메뉴 건너뛰기




Volumn 48, Issue 22, 2005, Pages 6908-6917

Selective inhibitors of the serine protease plasmin: Probing the S3 and S3′ subsites using a combinatorial library

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOHEXANONE DERIVATIVE; KALLIKREIN; PLASMIN; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; THROMBIN; TRYPSIN;

EID: 27444439184     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm050488k     Document Type: Article
Times cited : (21)

References (46)
  • 1
    • 0034628448 scopus 로고    scopus 로고
    • Protease inhibitors: Current status and future prospects
    • Leung, D.; Abbenante, G.; Fairlie, D. P. Protease Inhibitors: Current Status and Future Prospects. J. Med. Chem. 2000, 43, 305-341.
    • (2000) J. Med. Chem. , vol.43 , pp. 305-341
    • Leung, D.1    Abbenante, G.2    Fairlie, D.P.3
  • 2
    • 0029943568 scopus 로고    scopus 로고
    • Plasminogen activators and matrix metalloproteinases in angiogenesis
    • Mignatti, P.; Rifkin, D. B. Plasminogen Activators and Matrix Metalloproteinases in Angiogenesis. Enzyme Protein 1996, 49, 117-137.
    • (1996) Enzyme Protein , vol.49 , pp. 117-137
    • Mignatti, P.1    Rifkin, D.B.2
  • 4
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht, M. D.; Werb, Z. How Matrix Metalloproteinases Regulate Cell Behavior. Annu. Rev. Cell Dev. Biol. 2001, 17, 463-516.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 5
  • 6
    • 0014967219 scopus 로고
    • Plasminogen-plasmin system. VI. Preparation of alpha 2-macroglobulin antiplasmin from human plasma
    • Iwamoto, M.; Abiko, Y. Plasminogen-Plasmin System. VI. Preparation of Alpha 2-Macroglobulin Antiplasmin from Human Plasma. Biochim. Biophys. Acta 1970, 214, 402-410.
    • (1970) Biochim. Biophys. Acta , vol.214 , pp. 402-410
    • Iwamoto, M.1    Abiko, Y.2
  • 7
    • 0017102105 scopus 로고
    • Isolation and characterization of alpha2-plamsin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis
    • Moroi, M.; Aoki, N. Isolation and Characterization of Alpha2-Plamsin Inhibitor from Human Plasma. A Novel Proteinase Inhibitor which Inhibits Activator-Induced Clot Lysis. J. Biol. Chem. 1976, 251, 5956-5965.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5956-5965
    • Moroi, M.1    Aoki, N.2
  • 8
    • 0021228829 scopus 로고
    • The role of hemostasis and fibrinolysis in the metastatic spread of cancer
    • Markus, G. The Role of Hemostasis and Fibrinolysis in the Metastatic Spread of Cancer. Semin. Thromb. Hemostasis 1984, 10, 61-70.
    • (1984) Semin. Thromb. Hemostasis , vol.10 , pp. 61-70
    • Markus, G.1
  • 9
    • 0033981473 scopus 로고    scopus 로고
    • The plasminogen activation system in tumor growth, invasion, and metastasis
    • Andreasen, P. A.; Egelund, R.; Petersen, H. H. The Plasminogen Activation System in Tumor Growth, Invasion, and Metastasis. Cell Mol. Life Sci. 2000, 20, 25-40.
    • (2000) Cell Mol. Life Sci. , vol.20 , pp. 25-40
    • Andreasen, P.A.1    Egelund, R.2    Petersen, H.H.3
  • 10
    • 85008120698 scopus 로고
    • Plasmin and antiplasmin-their pathologic physiology
    • Okamoto, S. Plasmin and Antiplasmin-their Pathologic Physiology. Keio J. Med. 1959, 8, 211-217.
    • (1959) Keio J. Med. , vol.8 , pp. 211-217
    • Okamoto, S.1
  • 11
    • 0000518408 scopus 로고
    • An active stereoisomer (trans-form) of amcha and its antifibrinolytic (antiplasminic) action in vitro and in vivo
    • Okamoto, S.; Sato, S.; Tanaka, Y.; Okamoto, U. An Active Stereoisomer (Trans-Form) of Amcha and its Antifibrinolytic (Antiplasminic) Action in Vitro and in Vivo. Keio J. Med. 1964, 13, 177-185.
    • (1964) Keio J. Med. , vol.13 , pp. 177-185
    • Okamoto, S.1    Sato, S.2    Tanaka, Y.3    Okamoto, U.4
  • 12
    • 0016770029 scopus 로고
    • Plasminogen-plasmin system IX. Specific binding of tranexamic acid to plasmin
    • Iwamoto, M. Plasminogen-Plasmin System IX. Specific Binding of Tranexamic Acid to Plasmin. Thrombos. Diathes. Haemorrh. 1975, 33, 573-585.
    • (1975) Thrombos. Diathes. Haemorrh. , vol.33 , pp. 573-585
    • Iwamoto, M.1
  • 16
    • 0034531728 scopus 로고    scopus 로고
    • Development of potent and selective plasmin and plasma Kallikrein inhibitors and studies on the structure-activity relationship
    • Okada, Y.; Tsuda, Y.; Tada, M.; Wanaka, K.; Okamoto, U.; Hijikata-Okunomiya, A.; Okamoto, S. Development of Potent and Selective Plasmin and Plasma Kallikrein Inhibitors and Studies on the Structure-Activity Relationship. Chem. Pharm. Bull. 2000, 48, 1964-1972.
    • (2000) Chem. Pharm. Bull. , vol.48 , pp. 1964-1972
    • Okada, Y.1    Tsuda, Y.2    Tada, M.3    Wanaka, K.4    Okamoto, U.5    Hijikata-Okunomiya, A.6    Okamoto, S.7
  • 20
    • 0036537369 scopus 로고    scopus 로고
    • A selective plasmin inhibitor, trans-aminomethylcyclohexanecarbonyl-L-(O- picolyl)tyrosine-octylamide (YO-2), induces thymocyte apoptosis
    • Lee, E.; Enomoto, R.; Takemura, K.; Tsuda, Y.; Okada, Y. A Selective Plasmin Inhibitor, Trans-Aminomethylcyclohexanecarbonyl-L-(O-Picolyl)Tyrosine- Octylamide (YO-2), Induces Thymocyte Apoptosis. Biochem. Pharmacol. 2002, 63, 1315-1323.
    • (2002) Biochem. Pharmacol. , vol.63 , pp. 1315-1323
    • Lee, E.1    Enomoto, R.2    Takemura, K.3    Tsuda, Y.4    Okada, Y.5
  • 22
    • 0030909327 scopus 로고    scopus 로고
    • Using the electrostatic field effect to design a new class of inhibitors for cysteine proteases
    • Conroy, J. L.; Sanders, T. C.; Seto, C. T. Using the Electrostatic Field Effect to Design a New Class of Inhibitors for Cysteine Proteases. J. Am. Chem. Soc. 1997, 119, 4285-4291.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 4285-4291
    • Conroy, J.L.1    Sanders, T.C.2    Seto, C.T.3
  • 23
    • 0033614992 scopus 로고    scopus 로고
    • 4-Heterocyclohexanone-based inhibitors of the serine protease plasmin
    • Sanders, T. C.; Seto, C. T. 4-Heterocyclohexanone-Based Inhibitors of the Serine Protease Plasmin. J. Med. Chem. 1999, 42, 2969-2976.
    • (1999) J. Med. Chem. , vol.42 , pp. 2969-2976
    • Sanders, T.C.1    Seto, C.T.2
  • 24
    • 0037154811 scopus 로고    scopus 로고
    • Inhibitors of plasmin that extend into both the S and S′ binding sites: Cooperative interactions between S1 and S2
    • Abato, P.; Yuen, C. M.; Cubanski, J. Y.; Seto, C. T. Inhibitors of Plasmin that Extend into Both the S and S′ Binding Sites: Cooperative Interactions between S1 and S2. J. Org. Chem. 2002, 67, 1184-1191.
    • (2002) J. Org. Chem. , vol.67 , pp. 1184-1191
    • Abato, P.1    Yuen, C.M.2    Cubanski, J.Y.3    Seto, C.T.4
  • 25
    • 0032478745 scopus 로고    scopus 로고
    • 13C NMR studies that tetrahydropyranone-based inhibitors bind to cysteine proteases by reversible formation of a hemithioketal adduct
    • 13C NMR Studies that Tetrahydropyranone-Based Inhibitors Bind to Cysteine Proteases by Reversible Formation of a Hemithioketal Adduct. J. Org. Chem. 1998, 63, 2367-2370.
    • (1998) J. Org. Chem. , vol.63 , pp. 2367-2370
    • Conroy, J.L.1    Seto, C.T.2
  • 26
    • 0033598321 scopus 로고    scopus 로고
    • Combinatorial library of serine and cysteine protease inhibitors that interact with both the S and S′ binding sites
    • Abato, P.; Conroy, J. L.; Seto, C. T. Combinatorial Library of Serine and Cysteine Protease Inhibitors that Interact with Both the S and S′ Binding Sites. J. Med. Chem. 1999, 42, 4001-4009.
    • (1999) J. Med. Chem. , vol.42 , pp. 4001-4009
    • Abato, P.1    Conroy, J.L.2    Seto, C.T.3
  • 27
    • 0032487772 scopus 로고    scopus 로고
    • Synthesis of cyclohexanone-based cathepsin B inhibitors that interact with both the S and S′ binding sites
    • Conroy, J. L.; Abato, P.; Ghosh, M.; Austermuhle, M. I.; Kiefer, M. R.; Seto, C. T. Synthesis of Cyclohexanone-Based Cathepsin B Inhibitors that Interact with Both the S and S′ Binding Sites. Tetrahedron Lett. 1998, 39, 8253-8256.
    • (1998) Tetrahedron Lett. , vol.39 , pp. 8253-8256
    • Conroy, J.L.1    Abato, P.2    Ghosh, M.3    Austermuhle, M.I.4    Kiefer, M.R.5    Seto, C.T.6
  • 28
    • 0025893762 scopus 로고
    • General method for rapid synthesis of multicomponent peptide mixtures
    • (a) Furka, A.; Sebestyen, F.; Asgedom, M.; Dibo, G. General Method for Rapid Synthesis of Multicomponent Peptide Mixtures. Int. J. Pept. Protein Res. 1991, 37, 487-493.
    • (1991) Int. J. Pept. Protein Res. , vol.37 , pp. 487-493
    • Furka, A.1    Sebestyen, F.2    Asgedom, M.3    Dibo, G.4
  • 29
    • 0026419328 scopus 로고
    • A new type of synthetic peptide library for identifying ligand-binding activity
    • (b) Lam, K. S.; Salmon, S. E.; Hersh, E. M.; Hruby, V. J.; Kazmierski, W. M.; Knapp, R. J. A New Type of Synthetic Peptide Library for Identifying Ligand-Binding Activity. Nature 1991, 354, 82-84.
    • (1991) Nature , vol.354 , pp. 82-84
    • Lam, K.S.1    Salmon, S.E.2    Hersh, E.M.3    Hruby, V.J.4    Kazmierski, W.M.5    Knapp, R.J.6
  • 30
    • 0026419319 scopus 로고
    • Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery
    • (c) Houghten, R. A.; Pinilla, C.; Blondelle, S. E.; Appel, J. R.; Dooley, C. T.; Cuervo, J. H. Generation and Use of Synthetic Peptide Combinatorial Libraries for Basic Research and Drug Discovery. Nature, 1991, 354, 84-86.
    • (1991) Nature , vol.354 , pp. 84-86
    • Houghten, R.A.1    Pinilla, C.2    Blondelle, S.E.3    Appel, J.R.4    Dooley, C.T.5    Cuervo, J.H.6
  • 31
    • 0029076548 scopus 로고
    • A transition state analogue inhibitor combinatorial library
    • For other libraries that were constructed for screening against proteases, see: (a) Campbell, D. A.; Bermak, J. C.; Burkoth, T. S.; Patel, D. V. A Transition State Analogue Inhibitor Combinatorial Library. J. Am. Chem. Soc. 1995, 117, 5381-5382.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5381-5382
    • Campbell, D.A.1    Bermak, J.C.2    Burkoth, T.S.3    Patel, D.V.4
  • 32
    • 0026345157 scopus 로고
    • The rapid identification of HIV protease inhibitors through the synthesis and screening of defined peptide mixtures
    • (b) Owens, R. A.; Gesellchen, P. D.; Houchins, B. J.; DiMarchi, R. D. The Rapid Identification of HIV Protease Inhibitors through the Synthesis and Screening of Defined Peptide Mixtures. Biochem. Biophys. Res. Commun. 1991, 181, 402-408.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 402-408
    • Owens, R.A.1    Gesellchen, P.D.2    Houchins, B.J.3    Dimarchi, R.D.4
  • 33
    • 0028968619 scopus 로고
    • Expedient method for the solid-phase synthesis of aspartic protease inhibitors directed toward the generation of libraries
    • (c) Kick, E. K.; Ellman, J. A. Expedient Method for the Solid-Phase Synthesis of Aspartic Protease Inhibitors Directed Toward the Generation of Libraries. J. Med. Chem. 1995, 38, 1427-1430.
    • (1995) J. Med. Chem. , vol.38 , pp. 1427-1430
    • Kick, E.K.1    Ellman, J.A.2
  • 34
    • 0029092629 scopus 로고
    • Synthetic chemical diversity: Solid-phase synthesis of libraries of C2 symmetric inhibitors of HIV protease containing diamino diol and diamino alcohol cores
    • (d) Wang, J. T.; Li, S.; Wideburg, N.; Krafft, G. A.; Kempf, D. J. Synthetic Chemical Diversity: Solid-Phase Synthesis of Libraries of C2 Symmetric Inhibitors of HIV Protease Containing Diamino Diol and Diamino Alcohol Cores. J. Med. Chem. 1995, 38, 2995-3002.
    • (1995) J. Med. Chem. , vol.38 , pp. 2995-3002
    • Wang, J.T.1    Li, S.2    Wideburg, N.3    Krafft, G.A.4    Kempf, D.J.5
  • 36
    • 0023114779 scopus 로고
    • Effects of secondary interactions on the kinetics of peptide and peptide ester Hydrolysis by tissue kallikrein and trypsin
    • (a) Fiedler, F. Effects of Secondary Interactions on the Kinetics of Peptide and Peptide Ester Hydrolysis by Tissue Kallikrein and Trypsin. Eur. J. Biochem. 1987, 163, 303-312.
    • (1987) Eur. J. Biochem. , vol.163 , pp. 303-312
    • Fiedler, F.1
  • 37
    • 0023910977 scopus 로고
    • Horse urinary kallikrein, II. Effect of subsite interactions on its catalytic activity
    • (b) Araujo-Viel, M. S.; Juliano, M. A.; Oliveira, L.; Prado, E. S. Horse Urinary Kallikrein, II. Effect of Subsite Interactions on Its Catalytic Activity. Biol. Chem. Hoppe-Seyler 1988, 369, 397-401.
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 397-401
    • Araujo-Viel, M.S.1    Juliano, M.A.2    Oliveira, L.3    Prado, E.S.4
  • 38
    • 0033561266 scopus 로고    scopus 로고
    • Specificity of human tissue kallikrein towards substrates containing phe-phe pair of amino acids
    • Pimenta, D. C.; Chao, J.; Chao, L.; Juliano, M. A.; Juliano, L. Specificity of Human Tissue Kallikrein towards Substrates Containing Phe-Phe Pair of Amino Acids. Biochem. J. 1999, 339, 473-479.
    • (1999) Biochem. J. , vol.339 , pp. 473-479
    • Pimenta, D.C.1    Chao, J.2    Chao, L.3    Juliano, M.A.4    Juliano, L.5
  • 39
    • 0034087855 scopus 로고    scopus 로고
    • Negative selectivity and the evolution of protease cascades: The specificity of plasmin for peptide and protein substrates
    • (a) Hervio, L. S.; Coombs, G. S.; Bergstrom, R. C.; Trivedi, K.; Corey, D. R.; Madison, E. L. Negative Selectivity and the Evolution of Protease Cascades: The Specificity of Plasmin for Peptide and Protein Substrates. Chem. Biol. 2000, 7, 443-452.
    • (2000) Chem. Biol. , vol.7 , pp. 443-452
    • Hervio, L.S.1    Coombs, G.S.2    Bergstrom, R.C.3    Trivedi, K.4    Corey, D.R.5    Madison, E.L.6
  • 40
    • 0034608931 scopus 로고    scopus 로고
    • Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries
    • (b) Harris, J. L.; Backes, B. J.; Leonetti, F.; Mahrus, S.; Ellman, J. A.; Craik, C. S. Rapid and General Profiling of Protease Specificity by Using Combinatorial Fluorogenic Substrate Libraries. Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 7754-7759.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 7754-7759
    • Harris, J.L.1    Backes, B.J.2    Leonetti, F.3    Mahrus, S.4    Ellman, J.A.5    Craik, C.S.6
  • 41
    • 0033951198 scopus 로고    scopus 로고
    • Synthesis of positional-scanning libraries of fluorogenic peptide substrates to define the extended substrate specificity of plasmin and thrombin
    • (c) Backes, B. J.; Harris, J. L.; Leonetti, F.; Craik, C. S.; Ellman, J. A. Synthesis of Positional-Scanning Libraries of Fluorogenic Peptide Substrates to Define the Extended Substrate Specificity of Plasmin and Thrombin. Nat. Biotechnol. 2000, 18, 187-193.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 187-193
    • Backes, B.J.1    Harris, J.L.2    Leonetti, F.3    Craik, C.S.4    Ellman, J.A.5
  • 45
    • 0028201374 scopus 로고
    • Role of the S′ subsites in serine protease catalysis. Active-site mapping of rat chymotrypsin, rat trypsin, α-lytic protease, and cercarial protease from Schistosoma mansoni
    • Schellenberger, V.; Turck, C. W.; Rutter, W. J. Role of the S′ Subsites in Serine Protease Catalysis. Active-Site Mapping of Rat Chymotrypsin, Rat Trypsin, α-Lytic Protease, and Cercarial Protease from Schistosoma mansoni. Biochemistry 1994, 33, 4251-4257.
    • (1994) Biochemistry , vol.33 , pp. 4251-4257
    • Schellenberger, V.1    Turck, C.W.2    Rutter, W.J.3
  • 46
    • 1842635744 scopus 로고    scopus 로고
    • Evaluation of phage display system and leech-derived tryptase inhibitor as a tool for understanding the serine proteinase specificities
    • Campos, I. T.; Silva, M. M.; Azzolini, S. S.; Souza, A. F.; Sampaio, C. A. M.; Fritz, H.; Tanaka, A. S. Evaluation of Phage Display System and Leech-Derived Tryptase Inhibitor as a Tool for Understanding the Serine Proteinase Specificities. Arch. Biochem. Biophys. 2004, 425, 87-94.
    • (2004) Arch. Biochem. Biophys. , vol.425 , pp. 87-94
    • Campos, I.T.1    Silva, M.M.2    Azzolini, S.S.3    Souza, A.F.4    Sampaio, C.A.M.5    Fritz, H.6    Tanaka, A.S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.