메뉴 건너뛰기




Volumn 114, Issue 4, 2004, Pages 301-306

Inactivation of antiplasmin at low pH: Evidence for the formation of latent molecules

Author keywords

Antiplasmin; Inactivation; Latent; Serpin; Stability

Indexed keywords

ANTIPLASMIN;

EID: 4744358097     PISSN: 00493848     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.thromres.2004.06.014     Document Type: Article
Times cited : (4)

References (37)
  • 2
    • 0028912190 scopus 로고
    • A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism
    • Shore J.D., Day D.E., Francis-Chmura A.M., Verhamme I., Kvassman J., Lawrence D.A., et al. A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism. J. Biol. Chem. 270:1995;5395-5398
    • (1995) J. Biol. Chem. , vol.270 , pp. 5395-5398
    • Shore, J.D.1    Day, D.E.2    Francis-Chmura, A.M.3    Verhamme, I.4    Kvassman, J.5    Lawrence, D.A.6
  • 4
    • 0032546803 scopus 로고    scopus 로고
    • Mapping the serpin-proteinase complex using single cysteine variants of alpha1-proteinase inhibitor Pittsburgh
    • Stratikos E., Getting P.G.W. Mapping the serpin-proteinase complex using single cysteine variants of alpha1-proteinase inhibitor Pittsburgh. J. Biol. Chem. 273:1998;15582-15589
    • (1998) J. Biol. Chem. , vol.273 , pp. 15582-15589
    • Stratikos, E.1    Getting, P.G.W.2
  • 5
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington J.A., Read R.J., Carrell R.W. Structure of a serpin-protease complex shows inhibition by deformation. Nature. 407:2000;923-926
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 6
    • 0032532347 scopus 로고    scopus 로고
    • Antithrombins Wibble and Wobble (T85M/K): Archetypal conformational diseases with in vivo latent-transition, thrombosis, and heparin activation
    • Beauchamp N.J., Pike R.N., Daly M., Butler L., Makris M., Dafforn T., et al. Antithrombins Wibble and Wobble (T85M/K): archetypal conformational diseases with in vivo latent-transition, thrombosis, and heparin activation. Blood. 92:1998;2696-2706
    • (1998) Blood , vol.92 , pp. 2696-2706
    • Beauchamp, N.J.1    Pike, R.N.2    Daly, M.3    Butler, L.4    Makris, M.5    Dafforn, T.6
  • 7
    • 0032488667 scopus 로고    scopus 로고
    • Latent alpha1-antichymotrypsin. A molecular explanation for the inactivation of alpha1-antichymotrypsin in chronic bronchitis and emphysema
    • Chang W.S.W., Lomas D.A. Latent alpha1-antichymotrypsin. A molecular explanation for the inactivation of alpha1-antichymotrypsin in chronic bronchitis and emphysema. J. Biol. Chem. 273:1998;3695-3701
    • (1998) J. Biol. Chem. , vol.273 , pp. 3695-3701
    • Chang, W.S.W.1    Lomas, D.A.2
  • 9
    • 0022243864 scopus 로고
    • Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants
    • Hekman C.M., Loskutoff D.J. Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants. J. Biol. Chem. 260:1985;11581-11587
    • (1985) J. Biol. Chem. , vol.260 , pp. 11581-11587
    • Hekman, C.M.1    Loskutoff, D.J.2
  • 11
    • 0024537999 scopus 로고
    • Purification of high and low molecular weight plasminogen activator inhibitor 1 from fibrosarcoma cell-line HT 1080 conditioned medium
    • Lindahl T., Wiman B. Purification of high and low molecular weight plasminogen activator inhibitor 1 from fibrosarcoma cell-line HT 1080 conditioned medium. Biochim. Biophys. Acta. 994:1989;253-257
    • (1989) Biochim. Biophys. Acta , vol.994 , pp. 253-257
    • Lindahl, T.1    Wiman, B.2
  • 12
    • 0028937232 scopus 로고
    • Conformational studies on plasminogen activator inhibitor (PAI-1) in active, latent, substrate, and cleaved forms
    • Sancho E., Declerck P.J., Price N.C., Kelly S.M., Booth N.A. Conformational studies on plasminogen activator inhibitor (PAI-1) in active, latent, substrate, and cleaved forms. Biochemistry. 34:1995;1064-1069
    • (1995) Biochemistry , vol.34 , pp. 1064-1069
    • Sancho, E.1    Declerck, P.J.2    Price, N.C.3    Kelly, S.M.4    Booth, N.A.5
  • 13
    • 0029022692 scopus 로고
    • Molecular evolution of plasminogen activator inhibitor-1 functional stability
    • Berkenpas M.B., Lawrence D.A., Ginsburg D. Molecular evolution of plasminogen activator inhibitor-1 functional stability. EMBO J. 14:1995;2969-2977
    • (1995) EMBO J. , vol.14 , pp. 2969-2977
    • Berkenpas, M.B.1    Lawrence, D.A.2    Ginsburg, D.3
  • 14
    • 0343517587 scopus 로고    scopus 로고
    • PAI-1 stability: The role of histidine residues
    • Mångs H., Sui G.C., Wiman B. PAI-1 stability: the role of histidine residues. FEBS Lett. 475:2000;192-196
    • (2000) FEBS Lett. , vol.475 , pp. 192-196
    • Mångs, H.1    Sui, G.C.2    Wiman, B.3
  • 15
    • 0024427263 scopus 로고
    • Stability of plasminogen activator inhibitor 1 (PAI-1)
    • Lindahl T.L., Sigurdardottir O., Wiman B. Stability of plasminogen activator inhibitor 1 (PAI-1). Thromb. Haemost. 62:1989;748-751
    • (1989) Thromb. Haemost. , vol.62 , pp. 748-751
    • Lindahl, T.L.1    Sigurdardottir, O.2    Wiman, B.3
  • 16
    • 0642308772 scopus 로고
    • On the relationship between different molecular forms of the fast inhibitor of tissue plasminogen activator
    • Chmielewska J., Carlsson T., Urden G., Wiman B. On the relationship between different molecular forms of the fast inhibitor of tissue plasminogen activator. Fibrinolysis. 1:1987;67-73
    • (1987) Fibrinolysis , vol.1 , pp. 67-73
    • Chmielewska, J.1    Carlsson, T.2    Urden, G.3    Wiman, B.4
  • 17
    • 0023685082 scopus 로고
    • Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma. Identification as a multimeric form of S protein (vitronectin)
    • Declerck P.J., De Mol M., Alessi M.C., Baudner S., Paques E.P., Preissner K.T., et al. Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma. Identification as a multimeric form of S protein (vitronectin). J. Biol. Chem. 263:1988;15454-15461
    • (1988) J. Biol. Chem. , vol.263 , pp. 15454-15461
    • Declerck, P.J.1    De Mol, M.2    Alessi, M.C.3    Baudner, S.4    Paques, E.P.5    Preissner, K.T.6
  • 18
    • 0024213555 scopus 로고
    • Plasminogen activator inhibitor 1 (PAI) is bound to vitronectin in plasma
    • Wiman B., Almquist Å., Sigurdardottir O., Lindahl T. Plasminogen activator inhibitor 1 (PAI) is bound to vitronectin in plasma. FEBS Lett. 242:1988;125-128
    • (1988) FEBS Lett. , vol.242 , pp. 125-128
    • Wiman, B.1    Almquist, Å.2    Sigurdardottir, O.3    Lindahl, T.4
  • 19
    • 0024427263 scopus 로고
    • Stability of plasminogen activator inhibitor 1 (PAI-1)
    • Lindahl T.L., Sigurdardottir O., Wiman B. Stability of plasminogen activator inhibitor 1 (PAI-1). Thromb. Haemost. 62:1989;748-751
    • (1989) Thromb. Haemost. , vol.62 , pp. 748-751
    • Lindahl, T.L.1    Sigurdardottir, O.2    Wiman, B.3
  • 20
    • 0030700799 scopus 로고    scopus 로고
    • Preparative induction and characterization of L-antithrombin: A structural homologue of latent plasminogen activator inhibitor-1
    • Wardell M.R., Chang W.S., Bruce D., Skinner R., Lesk A.M., Carrell R.W. Preparative induction and characterization of L-antithrombin: a structural homologue of latent plasminogen activator inhibitor-1. Biochemistry. 36:1997;13133-13142
    • (1997) Biochemistry , vol.36 , pp. 13133-13142
    • Wardell, M.R.1    Chang, W.S.2    Bruce, D.3    Skinner, R.4    Lesk, A.M.5    Carrell, R.W.6
  • 21
    • 0026532063 scopus 로고
    • Conformation of the reactive site loop of alpha 1-proteinase inhibitor probed by limited proteolysis
    • Mast A.E., Enghild J.J., Salvesen G. Conformation of the reactive site loop of alpha 1-proteinase inhibitor probed by limited proteolysis. Biochemistry. 31:1992;2720-2728
    • (1992) Biochemistry , vol.31 , pp. 2720-2728
    • Mast, A.E.1    Enghild, J.J.2    Salvesen, G.3
  • 24
    • 0027999955 scopus 로고
    • Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn→Asp)
    • Bruce D., Perry D.J., Borg J.Y., Carrell R.W., Wardell M.R. Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn→Asp). J. Clin. Invest. 94:1994;2265-2274
    • (1994) J. Clin. Invest. , vol.94 , pp. 2265-2274
    • Bruce, D.1    Perry, D.J.2    Borg, J.Y.3    Carrell, R.W.4    Wardell, M.R.5
  • 25
    • 0028915906 scopus 로고
    • Antithrombin-TRI (Ala382 to Thr) causing severe thromboembolic tendency undergoes the S-to-R transition and is associated with a plasma-inactive high-molecular-weight complex of aggregated antithrombin
    • Lindo V.S., Kakkar V.V., Learmonth M., Melissari E., Zappacosta F., Panico M., et al. Antithrombin-TRI (Ala382 to Thr) causing severe thromboembolic tendency undergoes the S-to-R transition and is associated with a plasma-inactive high-molecular-weight complex of aggregated antithrombin. Br. J. Haematol. 89:1995;589-601
    • (1995) Br. J. Haematol. , vol.89 , pp. 589-601
    • Lindo, V.S.1    Kakkar, V.V.2    Learmonth, M.3    Melissari, E.4    Zappacosta, F.5    Panico, M.6
  • 26
    • 0026755363 scopus 로고
    • The mechanism of Z alpha 1-antitrypsin accumulation in the liver
    • Lomas D.A., Evans D.L., Finch J.T., Carrell R.W. The mechanism of Z alpha 1-antitrypsin accumulation in the liver. Nature. 357:1992;605-607
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 27
    • 0027295822 scopus 로고
    • Alpha 1-antitrypsin Siiyama (Ser53→Phe): Further evidence for intracellular loop-sheet polymerisation
    • Lomas D.A., Finch J.T., Seyama K., Nukiva T., Carrell R.W. Alpha 1-antitrypsin Siiyama (Ser53→Phe): further evidence for intracellular loop-sheet polymerisation. J. Biol. Chem. 268:1993;15333-15335
    • (1993) J. Biol. Chem. , vol.268 , pp. 15333-15335
    • Lomas, D.A.1    Finch, J.T.2    Seyama, K.3    Nukiva, T.4    Carrell, R.W.5
  • 29
    • 0037446935 scopus 로고    scopus 로고
    • A redox-sensitive loop regulates plasminogen activator inhibitor type 2 (PAI-2) polymerisation
    • Wilczynska M., Lobov S., Ohlsson P.I., Ny T. A redox-sensitive loop regulates plasminogen activator inhibitor type 2 (PAI-2) polymerisation. EMBO J. 22:2003;1753-1761
    • (2003) EMBO J. , vol.22 , pp. 1753-1761
    • Wilczynska, M.1    Lobov, S.2    Ohlsson, P.I.3    Ny, T.4
  • 30
    • 0017710297 scopus 로고
    • Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma
    • Wiman B., Collen D. Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma. Eur. J. Biochem. 78:1977;19-26
    • (1977) Eur. J. Biochem. , vol.78 , pp. 19-26
    • Wiman, B.1    Collen, D.2
  • 31
    • 0019159024 scopus 로고
    • Affinity-chromatographic purification of human alpha 2-antiplasmin
    • Wiman B. Affinity-chromatographic purification of human alpha 2-antiplasmin. Biochem. J. 191:1980;229-232
    • (1980) Biochem. J. , vol.191 , pp. 229-232
    • Wiman, B.1
  • 33
    • 0015690747 scopus 로고
    • Multiphasic zone electrophoresis: IV. Design and analysis of discontinuous buffer systems with a digital computer
    • Jovin T.M. Multiphasic zone electrophoresis: IV. Design and analysis of discontinuous buffer systems with a digital computer. Ann. N. Y. Acad. Sci. 209:1973;477-496
    • (1973) Ann. N. Y. Acad. Sci. , vol.209 , pp. 477-496
    • Jovin, T.M.1
  • 34
    • 0034713878 scopus 로고    scopus 로고
    • Structures of active and latent PAI-1: A possible stabilizing role for chloride ions
    • Stout T.J., Graham H., Buckley D.I., Matthews D.J. Structures of active and latent PAI-1: a possible stabilizing role for chloride ions. Biochemistry. 39:2000;8460-8469
    • (2000) Biochemistry , vol.39 , pp. 8460-8469
    • Stout, T.J.1    Graham, H.2    Buckley, D.I.3    Matthews, D.J.4
  • 35
    • 0038053035 scopus 로고    scopus 로고
    • Serpin polymerization is prevented by a hydrogen bond network that is centered on his-334 and stabilized by glycerol
    • Zhou A., Stein P.E., Huntington J.A., Carrell R.W. Serpin polymerization is prevented by a hydrogen bond network that is centered on his-334 and stabilized by glycerol. J. Biol. Chem. 278:2003;15116-15122
    • (2003) J. Biol. Chem. , vol.278 , pp. 15116-15122
    • Zhou, A.1    Stein, P.E.2    Huntington, J.A.3    Carrell, R.W.4
  • 36
    • 0028773279 scopus 로고
    • Biological implications of a 3 a structure of dimeric antithrombin
    • Carrell R.W., Stein P.E., Fermi G., Wardell M.R. Biological implications of a 3 A structure of dimeric antithrombin. Structure. 2:1994;257-270
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.