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Volumn 61, Issue 4, 2005, Pages 870-877

Mutagenesis at Pro309 of single-chain urokinase-type plasminogen activator alters its catalytic properties

Author keywords

Amidolytic activity; Cassette mutagenesis; Fibrin fragment D dimer; Fibrin fragment E; Plasminogen activation; Secondary site(s) of substrate interaction; Substrate specificity

Indexed keywords

AMINO ACID; COMPLEMENTARY DNA; D DIMER; FIBRIN DEGRADATION PRODUCT; FIBRIN FRAGMENT E; PLASMINOGEN ACTIVATOR; PROLINE; PROUROKINASE; UNCLASSIFIED DRUG; PEPTIDE FRAGMENT; PLASMINOGEN; PRIMER DNA; RECOMBINANT PROTEIN; UROKINASE;

EID: 28644441521     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20686     Document Type: Article
Times cited : (3)

References (35)
  • 2
    • 0029827894 scopus 로고    scopus 로고
    • Targeted gene manipulation and transfer of the plasminogen and coagulation systems in mice
    • Carmeliet P, Collen D. Targeted gene manipulation and transfer of the plasminogen and coagulation systems in mice. Fibrinolysis 1996;10:195-213.
    • (1996) Fibrinolysis , vol.10 , pp. 195-213
    • Carmeliet, P.1    Collen, D.2
  • 3
    • 0023784931 scopus 로고
    • One-chain urokinase-type plasminogen activator from human sarcoma cells is a proenzyme with little or no intrinsic activity
    • Petersen LC, Lund LR, Dano K, Nielsen LS, Skriver L. One-chain urokinase-type plasminogen activator from human sarcoma cells is a proenzyme with little or no intrinsic activity. J Biol Chem 1988;263:11189-11195.
    • (1988) J Biol Chem , vol.263 , pp. 11189-11195
    • Petersen, L.C.1    Lund, L.R.2    Dano, K.3    Nielsen, L.S.4    Skriver, L.5
  • 4
    • 0027475969 scopus 로고
    • The kinetics of plasminogen activation by thrombin-cleaved pro-urokinase and promotion of its activity by fibrin fragment E-2 and by tissue plasminogen activator
    • Liu J, Gurewich V. The kinetics of plasminogen activation by thrombin-cleaved pro-urokinase and promotion of its activity by fibrin fragment E-2 and by tissue plasminogen activator. Blood 1993;81:980-987.
    • (1993) Blood , vol.81 , pp. 980-987
    • Liu, J.1    Gurewich, V.2
  • 5
    • 0025262153 scopus 로고
    • Plasminogen activation with single-chain urokinase-type plasminogen activator (scu-PA). Studies with active site mutagenized plasminogen (Ser740→ Ala) and plasmin-resistant scu-PA (Lys158→ Glu)
    • Lijnen HR, Van Hoef B, Nelles L, Collen D. Plasminogen activation with single-chain urokinase-type plasminogen activator (scu-PA). Studies with active site mutagenized plasminogen (Ser740→ Ala) and plasmin-resistant scu-PA (Lys158→ Glu). J Biol Chem 1990;265:5232-5236.
    • (1990) J Biol Chem , vol.265 , pp. 5232-5236
    • Lijnen, H.R.1    Van Hoef, B.2    Nelles, L.3    Collen, D.4
  • 6
    • 0024268751 scopus 로고
    • Characterization of the intrinsic fibrinolytic properties of pro-urokinase through a study of plasmin-resistant mutant forms produced by site-specific mutagenesis of lysine(158)
    • Gurewich V, Pannell R, Broeze RJ, and Mao J. Characterization of the intrinsic fibrinolytic properties of pro-urokinase through a study of plasmin-resistant mutant forms produced by site-specific mutagenesis of lysine(158). J Clin Invest 1988;82:1956-1962.
    • (1988) J Clin Invest , vol.82 , pp. 1956-1962
    • Gurewich, V.1    Pannell, R.2    Broeze, R.J.3    Mao, J.4
  • 7
    • 0023101988 scopus 로고
    • Functional role of proteolytic cleavage at arginine-275 of human tissue plasminogen activator as assessed by site-directed mutagenesis
    • Tate KM, Higgins DL, Holmes WE, Winkler ME, Heyneker HL, Vehar GA. Functional role of proteolytic cleavage at arginine-275 of human tissue plasminogen activator as assessed by site-directed mutagenesis. Biochemistry 1987;26:338-343.
    • (1987) Biochemistry , vol.26 , pp. 338-343
    • Tate, K.M.1    Higgins, D.L.2    Holmes, W.E.3    Winkler, M.E.4    Heyneker, H.L.5    Vehar, G.A.6
  • 8
    • 0028804819 scopus 로고
    • Variants of tissue-type plasminogen activator with substantially enhanced response and selectivity toward fibrin co-factors
    • Strandberg L, Medison EL. Variants of tissue-type plasminogen activator with substantially enhanced response and selectivity toward fibrin co-factors. J Biol Chem 1995;270:23444-23449.
    • (1995) J Biol Chem , vol.270 , pp. 23444-23449
    • Strandberg, L.1    Medison, E.L.2
  • 9
    • 0025248410 scopus 로고
    • Quenching of the amidolytic activity of one-chain tissue-type plasminogen activator by mutation of lysine-416
    • Petersen LC, Boel E, Johannessen M, Foster D. Quenching of the amidolytic activity of one-chain tissue-type plasminogen activator by mutation of lysine-416. Biochemistry 1990;29:3451-3457.
    • (1990) Biochemistry , vol.29 , pp. 3451-3457
    • Petersen, L.C.1    Boel, E.2    Johannessen, M.3    Foster, D.4
  • 10
    • 0031036522 scopus 로고    scopus 로고
    • Converting tissue type plasminogen activator into a zymogen. Important role of Lys156
    • Tachias K, Madison EL. Converting tissue type plasminogen activator into a zymogen. Important role of Lys156. J Biol Chem 1997;272:28-31.
    • (1997) J Biol Chem , vol.272 , pp. 28-31
    • Tachias, K.1    Madison, E.L.2
  • 11
    • 0029665065 scopus 로고    scopus 로고
    • The 2.3 a crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator
    • Lamba D, Bauer M, Huber R, Fischer S, Rudolph R, Kohnert U, Bode W. The 2.3 A crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator. J Mol Biol 1996;258:117-135.
    • (1996) J Mol Biol , vol.258 , pp. 117-135
    • Lamba, D.1    Bauer, M.2    Huber, R.3    Fischer, S.4    Rudolph, R.5    Kohnert, U.6    Bode, W.7
  • 12
    • 0029825436 scopus 로고    scopus 로고
    • A site-directed mutagenesis of pro-urokinase which substantially reduces its intrinsic activity
    • Liu J, Tang W, Sun Z, Kung W, Pannell R, Sarmientos P, Gurewich V. A site-directed mutagenesis of pro-urokinase which substantially reduces its intrinsic activity. Biochemistry 1996;35:14070-14076.
    • (1996) Biochemistry , vol.35 , pp. 14070-14076
    • Liu, J.1    Tang, W.2    Sun, Z.3    Kung, W.4    Pannell, R.5    Sarmientos, P.6    Gurewich, V.7
  • 13
    • 0027496219 scopus 로고
    • Converting tissue plasminogen activator to a zymogen: A regulatory triad of Asp-His-Ser
    • Madison EL, Kobe A, Gething M, Sambrook JF, Goldsmith EJ. Converting tissue plasminogen activator to a zymogen: a regulatory triad of Asp-His-Ser. Science 1993;262:419-421.
    • (1993) Science , vol.262 , pp. 419-421
    • Madison, E.L.1    Kobe, A.2    Gething, M.3    Sambrook, J.F.4    Goldsmith, E.J.5
  • 14
    • 0022481025 scopus 로고
    • Pro-urokinase: A study of its stability in plasma and of a mechanism for its selective fibrinolytic effect
    • Pannell R, Gurewich V. Pro-urokinase: a study of its stability in plasma and of a mechanism for its selective fibrinolytic effect. Blood 1986;67:1215-1223.
    • (1986) Blood , vol.67 , pp. 1215-1223
    • Pannell, R.1    Gurewich, V.2
  • 15
    • 0020471109 scopus 로고
    • Fibrinolytic properties of one-chain and two-chain human extrinsic (tissue-type) plasminogen activator
    • Rijken DC, Hoylaerts M, Collen D. Fibrinolytic properties of one-chain and two-chain human extrinsic (tissue-type) plasminogen activator. J Biol Chem 1982;257:2920-2925.
    • (1982) J Biol Chem , vol.257 , pp. 2920-2925
    • Rijken, D.C.1    Hoylaerts, M.2    Collen, D.3
  • 16
    • 0020472522 scopus 로고
    • Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin
    • Hoylaerts M, Rijken DC, Lijnen HR, Collen D. Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin. J Biol Chem 1982;257:2912-2919.
    • (1982) J Biol Chem , vol.257 , pp. 2912-2919
    • Hoylaerts, M.1    Rijken, D.C.2    Lijnen, H.R.3    Collen, D.4
  • 17
    • 0019987224 scopus 로고
    • Studies on the kinetics of plasminogen activation by tissue plasminogen activator
    • Ranby M. Studies on the kinetics of plasminogen activation by tissue plasminogen activator. Biochim Biophy Acta 1982;704:461-469.
    • (1982) Biochim Biophy Acta , vol.704 , pp. 461-469
    • Ranby, M.1
  • 18
    • 8044258036 scopus 로고
    • The fibrin specificity of single chain-urokinase (sc-UK) induced proteolysis is not dependent on fibrin binding
    • Gurewich V, Pannell R. The fibrin specificity of single chain-urokinase (sc-UK) induced proteolysis is not dependent on fibrin binding. Thromb Haemost 1983;50:386.
    • (1983) Thromb Haemost , vol.50 , pp. 386
    • Gurewich, V.1    Pannell, R.2
  • 19
    • 28644439133 scopus 로고
    • Pro-urokinase (Pro-UK), the single-chain urokinase-type plasminogen activator (scu-PA) does not bind to fibrin. Isotopic and spectrophotometric studies using fibrin in solid-phase
    • Angles-Cano E, Pannell R, Gurewich V. Pro-urokinase (Pro-UK), the single-chain urokinase-type plasminogen activator (scu-PA) does not bind to fibrin. Isotopic and spectrophotometric studies using fibrin in solid-phase. Blood 1986;(Suppl 1):343.
    • (1986) Blood , Issue.SUPPL. 1 , pp. 343
    • Angles-Cano, E.1    Pannell, R.2    Gurewich, V.3
  • 20
    • 0026334980 scopus 로고
    • A comparative study of the promotion of tissue plasminogen activator and pro-urokinase-induced plasminogen activation by fragments D and E-2 of fibrin
    • Liu J, Gurewich V. A comparative study of the promotion of tissue plasminogen activator and pro-urokinase-induced plasminogen activation by fragments D and E-2 of fibrin. J Clin Invest 1991;88:2012-2017.
    • (1991) J Clin Invest , vol.88 , pp. 2012-2017
    • Liu, J.1    Gurewich, V.2
  • 21
    • 0014965504 scopus 로고
    • Three-dimensional structure of tosylelastase
    • Shotton DM, Watson HC. Three-dimensional structure of tosylelastase. Nature 1970;225:811-816.
    • (1970) Nature , vol.225 , pp. 811-816
    • Shotton, D.M.1    Watson, H.C.2
  • 22
    • 0015946772 scopus 로고
    • The structure of bovine trypsin: Electron density maps of the inhibited enzyme at 5 Angstrom and at 2-7 Angstron resolution
    • Stroud RM, Kay LM., Dickerson RE. The structure of bovine trypsin: electron density maps of the inhibited enzyme at 5 Angstrom and at 2-7 Angstron resolution. J Mol Biol 1974;83:185-208.
    • (1974) J Mol Biol , vol.83 , pp. 185-208
    • Stroud, R.M.1    Kay, L.M.2    Dickerson, R.E.3
  • 23
    • 0031026330 scopus 로고    scopus 로고
    • Identification of a hydrophobic exosite on tissue type plasminogen activator that modulates specificity for plasminogen
    • Ke S, Tachias K, Lamba D, Bode W, Madison EL. Identification of a hydrophobic exosite on tissue type plasminogen activator that modulates specificity for plasminogen. J Biol Chem 1997;272:1811-1816.
    • (1997) J Biol Chem , vol.272 , pp. 1811-1816
    • Ke, S.1    Tachias, K.2    Lamba, D.3    Bode, W.4    Madison, E.L.5
  • 24
    • 0034629461 scopus 로고    scopus 로고
    • Re-engineering of human urokinase provides a system for structure-based drug design at high resolution and reveals a novel structural subsite
    • Nienaber V, Wang J, Davidson D, Henkin J. Re-engineering of human urokinase provides a system for structure-based drug design at high resolution and reveals a novel structural subsite. J Biol Chem 2000;275:7239-7248.
    • (2000) J Biol Chem , vol.275 , pp. 7239-7248
    • Nienaber, V.1    Wang, J.2    Davidson, D.3    Henkin, J.4
  • 25
    • 0034636986 scopus 로고    scopus 로고
    • Crystals of the urokinase type plasminogen activator variant beta(c)-uPAin complex with small molecule inhibitors open the way towards structure-based drug design
    • Zeslawska E, Schweinitz A, Karcher A, Sondermann P, Sperl S, Sturzebecher J, Jacob U. Crystals of the urokinase type plasminogen activator variant beta(c)-uPAin complex with small molecule inhibitors open the way towards structure-based drug design. J Mol Biol 2000;301:465-475.
    • (2000) J Mol Biol , vol.301 , pp. 465-475
    • Zeslawska, E.1    Schweinitz, A.2    Karcher, A.3    Sondermann, P.4    Sperl, S.5    Sturzebecher, J.6    Jacob, U.7
  • 26
    • 0037453226 scopus 로고    scopus 로고
    • Crystals of urokinase type plasminogen activator complexes reveal the binding mode of peptidomimetic inhibitors
    • Zeslawska E, Jacob U, Schweinitz A, Coombs G, Bode W, Madison E. Crystals of urokinase type plasminogen activator complexes reveal the binding mode of peptidomimetic inhibitors. J Mol Biol 2003;328:109-118.
    • (2003) J Mol Biol , vol.328 , pp. 109-118
    • Zeslawska, E.1    Jacob, U.2    Schweinitz, A.3    Coombs, G.4    Bode, W.5    Madison, E.6
  • 27
    • 0030861952 scopus 로고    scopus 로고
    • Identification of a flexible loop region (297-313) of urokinase-type plasminogen activator, which helps determine its catalytic activity
    • Sun Z, Jiang Y, Ma Z, Wu H, Liu B, Xu Y, Tang W, Chen Y, Li C, Zhu D, Gurewich V, Liu J. Identification of a flexible loop region (297-313) of urokinase-type plasminogen activator, which helps determine its catalytic activity. J Biol Chem 1997;272:23818-23823.
    • (1997) J Biol Chem , vol.272 , pp. 23818-23823
    • Sun, Z.1    Jiang, Y.2    Ma, Z.3    Wu, H.4    Liu, B.5    Xu, Y.6    Tang, W.7    Chen, Y.8    Li, C.9    Zhu, D.10    Gurewich, V.11    Liu, J.12
  • 28
    • 0030878999 scopus 로고    scopus 로고
    • Optimal subsite occupancy and design of a selective inhibitor of urokinase
    • Ke S, Coombs GS, Tachias K, Corey DR, Madison EL. Optimal subsite occupancy and design of a selective inhibitor of urokinase. J Biol Chem 1997;272:20456-20462.
    • (1997) J Biol Chem , vol.272 , pp. 20456-20462
    • Ke, S.1    Coombs, G.S.2    Tachias, K.3    Corey, D.R.4    Madison, E.L.5
  • 30
    • 0032478193 scopus 로고    scopus 로고
    • Analysis of the forces which stabilize the active conformation of urokinase-type plasminogen activator
    • Sun Z, Liu B, Chen Y, Gurewich V, Zhu D, Liu J. Analysis of the forces which stabilize the active conformation of urokinase-type plasminogen activator. Biochemistry 1998;37:2935-2940.
    • (1998) Biochemistry , vol.37 , pp. 2935-2940
    • Sun, Z.1    Liu, B.2    Chen, Y.3    Gurewich, V.4    Zhu, D.5    Liu, J.6
  • 31
    • 0022531818 scopus 로고
    • Purification and characterization of recombinant single-chain urokinase produced in Escherichia coli
    • Winkler ME, Blaber M. Purification and characterization of recombinant single-chain urokinase produced in Escherichia coli. Biochemistry 1986;25:4041-4045.
    • (1986) Biochemistry , vol.25 , pp. 4041-4045
    • Winkler, M.E.1    Blaber, M.2
  • 34
    • 0942298106 scopus 로고    scopus 로고
    • The elusive role of the potential factor X cation-binding exosite-1 in substrate and inhibitor interactions
    • Bianchini EP, Pike RN, Le Bonniec BF. The elusive role of the potential factor X cation-binding exosite-1 in substrate and inhibitor interactions. J Biol Chem 2004;279:3671-3679.
    • (2004) J Biol Chem , vol.279 , pp. 3671-3679
    • Bianchini, E.P.1    Pike, R.N.2    Le Bonniec, B.F.3
  • 35
    • 0035805579 scopus 로고    scopus 로고
    • Heparin enhances the specificity of antithrombin for thrombin and factor Xa independent of the reactive center loop sequence. Evidence for an exosite determinant of factor Xa specificity in heparin-activated antithrombin
    • Chuang Y, Swanson R, Raja SM, Olson ST. Heparin enhances the specificity of antithrombin for thrombin and factor Xa independent of the reactive center loop sequence. Evidence for an exosite determinant of factor Xa specificity in heparin-activated antithrombin. J Biol Chem 2001;276:14961-14971.
    • (2001) J Biol Chem , vol.276 , pp. 14961-14971
    • Chuang, Y.1    Swanson, R.2    Raja, S.M.3    Olson, S.T.4


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