles of thermal instability and proteolytic cleavage in regulation of activated thrombin-activable fibrinolysis inhibitor
    • 10.1074/jbc.275.17.12868 10777585
    • Roles of thermal instability and proteolytic cleavage in regulation of activated thrombin-activable fibrinolysis inhibitor. MB Boffa R Bell WK Stevens ME Nesheim, J Biol Chem 2000 275 17 12868 12878 10.1074/jbc.275.17.12868 10777585
    • (2000) J Biol Chem , vol.275 , Issue.17 , pp. 12868-12878
    • Boffa, M.B.1    Bell, R.2    Stevens, W.K.3    Nesheim, M.E.4
  • 22
    • 0034725047 scopus 로고    scopus 로고
    • Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage
    • 10.1074/jbc.275.17.12410 10777524
    • Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage. PF Marx TM Hackeng PE Dawson JH Griffin JC Meijers BN Bouma, J Biol Chem 2000 275 17 12410 12415 10.1074/jbc.275.17.12410 10777524
    • (2000) J Biol Chem , vol.275 , Issue.17 , pp. 12410-12415
    • Marx, P.F.1    Hackeng, T.M.2    Dawson, P.E.3    Griffin, J.H.4    Meijers, J.C.5    Bouma, B.N.6
  • 23
    • 0036191244 scopus 로고    scopus 로고
    • Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N
    • 11939578
    • Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N. WD Campbell E Lazoura N Okada H Okada, Microbiol Immunol 2002 46 2 131 134 11939578
    • (2002) Microbiol Immunol , vol.46 , Issue.2 , pp. 131-134
    • Campbell, W.D.1    Lazoura, E.2    Okada, N.3    Okada, H.4
  • 24
    • 0345803939 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor, a potential regulator of vascular inflammation
    • 10.1074/jbc.M306977200 14525995
    • Thrombin activatable fibrinolysis inhibitor, a potential regulator of vascular inflammation. T Myles T Nishimura TH Yun M Nagashima J Morser AJ Patterson RG Pearl LL Leung, J Biol Chem 2003 278 51 51059 51067 10.1074/jbc.M306977200 14525995
    • (2003) J Biol Chem , vol.278 , Issue.51 , pp. 51059-51067
    • Myles, T.1    Nishimura, T.2    Yun, T.H.3    Nagashima, M.4    Morser, J.5    Patterson, A.J.6    Pearl, R.G.7    Leung, L.L.8
  • 26
    • 0036172375 scopus 로고    scopus 로고
    • Insulin resistance is associated with increased circulating level of thrombin-activatable fibrinolysis inhibitor in type 2 diabetic patients
    • 10.1210/jc.87.2.660 11836301
    • Insulin resistance is associated with increased circulating level of thrombin-activatable fibrinolysis inhibitor in type 2 diabetic patients. Y Hori EC Gabazza Y Yano A Katsuki K Suzuki Y Adachi Y Sumida, J Clin Endocrinol Metab 2002 87 2 660 665 10.1210/jc.87.2.660 11836301
    • (2002) J Clin Endocrinol Metab , 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
  • 29
    • 0035073313 scopus 로고    scopus 로고
    • Low levels of thrombin activatable fibrinolysis inhibitor (TAFI) in patients with chronic liver disease
    • 11341503
    • Low levels of thrombin activatable fibrinolysis inhibitor (TAFI) in patients with chronic liver disease. DH Van Thiel M George J Fareed, Thromb Haemost 2001 85 4 667 670 11341503
    • (2001) Thromb Haemost , vol.85 , Issue.4 , pp. 667-670
    • Van Thiel, D.H.1    George, M.2    Fareed, J.3
  • 30
    • 4444246103 scopus 로고    scopus 로고
    • A functional single nucleotide polymorphism in the thrombin-activatable fibrinolysis inhibitor (TAFI) gene associates with outcome of meningococcal disease
    • 10.1111/j.1538-7836.2004.00557.x 14717966
    • A functional single nucleotide polymorphism in the thrombin-activatable fibrinolysis inhibitor (TAFI) gene associates with outcome of meningococcal disease. JA Kremer Hovinga RF Franco MA Zago H Ten Cate RG Westendorp PH Reitsma, J Thromb Haemost 2004 2 1 54 57 10.1111/j.1538-7836.2004.00557.x 14717966
    • (2004) J Thromb Haemost , 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.5    Reitsma, P.H.6
  • 31
    • 0032877624 scopus 로고    scopus 로고
    • A novel approach to arterial thrombolysis
    • 10515877
    • A novel approach to arterial thrombolysis. P Klement P Liao L Bajzar, Blood 1999 94 8 2735 2743 10515877
    • (1999) Blood , vol.94 , Issue.8 , pp. 2735-2743
    • Klement, P.1    Liao, P.2    Bajzar, L.3
  • 34
    • 24944445159 scopus 로고    scopus 로고
    • Inhibition of carboxypeptidase U (TAFIa) activity improves rt-PA induced thrombolysis in a dog model of coronary artery thrombosis
    • 10.1016/j.thromres.2005.02.009 16181987
    • Inhibition of carboxypeptidase U (TAFIa) activity improves rt-PA induced thrombolysis in a dog model of coronary artery thrombosis. JA Bjorkman TI Abrahamsson VK Nerme CJ Mattsson, Thromb Res 2005 116 6 519 524 10.1016/j.thromres.2005.02.009 16181987
    • (2005) Thromb Res , vol.116 , Issue.6 , pp. 519-524
    • Bjorkman, J.A.1    Abrahamsson, T.I.2    Nerme, V.K.3    Mattsson, C.J.4
  • 35
    • 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
    • 10.1111/j.1538-7836.2006.02224.x 17002650
    • Characterization of rat thrombin-activatable fibrinolysis inhibitor (TAFI)-a comparative study assessing the biological equivalence of rat, murine and human TAFI. K Hillmayer A Macovei D Pauwels G Compernolle PJ Declerck A Gils, J Thromb Haemost 2006 4 11 2470 2477 10.1111/j.1538-7836.2006.02224.x 17002650
    • (2006) J Thromb Haemost , 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
  • 36
    • 33645563991 scopus 로고    scopus 로고
    • Murine model of ferric chloride-induced vena cava thrombosis: Evidence for effect of potato carboxypeptidase inhibitor
    • 10.1111/j.1538-7836.2006.01703.x 16420573
    • Murine model of ferric chloride-induced vena cava thrombosis: evidence for effect of potato carboxypeptidase inhibitor. X Wang PL Smith MY Hsu ML Ogletree WA Schumacher, J Thromb Haemost 2006 4 2 403 410 10.1111/j.1538-7836. 2006.01703.x 16420573
    • (2006) J Thromb Haemost , vol.4 , Issue.2 , pp. 403-410
    • Wang, X.1    Smith, P.L.2    Hsu, M.Y.3    Ogletree, M.L.4    Schumacher, W.A.5
  • 37
    • 0036482279 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor (TAFI) deficient mice
    • 10.2741/nagashim 11815293
    • Thrombin-activatable fibrinolysis inhibitor (TAFI) deficient mice. M Nagashima ZF Yin GJ Broze Jr J Morser, Front Biosci 2002 7 d556 568 10.2741/nagashim 11815293
    • (2002) Front Biosci , vol.7 , pp. 556-568
    • Nagashima, M.1    Yin, Z.F.2    Jr J., B.G.3    Morser, J.4
  • 39
    • 0036384505 scopus 로고    scopus 로고
    • Human procarboxypeptidase B: Three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI)
    • 10.1016/S0022-2836(02)00648-4 12162965
    • Human procarboxypeptidase B: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI). PJ Barbosa Pereira S Segura-Martin B Oliva C Ferrer-Orta FX Aviles M Coll FX Gomis-Ruth J Vendrell, J Mol Biol 2002 321 3 537 547 10.1016/S0022-2836(02)00648-4 12162965
    • (2002) J Mol Biol , vol.321 , Issue.3 , pp. 537-547
    • Barbosa Pereira, P.J.1    Segura-Martin, S.2    Oliva, B.3    Ferrer-Orta, C.4    Aviles, F.X.5    Coll, M.6    Gomis-Ruth, F.X.7    Vendrell, J.8
  • 40
    • 0015501866 scopus 로고
    • Isolation and characterization of pancreatic procarboxypeptidase B and carboxypeptidase B of the African lungfish
    • 10.1021/bi00771a018 5079891
    • Isolation and characterization of pancreatic procarboxypeptidase B and carboxypeptidase B of the African lungfish. GR Reeck H Neurath, Biochemistry 1972 11 21 3947 3955 10.1021/bi00771a018 5079891
    • (1972) Biochemistry , vol.11 , Issue.21 , pp. 3947-3955
    • Reeck, G.R.1    Neurath, H.2
  • 41
    • 53449101060 scopus 로고    scopus 로고
    • Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: A novel mechanism for enzyme autoregulation
    • 10.1182/blood-2008-03-146001 18559974
    • Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme autoregulation. PF Marx TH Brondijk T Plug RA Romijn W Hemrika JC Meijers EG Huizinga, Blood 2008 112 7 2803 2809 10.1182/blood-2008-03-146001 18559974
    • (2008) Blood , vol.112 , Issue.7 , 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
  • 42
    • 57649223597 scopus 로고    scopus 로고
    • The Crystal Structure of Thrombin-activable Fibrinolysis Inhibitor (TAFI) Provides the Structural Basis for Its Intrinsic Activity and the Short Half-life of TAFIa
    • 10.1074/jbc.M804003200 18669641
    • The Crystal Structure of Thrombin-activable Fibrinolysis Inhibitor (TAFI) Provides the Structural Basis for Its Intrinsic Activity and the Short Half-life of TAFIa. K Anand I Pallares Z Valnickova T Christensen J Vendrell KU Wendt HA Schreuder JJ Enghild FX Aviles, J Biol Chem 2008 283 43 29416 29423 10.1074/jbc.M804003200 18669641
    • (2008) J Biol Chem , vol.283 , Issue.43 , pp. 29416-29423
    • Anand, K.1    Pallares, I.2    Valnickova, Z.3    Christensen, T.4    Vendrell, J.5    Wendt, K.U.6    Schreuder, H.A.7    Enghild, J.J.8    Aviles, F.X.9
  • 43
    • 13544272567 scopus 로고    scopus 로고
    • A carboxypeptidase inhibitor from the tick Rhipicephalus bursa: Isolation, cDNA cloning, recombinant expression, and characterization
    • 10.1074/jbc.M411086200 15561703
    • A carboxypeptidase inhibitor from the tick Rhipicephalus bursa: isolation, cDNA cloning, recombinant expression, and characterization. JL Arolas J Lorenzo A Rovira J Castella FX Aviles CP Sommerhoff, J Biol Chem 2005 280 5 3441 3448 10.1074/jbc.M411086200 15561703
    • (2005) J Biol Chem , vol.280 , Issue.5 , pp. 3441-3448
    • Arolas, J.L.1    Lorenzo, J.2    Rovira, A.3    Castella, J.4    Aviles, F.X.5    Sommerhoff, C.P.6
  • 44
    • 20444446808 scopus 로고    scopus 로고
    • The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode
    • 10.1016/j.jmb.2005.05.015 15961103
    • The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode. JL Arolas GM Popowicz J Lorenzo CP Sommerhoff R Huber FX Aviles TA Holak, J Mol Biol 2005 350 3 489 498 10.1016/j.jmb.2005.05.015 15961103
    • (2005) J Mol Biol , vol.350 , Issue.3 , pp. 489-498
    • Arolas, J.L.1    Popowicz, G.M.2    Lorenzo, J.3    Sommerhoff, C.P.4    Huber, R.5    Aviles, F.X.6    Holak, T.A.7
  • 46
    • 39449126006 scopus 로고    scopus 로고
    • Biochemical Importance of Glycosylation in Thrombin Activatable Fibrinolysis Inhibitor
    • 10.1161/CIRCRESAHA.107.157099 18063813
    • Biochemical Importance of Glycosylation in Thrombin Activatable Fibrinolysis Inhibitor. K Buelens K Hillmayer G Compernolle PJ Declerck A Gils, Circ Res 2007 102 3 295 301 10.1161/CIRCRESAHA.107.157099 18063813
    • (2007) Circ Res , vol.102 , Issue.3 , pp. 295-301
    • Buelens, K.1    Hillmayer, K.2    Compernolle, G.3    Declerck, P.J.4    Gils, A.5
  • 47
    • 0031766583 scopus 로고    scopus 로고
    • Identification and characterization of two thrombin-activatable fibrinolysis inhibitor isoforms
    • 9869166
    • Identification and characterization of two thrombin-activatable fibrinolysis inhibitor isoforms. L Zhao J Morser L Bajzar M Nesheim M Nagashima, Thromb Haemost 1998 80 6 949 955 9869166
    • (1998) Thromb Haemost , vol.80 , Issue.6 , pp. 949-955
    • Zhao, L.1    Morser, J.2    Bajzar, L.3    Nesheim, M.4    Nagashima, M.5
  • 48
    • 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
    • 10.1111/j.1742-4658.2006.05110.x 16441664
    • Limited mutagenesis increases the stability of human carboxypeptidase U (TAFIa) and demonstrates the importance of CPU stability over proCPU concentration in down-regulating fibrinolysis. W Knecht J Willemse H Stenhamre M Andersson P Berntsson C Furebring A Harrysson AC Hager BM Wissing D Hendriks, Febs J 2006 273 4 778 792 10.1111/j.1742-4658.2006.05110.x 16441664
    • (2006) Febs J , vol.273 , Issue.4 , 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
  • 49
    • 34548840834 scopus 로고    scopus 로고
    • Comparative evaluation of stable TAFIa variants importance of alpha-helix 9 and beta-sheet 11 for TAFIa (in)stability
    • 10.1111/j.1538-7836.2007.02720.x 17666015
    • Comparative evaluation of stable TAFIa variants importance of alpha-helix 9 and beta-sheet 11 for TAFIa (in)stability. E Ceresa M De Maeyer A Jonckheer M Peeters Y Engelborghs PJ Declerck A Gils, J Thromb Haemost 2007 5 10 2105 12 10.1111/j.1538-7836.2007.02720.x 17666015
    • (2007) J Thromb Haemost , vol.5 , Issue.10 , pp. 2105-12
    • Ceresa, E.1    De Maeyer, M.2    Jonckheer, A.3    Peeters, M.4    Engelborghs, Y.5    Declerck, P.J.6    Gils, A.7
  • 50
    • 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
    • 10.1182/blood.V98.6.1992 11565542
    • 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. GJ Brouwers HL Vos FW Leebeek S Bulk M Schneider M Boffa M Koschinsky NH van Tilburg ME Nesheim RM Bertina, Blood 2001 98 6 1992 1993 10.1182/blood.V98.6.1992 11565542
    • (2001) Blood , vol.98 , Issue.6 , 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.7    Van Tilburg, N.H.8    Nesheim, M.E.9    Bertina, R.M.10
  • 51
    • 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
    • 10.1074/jbc.M104444200 11684677
    • Two naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme. M Schneider M Boffa R Stewart M Rahman M Koschinsky M Nesheim, J Biol Chem 2002 277 2 1021 1030 10.1074/jbc.M104444200 11684677
    • (2002) J Biol Chem , 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
  • 52
    • 24944454310 scopus 로고    scopus 로고
    • Role of isoleucine residues 182 and 183 in thrombin-activatable fibrinolysis inhibitor
    • 10.1111/j.1538-7836.2005.01322.x 15946220
    • Role of isoleucine residues 182 and 183 in thrombin-activatable fibrinolysis inhibitor. PF Marx SR Havik BN Bouma JC Meijers, J Thromb Haemost 2005 3 6 1293 1300 10.1111/j.1538-7836.2005.01322.x 15946220
    • (2005) J Thromb Haemost , vol.3 , Issue.6 , pp. 1293-1300
    • Marx, P.F.1    Havik, S.R.2    Bouma, B.N.3    Meijers, J.C.4
  • 53
    • 0014932863 scopus 로고
    • Plasminogen: Purification from human plasma by affinity chromatography
    • 10.1126/science.170.3962.1095 5475635
    • Plasminogen: purification from human plasma by affinity chromatography. DG Deutsch ET Mertz, Science 1970 170 962 1095 1096 10.1126/science.170.3962. 1095 5475635
    • (1970) Science , vol.170 , Issue.962 , pp. 1095-1096
    • Deutsch, D.G.1    Mertz, E.T.2
  • 54
    • 0019792891 scopus 로고
    • Evaluation of three sodium dodecyl sulphate-polyacrylamide gel electrophoresis buffer systems
    • 10.1016/S0021-9673(00)80500-2
    • Evaluation of three sodium dodecyl sulphate-polyacrylamide gel electrophoresis buffer systems. AF Bury, J Chromatogr 1981 213 491 450 10.1016/S0021-9673(00)80500-2
    • (1981) J Chromatogr , vol.213 , pp. 491-450
    • Bury, A.F.1
  • 55
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • 3611052
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. P Matsudaira, J Biol Chem 1987 262 21 10035 10038 3611052
    • (1987) J Biol Chem , vol.262 , Issue.21 , pp. 10035-10038
    • Matsudaira, P.1
  • 56
    • 0022248719 scopus 로고
    • Assay of carboxypeptidase N activity in serum by liquid-chromatographic determination of hippuric acid
    • 3933850
    • Assay of carboxypeptidase N activity in serum by liquid-chromatographic determination of hippuric acid. D Hendriks S Scharpe M van Sande, Clin Chem 1985 31 12 1936 1939 3933850
    • (1985) Clin Chem , vol.31 , Issue.12 , pp. 1936-1939
    • Hendriks, D.1    Scharpe, S.2    Van Sande, M.3
  • 57
    • 0030611710 scopus 로고    scopus 로고
    • Resistance of gammaA/gamma' fibrin clots to fibrinolysis
    • 10.1074/jbc.272.22.14251 9162058
    • Resistance of gammaA/gamma' fibrin clots to fibrinolysis. LA Falls DH Farrell, J Biol Chem 1997 272 22 14251 14256 10.1074/jbc.272.22.14251 9162058
    • (1997) J Biol Chem , vol.272 , Issue.22 , pp. 14251-14256
    • Falls, L.A.1    Farrell, D.H.2
  • 58
    • 0033057707 scopus 로고    scopus 로고
    • Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry
    • 10.1002/(SICI)1096-9888(199902)34:2<105::AID-JMS768>3.0.CO;2-4 10093212
    • Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J Gobom E Nordhoff E Mirgorodskaya R Ekman P Roepstorff, J Mass Spectrom 1999 34 2 105 116 10.1002/(SICI)1096-9888(199902)34:2<105::AID-JMS768>3.0.CO;2-4 10093212
    • (1999) J Mass Spectrom , vol.34 , Issue.2 , pp. 105-116
    • Gobom, J.1    Nordhoff, E.2    Mirgorodskaya, E.3    Ekman, R.4    Roepstorff, P.5


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