메뉴 건너뛰기




Volumn 11, Issue 5-6, 1997, Pages 265-271

Construction and characterization of plasminogen activator inhibitor-1 mutants in which part of the active site loop is deleted

Author keywords

[No Author keywords available]

Indexed keywords

PLASMINOGEN ACTIVATOR INHIBITOR 1;

EID: 0031474233     PISSN: 13690191     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0268-9499(97)80111-7     Document Type: Article
Times cited : (4)

References (46)
  • 2
    • 0345693050 scopus 로고
    • Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor
    • Ny T, Sawdey M, Lawrence D, Milan JL, Loskutoff DJ. Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor. Proc Natl Acad Sci USA 1986; 83: 6776-6780.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6776-6780
    • Ny, T.1    Sawdey, M.2    Lawrence, D.3    Milan, J.L.4    Loskutoff, D.J.5
  • 3
    • 0022852285 scopus 로고
    • cDNA cloning of human plasminogen activator-inhibitor from endothelial cells
    • Ginsburg D, Zeheb R, Young AY, et al. cDNA cloning of human plasminogen activator-inhibitor from endothelial cells. J Clin Invest 1986; 78: 1673-1680.
    • (1986) J Clin Invest , vol.78 , pp. 1673-1680
    • Ginsburg, D.1    Zeheb, R.2    Young, A.Y.3
  • 4
    • 0022887824 scopus 로고
    • Plasminogen activator inhibitor type 1: Reactive center and amino-terminal heterogeneity determined by protein and cDNA sequencing
    • Andreasen PA, Riccio A, Welinder KG et al. Plasminogen activator inhibitor type 1: reactive center and amino-terminal heterogeneity determined by protein and cDNA sequencing. FEBS Lett 1986; 209: 213-218.
    • (1986) FEBS Lett , vol.209 , pp. 213-218
    • Andreasen, P.A.1    Riccio, A.2    Welinder, K.G.3
  • 5
    • 0001724344 scopus 로고
    • Barret AJ, Salvesen G, eds. Amsterdam: Elsevier Scientific Publishing Co
    • Carrell RW, Boswell DR. In: Barret AJ, Salvesen G, eds. Proteinase Inhibitors. Amsterdam: Elsevier Scientific Publishing Co 1986: 403-425.
    • (1986) Proteinase Inhibitors , pp. 403-425
    • Carrell, R.W.1    Boswell, D.R.2
  • 6
    • 0024423930 scopus 로고
    • 1-antitrypsin for structure and function of serpins
    • 1-antitrypsin for structure and function of serpins. Biochemistry 1989; 28: 8951-8966.
    • (1989) Biochemistry , vol.28 , pp. 8951-8966
    • Huber, R.1    Carrell, R.W.2
  • 7
    • 0026571516 scopus 로고
    • The latent tendencies of PAI-1
    • Sprang SR. The latent tendencies of PAI-1. Trends Biochem Sci 1992; 17: 49-50.
    • (1992) Trends Biochem Sci , vol.17 , pp. 49-50
    • Sprang, S.R.1
  • 8
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M, Kato I. Protein inhibitors of proteinases. Annu Rev Biochem 1980; 49: 593-626.
    • (1980) Annu Rev Biochem , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 9
    • 0025021029 scopus 로고
    • The mechanism of the reaction between human plasminogen activator inhibitor-1 and tissue plasminogen activator
    • Lindahl TL, Ohlsson PI, Wiman B. The mechanism of the reaction between human plasminogen activator inhibitor-1 and tissue plasminogen activator. Biochem J 1990; 265: 109-113.
    • (1990) Biochem J , vol.265 , pp. 109-113
    • Lindahl, T.L.1    Ohlsson, P.I.2    Wiman, B.3
  • 10
    • 0023687390 scopus 로고
    • Purification and characterization of natural and recombinant human plasminogen activator inhibitor-1 (PAI-1)
    • Alessi MC, Declerck PJ, De Mol M, Nelles L, Collen D. Purification and characterization of natural and recombinant human plasminogen activator inhibitor-1 (PAI-1). Eur J Biochem 1988; 175: 531-540.
    • (1988) Eur J Biochem , vol.175 , pp. 531-540
    • Alessi, M.C.1    Declerck, P.J.2    De Mol, M.3    Nelles, L.4    Collen, D.5
  • 11
    • 0024791659 scopus 로고
    • Purification of active human plasminogen activator inhibitor-1 from Escherichia coli. Comparison with natural and recombinant forms purified from eucaryotic cells
    • Lawrence DA, Strandberg L, Grundstrom T, Ny T. Purification of active human plasminogen activator inhibitor-1 from Escherichia coli. Comparison with natural and recombinant forms purified from eucaryotic cells. Eur J Biochem 1989; 186: 523-533.
    • (1989) Eur J Biochem , vol.186 , pp. 523-533
    • Lawrence, D.A.1    Strandberg, L.2    Grundstrom, T.3    Ny, T.4
  • 12
    • 0026546881 scopus 로고
    • Structural basis of latency in plasminogen activator inhibitor-1
    • Mottonen J, Strand A, Symersky J, et al. Structural basis of latency in plasminogen activator inhibitor-1. Nature 1992; 355: 270-273.
    • (1992) Nature , vol.355 , pp. 270-273
    • Mottonen, J.1    Strand, A.2    Symersky, J.3
  • 13
    • 0022243864 scopus 로고
    • Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants
    • Hekman CM, Loskutoff DJ. Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants. J Biol Chem 1985; 260: 11581-11587.
    • (1985) J Biol Chem , vol.260 , pp. 11581-11587
    • Hekman, C.M.1    Loskutoff, D.J.2
  • 14
    • 0026664170 scopus 로고
    • Identification of a conformationally distinct form of plasminogen activator inhibitor-1, acting as a non-inhibitory substrate for tissue-type plasminogen activator
    • Declerck PJ, De Mol M, Vaughan DE, Collen D. Identification of a conformationally distinct form of plasminogen activator inhibitor-1, acting as a non-inhibitory substrate for tissue-type plasminogen activator. J Biol Chem 1992; 267: 11693-11696.
    • (1992) J Biol Chem , vol.267 , pp. 11693-11696
    • Declerck, P.J.1    De Mol, M.2    Vaughan, D.E.3    Collen, D.4
  • 15
    • 0026471040 scopus 로고
    • A substrate-like form of plasminogen activator inhibitor type 1. Conversions between different forms by sodium dodecyl sulphate
    • Urano T, Strandberg L, Johansson LB, Ny T. A substrate-like form of plasminogen activator inhibitor type 1. Conversions between different forms by sodium dodecyl sulphate. Eur J Biochem 1992; 209: 985-992.
    • (1992) Eur J Biochem , vol.209 , pp. 985-992
    • Urano, T.1    Strandberg, L.2    Johansson, L.B.3    Ny, T.4
  • 16
    • 0027290655 scopus 로고
    • Interconversions between active, inert and substrate forms of denatured/refolded type-1 plasminogen activator inhibitor
    • Munch M, Heegaard CW, Andreasen PA. Interconversions between active, inert and substrate forms of denatured/refolded type-1 plasminogen activator inhibitor. Biochim Biophys Acta 1993; 1202: 29-37.
    • (1993) Biochim Biophys Acta , vol.1202 , pp. 29-37
    • Munch, M.1    Heegaard, C.W.2    Andreasen, P.A.3
  • 18
    • 0024344169 scopus 로고
    • Efficient oligonucleotide-directed construction of mutations in expression vectors by the gapped duplex DNA method using alternating selectable markers
    • Stanssens P, Opsomer C, McKeown YM, Kramer W, Zabeau M, Fritz HJ. Efficient oligonucleotide-directed construction of mutations in expression vectors by the gapped duplex DNA method using alternating selectable markers. Nucleic Acids Res 1989; 17: 4441-4454.
    • (1989) Nucleic Acids Res , vol.17 , pp. 4441-4454
    • Stanssens, P.1    Opsomer, C.2    McKeown, Y.M.3    Kramer, W.4    Zabeau, M.5    Fritz, H.J.6
  • 19
    • 0028064911 scopus 로고
    • Conversion of plasminogen activator inhibitor-1 from inhibitor to substrate by point mutations in the reactive-site loop
    • Audenaert AM, Knockaert I, Collen D, Declerck PJ. Conversion of plasminogen activator inhibitor-1 from inhibitor to substrate by point mutations in the reactive-site loop. J Biol Chem 1994; 269: 19559-19564.
    • (1994) J Biol Chem , vol.269 , pp. 19559-19564
    • Audenaert, A.M.1    Knockaert, I.2    Collen, D.3    Declerck, P.J.4
  • 20
    • 0029943026 scopus 로고    scopus 로고
    • Substrate behaviour of plasminogen activator inhibitor-1 is not associated with a lack of insertion of the reactive site loop
    • Gils A, Knockaert I, Declerck PJ. Substrate behaviour of plasminogen activator inhibitor-1 is not associated with a lack of insertion of the reactive site loop. Biochemistry 1996; 35: 7474-7481.
    • (1996) Biochemistry , vol.35 , pp. 7474-7481
    • Gils, A.1    Knockaert, I.2    Declerck, P.J.3
  • 21
    • 0021214374 scopus 로고
    • Evidence for the occurrence of a fast-acting inhibitor for tissue-type plasminogen activator in human plasma
    • Verheijen JH, Chang GTG, Kluft C. Evidence for the occurrence of a fast-acting inhibitor for tissue-type plasminogen activator in human plasma. Thromb Haemost 1984; 51: 392-395.
    • (1984) Thromb Haemost , vol.51 , pp. 392-395
    • Verheijen, J.H.1    Chang, G.T.G.2    Kluft, C.3
  • 22
    • 0027965876 scopus 로고
    • Purification and characterization of active and stable recombinant plasminogen activator inhibitor (PAI-1) accumulated at high level in Escherichia coli
    • Sancho E, Tonge DW, Hockney RC, Booth NA. Purification and characterization of active and stable recombinant plasminogen activator inhibitor (PAI-1) accumulated at high level in Escherichia coli. Eur J Biochem 1994; 224: 125-134.
    • (1994) Eur J Biochem , vol.224 , pp. 125-134
    • Sancho, E.1    Tonge, D.W.2    Hockney, R.C.3    Booth, N.A.4
  • 23
    • 0023840967 scopus 로고
    • Measurement of plasminogen activator inhibitor-1 in biological fluids with a murine monoclonal antibody-based enzyme-linked immunosorbent assay
    • Declerck PJ, Alessi MC, Verstreken M, Kruithof EKO, Juhan-Vague I, Collen D. Measurement of plasminogen activator inhibitor-1 in biological fluids with a murine monoclonal antibody-based enzyme-linked immunosorbent assay. Blood 1988; 71: 220-225.
    • (1988) Blood , vol.71 , pp. 220-225
    • Declerck, P.J.1    Alessi, M.C.2    Verstreken, M.3    Kruithof, E.K.O.4    Juhan-Vague, I.5    Collen, D.6
  • 24
    • 0028281746 scopus 로고
    • Engineering plasminogen activator inhibitor 1 mutants with increased functional stability
    • Lawrence DA, Olson ST, Palaniappan S, Ginsburg D. Engineering plasminogen activator inhibitor 1 mutants with increased functional stability. Biochemistry 1994; 33: 3643-3648.
    • (1994) Biochemistry , vol.33 , pp. 3643-3648
    • Lawrence, D.A.1    Olson, S.T.2    Palaniappan, S.3    Ginsburg, D.4
  • 25
    • 0029022692 scopus 로고
    • Molecular evolution of plasminogen activator inhibitor-1: Functional stability
    • Berkenpas MB, Lawrence DA, Ginsburg D. Molecular evolution of plasminogen activator inhibitor-1: functional stability. EMBO J 1995; 14: 2969-2977.
    • (1995) EMBO J , vol.14 , pp. 2969-2977
    • Berkenpas, M.B.1    Lawrence, D.A.2    Ginsburg, D.3
  • 26
    • 0029317438 scopus 로고
    • Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition
    • Tucker HM, Mottonen J, Goldsmith EJ, Gerard RD. Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition. Nature Struct Biol 1995; 2: 442-445.
    • (1995) Nature Struct Biol , vol.2 , pp. 442-445
    • Tucker, H.M.1    Mottonen, J.2    Goldsmith, E.J.3    Gerard, R.D.4
  • 27
    • 0023716783 scopus 로고
    • Antithrombin-III-Hamilton: A gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity
    • Devraj-Kizuk R, Chui DH, Prochownik EV, Carter CJ, Ofosu FA, Blajchman MA. Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity. Blood 1988; 72: 1518-1523.
    • (1988) Blood , vol.72 , pp. 1518-1523
    • Devraj-Kizuk, R.1    Chui, D.H.2    Prochownik, E.V.3    Carter, C.J.4    Ofosu, F.A.5    Blajchman, M.A.6
  • 28
    • 0024418272 scopus 로고
    • Antithrombin Cambridge, 384 Ala to Pro: A new variant identified using the polymerase chain reaction
    • Perry DJ, Harper PL, Fairham S, Daly M, Carrell RW. Antithrombin Cambridge, 384 Ala to Pro: a new variant identified using the polymerase chain reaction. FEBS Lett 1989; 254: 174-176.
    • (1989) FEBS Lett , vol.254 , pp. 174-176
    • Perry, D.J.1    Harper, P.L.2    Fairham, S.3    Daly, M.4    Carrell, R.W.5
  • 29
    • 0025097925 scopus 로고
    • Type II Hereditary angioneurotic edema that may result from a single nucleotide change in the codon for alanine-436 in the C1 inhibitor gene
    • Levy NJ, Ramesh N, Cicardi M, Harrison RA, Davis AE. Type II Hereditary angioneurotic edema that may result from a single nucleotide change in the codon for alanine-436 in the C1 inhibitor gene. Proc Natl Acad Sci USA 1990; 87: 265-268.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 265-268
    • Levy, N.J.1    Ramesh, N.2    Cicardi, M.3    Harrison, R.A.4    Davis, A.E.5
  • 30
    • 0025947568 scopus 로고
    • Antithrombin Glasgow II: Alanine 382 to threonine mutation in the serpin P12 position, resulting in a substrate reaction with thrombin
    • Ireland H, Lane DA, Thompson E, et al. Antithrombin Glasgow II: alanine 382 to threonine mutation in the serpin P12 position, resulting in a substrate reaction with thrombin. Br J Haematol 1991; 79: 70-74.
    • (1991) Br J Haematol , vol.79 , pp. 70-74
    • Ireland, H.1    Lane, D.A.2    Thompson, E.3
  • 31
    • 0025797520 scopus 로고
    • Antithrombin Cambridge II, 384 Ala to SER. Further evidence of the role of the reactive centre loop in the inhibitory function of the serpins
    • Perry DJ, Daly M, Harper PL, Tait RC, Price J, Walker ID, Carrell RW. Antithrombin Cambridge II, 384 Ala to SER. Further evidence of the role of the reactive centre loop in the inhibitory function of the serpins. FEBS Lett 1991; 285: 248-250.
    • (1991) FEBS Lett , vol.285 , pp. 248-250
    • Perry, D.J.1    Daly, M.2    Harper, P.L.3    Tait, R.C.4    Price, J.5    Walker, I.D.6    Carrell, R.W.7
  • 33
    • 17444434242 scopus 로고
    • C1 inhibitor hinge region mutations produce dysfunction by different mechanisms
    • Davis AE, Aulak K, Parad RB, et al. C1 inhibitor hinge region mutations produce dysfunction by different mechanisms. Nat Genet 1992; 1: 354-358.
    • (1992) Nat Genet , vol.1 , pp. 354-358
    • Davis, A.E.1    Aulak, K.2    Parad, R.B.3
  • 34
    • 0027923966 scopus 로고
    • A hinge region mutation in C1-inhibitor (Ala436→Thr) results in nonsubstrate-like behavior and in polymerization of the molecule
    • Aulak KS, Eldering E, Hack CE, et al. A hinge region mutation in C1-inhibitor (Ala436→Thr) results in nonsubstrate-like behavior and in polymerization of the molecule. J Biol Chem 1993; 268: 18088-18094.
    • (1993) J Biol Chem , vol.268 , pp. 18088-18094
    • Aulak, K.S.1    Eldering, E.2    Hack, C.E.3
  • 35
    • 0027945176 scopus 로고
    • Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition
    • Lawrence DA, Olson ST, Palaniappan S, Ginsburg D. Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition. J Biol Chem 1994; 269: 27657-27662.
    • (1994) J Biol Chem , vol.269 , pp. 27657-27662
    • Lawrence, D.A.1    Olson, S.T.2    Palaniappan, S.3    Ginsburg, D.4
  • 36
    • 0030973123 scopus 로고    scopus 로고
    • Proteinase specificity and functional diversity in point mutants of plasminogen activator inhibitor 1
    • Gils A, Declerck PJ. Proteinase specificity and functional diversity in point mutants of plasminogen activator inhibitor 1. J Biol Chem 1997; 272: 12662-12666.
    • (1997) J Biol Chem , vol.272 , pp. 12662-12666
    • Gils, A.1    Declerck, P.J.2
  • 37
    • 0025936528 scopus 로고
    • Mobile reactive centre of serpins and the control of thrombosis
    • Carrell RW, Evans DL, Stein P. Mobile reactive centre of serpins and the control of thrombosis. Nature 1991; 353: 576-578.
    • (1991) Nature , vol.353 , pp. 576-578
    • Carrell, R.W.1    Evans, D.L.2    Stein, P.3
  • 39
    • 0028359849 scopus 로고
    • Proteolytically cleaved mutant antithrombin-Hamilton has high stability to denaturation characteristic of wild type inhibitor serpins
    • Wright HT, Blajchman MA. Proteolytically cleaved mutant antithrombin-Hamilton has high stability to denaturation characteristic of wild type inhibitor serpins. FEBS Lett 1994; 348: 14-16.
    • (1994) FEBS Lett , vol.348 , pp. 14-16
    • Wright, H.T.1    Blajchman, M.A.2
  • 40
    • 0028937232 scopus 로고
    • Conformational studies on plasminogen activator inhibitor-1 (PAI-1) in active, latent, substrate, and cleaved forms
    • Sancho E, Declerck PJ, Price NC, Kelly SM, Booth NA. Conformational studies on plasminogen activator inhibitor-1 (PAI-1) in active, latent, substrate, and cleaved forms. Biochemistry 1995; 34: 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
  • 41
    • 0030983024 scopus 로고    scopus 로고
    • Rational design of complex formation between plasminogen activator inhibitor-1 and its target proteinases
    • Aertgeerts K, De Ranter CJ, Booth NA, Declerck PJ. Rational design of complex formation between plasminogen activator inhibitor-1 and its target proteinases. J Struct Biol 1997; 118: 236-242.
    • (1997) J Struct Biol , vol.118 , pp. 236-242
    • Aertgeerts, K.1    De Ranter, C.J.2    Booth, N.A.3    Declerck, P.J.4
  • 42
    • 0031036673 scopus 로고    scopus 로고
    • Major proteinase movement upon stable serpin-proteinase complex formation
    • Stratikos E, Gettins PGW. Major proteinase movement upon stable serpin-proteinase complex formation. Proc Natl Acad Sci USA 1997; 94: 453-458.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 453-458
    • Stratikos, E.1    Gettins, P.G.W.2
  • 44
    • 0029992894 scopus 로고    scopus 로고
    • Distortion of the active site loop of chymotrypsin complexed with a serpin
    • Plotnick MI, Mayne L, Schechter NM, Rubin H. Distortion of the active site loop of chymotrypsin complexed with a serpin. Biochemistry 1996; 35: 7586-7590.
    • (1996) Biochemistry , vol.35 , pp. 7586-7590
    • Plotnick, M.I.1    Mayne, L.2    Schechter, N.M.3    Rubin, H.4
  • 45
    • 0027633477 scopus 로고
    • The role of conformational change in serpin structure and function
    • Gettins P, Patston PA, Schapira M. The role of conformational change in serpin structure and function. Bioessays 1993; 15: 461-467.
    • (1993) Bioessays , vol.15 , pp. 461-467
    • Gettins, P.1    Patston, P.A.2    Schapira, M.3
  • 46
    • 0028168253 scopus 로고
    • Alpha 1-proteinase inhibitor variant T345R. Influence of P14 residue on substrate and inhibitory pathways
    • Hood DB, Huntington JA, Gettins PGW. Alpha 1-proteinase inhibitor variant T345R. Influence of P14 residue on substrate and inhibitory pathways. Biochemistry 1994; 33: 8538-8547.
    • (1994) Biochemistry , vol.33 , pp. 8538-8547
    • Hood, D.B.1    Huntington, J.A.2    Gettins, P.G.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.