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Volumn 8, Issue 4, 2001, Pages 313-327

Bivalent inhibition of human β-tryptase

Author keywords

Cyclodextrin; Tryptase; Bivalent inhibitor; Circular dichroism; X ray analysis

Indexed keywords

BETA CYCLODEXTRIN; BETA CYCLODEXTRIN DERIVATIVE; CYCLODEXTRIN; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; THROMBIN; TRYPSIN; TRYPTASE;

EID: 0035033274     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(01)00011-4     Document Type: Article
Times cited : (59)

References (59)
  • 1
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems - Implications for design and use of multivalent ligands and inhibitors
    • Mammen M., Choi S.-K., Whitesides G.M. Polyvalent interactions in biological systems - Implications for design and use of multivalent ligands and inhibitors. Angew. Chem. Int. Ed. Engl. 37:1998;2755-2794.
    • (1998) Angew. Chem. Int. Ed. Engl. , vol.37 , pp. 2755-2794
    • Mammen, M.1    Choi, S.-K.2    Whitesides, G.M.3
  • 2
    • 0030088053 scopus 로고    scopus 로고
    • Strength in numbers: Non-natural polyvalent carbohydrate derivatives
    • Kiessling L.L., Pohl N.L. Strength in numbers: non-natural polyvalent carbohydrate derivatives. Chem. Biol. 3:1996;71-77.
    • (1996) Chem. Biol. , vol.3 , pp. 71-77
    • Kiessling, L.L.1    Pohl, N.L.2
  • 3
    • 0000358206 scopus 로고
    • Carbohydrate-protein interactions: Basis of glycobiology
    • Lee Y.C., Lee R.T. Carbohydrate-protein interactions: basis of glycobiology. Acc. Chem. Res. 28:1995;321-327.
    • (1995) Acc. Chem. Res. , vol.28 , pp. 321-327
    • Lee, Y.C.1    Lee, R.T.2
  • 4
    • 0024395393 scopus 로고
    • Towards the development of antimicrobial drugs acting by inhibition of pathogen attachment to host cells: A need for polyvalency
    • Matrosovich M.N. Towards the development of antimicrobial drugs acting by inhibition of pathogen attachment to host cells: a need for polyvalency. FEBS Lett. 252:1989;1-4.
    • (1989) FEBS Lett. , vol.252 , pp. 1-4
    • Matrosovich, M.N.1
  • 5
    • 0026080794 scopus 로고
    • Polyacrylamides bearing pendant α-sialoside groups strongly inhibit agglutination of erythrocytes by influenza virus
    • Spaltenstein A., Whitesides G.M. Polyacrylamides bearing pendant α-sialoside groups strongly inhibit agglutination of erythrocytes by influenza virus. J. Am. Chem. Soc. 113:1991;686-687.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 686-687
    • Spaltenstein, A.1    Whitesides, G.M.2
  • 6
    • 0026337968 scopus 로고
    • Ligand recognition by influenza virus. The binding of bivalent sialosides
    • Glick G.D., Toogood P.L., Wiley D.C., Skehel J.J., Knowles J.R. Ligand recognition by influenza virus. The binding of bivalent sialosides. J. Biol. Chem. 266:1991;23660-23669.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23660-23669
    • Glick, G.D.1    Toogood, P.L.2    Wiley, D.C.3    Skehel, J.J.4    Knowles, J.R.5
  • 7
    • 0034701264 scopus 로고    scopus 로고
    • High-affinity pentavalent ligands of Escherichia coli heat-labile enterotoxin by modular structure-based design
    • Fan E., Zhang Z., Minke W.E., Hou Z., Verlinde C.L.M.J., Hol W.G.J. High-affinity pentavalent ligands of Escherichia coli heat-labile enterotoxin by modular structure-based design. J. Am. Chem. Soc. 122:2000;2663-2664.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2663-2664
    • Fan, E.1    Zhang, Z.2    Minke, W.E.3    Hou, Z.4    Verlinde, C.L.M.J.5    Hol, W.G.J.6
  • 8
    • 0030198872 scopus 로고    scopus 로고
    • Synthesis and characterization of bivalent peptide ligands targeted to G-protein-coupled receptors
    • Carrithers M.G., Lerner M.R. Synthesis and characterization of bivalent peptide ligands targeted to G-protein-coupled receptors. Chem. Biol. 3:1996;537-542.
    • (1996) Chem. Biol. , vol.3 , pp. 537-542
    • Carrithers, M.G.1    Lerner, M.R.2
  • 9
    • 0032531947 scopus 로고    scopus 로고
    • Spanning binding sites on allosteric proteins with polymer-linked ligand dimers
    • Kramer R.H., Karpen J.W. Spanning binding sites on allosteric proteins with polymer-linked ligand dimers. Nature. 395:1998;710-713.
    • (1998) Nature , vol.395 , pp. 710-713
    • Kramer, R.H.1    Karpen, J.W.2
  • 11
    • 0029817834 scopus 로고    scopus 로고
    • Highly potent, selective, and low cost bis-tetrahydroaminacrine inhibitors of acetylcholinesterase. Steps toward novel drugs for treating Alzheimer's disease
    • Pang Y.-P., Quiram P., Jelacic T., Hong F., Brimijoin S. Highly potent, selective, and low cost bis-tetrahydroaminacrine inhibitors of acetylcholinesterase. Steps toward novel drugs for treating Alzheimer's disease. J. Biol. Chem. 271:1996;23646-23649.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23646-23649
    • Pang, Y.-P.1    Quiram, P.2    Jelacic, T.3    Hong, F.4    Brimijoin, S.5
  • 12
    • 0040111705 scopus 로고    scopus 로고
    • Bivalent inhibitors of protein tyrosine kinases
    • Profit A.A., Lee T.R., Lawrence D.S. Bivalent inhibitors of protein tyrosine kinases. J. Am. Chem. Soc. 121:1999;280-283.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 280-283
    • Profit, A.A.1    Lee, T.R.2    Lawrence, D.S.3
  • 13
    • 0029104794 scopus 로고
    • Anticoagulatory substances of bloodsucking animals - From hirudin to hirudin mimetics
    • Dodt J. Anticoagulatory substances of bloodsucking animals - from hirudin to hirudin mimetics. Angew. Chem. Int. Ed. Engl. 34:1995;867-880.
    • (1995) Angew. Chem. Int. Ed. Engl. , vol.34 , pp. 867-880
    • Dodt, J.1
  • 16
    • 0015313012 scopus 로고
    • The influence of polyvalency on the binding properties of antibodies
    • Crothers D.M., Metzger H. The influence of polyvalency on the binding properties of antibodies. Immunochemistry. 9:1972;341-357.
    • (1972) Immunochemistry , vol.9 , pp. 341-357
    • Crothers, D.M.1    Metzger, H.2
  • 17
    • 0018797909 scopus 로고
    • Evaluation of group contributions to ligand binding
    • Rappaport H.P. Evaluation of group contributions to ligand binding. J. Theor. Biol. 79:1979;157-165.
    • (1979) J. Theor. Biol. , vol.79 , pp. 157-165
    • Rappaport, H.P.1
  • 18
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks W.P. On the attribution and additivity of binding energies. Proc. Natl. Acad. Sci. USA. 78:1981;4046-4050.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 19
    • 0032076568 scopus 로고    scopus 로고
    • A trivalent system from vancomycin·D-Ala-D-Ala with higher affinity than avidin·biotin
    • Rao J., Lahiri J., Isaacs L., Weis R.M., Whitesides G.M. A trivalent system from vancomycin·D-Ala-D-Ala with higher affinity than avidin·biotin. Science. 280:1998;708-711.
    • (1998) Science , vol.280 , pp. 708-711
    • Rao, J.1    Lahiri, J.2    Isaacs, L.3    Weis, R.M.4    Whitesides, G.M.5
  • 20
    • 0034728565 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of a high-affinity trivalent system derived from vancomycin and L-Lys-D-Ala-D-Ala
    • Rao J., Lahiri J., Weis R.M., Whitesides G.M. Design, synthesis, and characterization of a high-affinity trivalent system derived from vancomycin and L-Lys-D-Ala-D-Ala. J. Am. Chem. Soc. 122:2000;2698-2710.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2698-2710
    • Rao, J.1    Lahiri, J.2    Weis, R.M.3    Whitesides, G.M.4
  • 29
    • 0032558114 scopus 로고    scopus 로고
    • Cyclodextrin as carrier of peptide hormones. Conformational and biological properties of β-cyclodextrin/gastrin constructs
    • Schaschke N., Fiori S., Weyher E., Escrieut C., Fourmy D., Müller G., Moroder L. Cyclodextrin as carrier of peptide hormones. Conformational and biological properties of β-cyclodextrin/gastrin constructs. J. Am. Chem. Soc. 120:1998;7030-7038.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7030-7038
    • Schaschke, N.1    Fiori, S.2    Weyher, E.3    Escrieut, C.4    Fourmy, D.5    Müller, G.6    Moroder, L.7
  • 31
    • 33845469892 scopus 로고
    • Characterization of regiospecific A,C- And A,D-disulfonate capping of β-cyclodextrin. Capping as an efficient production technique
    • Tabushi I., Yamamura K., Nabeshima T. Characterization of regiospecific A,C- and A,D-disulfonate capping of β-cyclodextrin. Capping as an efficient production technique. J. Am. Chem. Soc. 106:1984;5267-5270.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 5267-5270
    • Tabushi, I.1    Yamamura, K.2    Nabeshima, T.3
  • 32
  • 33
    • 0022872843 scopus 로고
    • Regulation of tryptase from human lung mast cells by heparin. Stabilization of the active tetramer
    • Schwartz L.B., Bradford T.R. Regulation of tryptase from human lung mast cells by heparin. Stabilization of the active tetramer. J. Biol. Chem. 261:1986;7372-7379.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7372-7379
    • Schwartz, L.B.1    Bradford, T.R.2
  • 34
    • 0023567897 scopus 로고
    • Regulation of human mast cell tryptase. Effects of enzyme concentration, ionic strength and the structure and negative charge density of polysacchrides
    • Alter S.C., Metcalf D.D., Bradford T.R., Schwartz L.B. Regulation of human mast cell tryptase. Effects of enzyme concentration, ionic strength and the structure and negative charge density of polysacchrides. Biochem. J. 248:1987;821-827.
    • (1987) Biochem. J. , vol.248 , pp. 821-827
    • Alter, S.C.1    Metcalf, D.D.2    Bradford, T.R.3    Schwartz, L.B.4
  • 35
    • 0026518944 scopus 로고
    • Protease composition of exocytosed human skin mast cell protease-proteoglycan complexes. Tryptase resides in a complex distinct from chymase and carboxypeptidase
    • Goldstein S.M., Leong J., Schwartz L.B., Cooke D. Protease composition of exocytosed human skin mast cell protease-proteoglycan complexes. Tryptase resides in a complex distinct from chymase and carboxypeptidase. J. Immunol. 148:1992;2475-2482.
    • (1992) J. Immunol. , vol.148 , pp. 2475-2482
    • Goldstein, S.M.1    Leong, J.2    Schwartz, L.B.3    Cooke, D.4
  • 36
    • 0031762406 scopus 로고    scopus 로고
    • Regulation of the activity of secreted human lung mast cell tryptase by mast cell proteoglycans
    • Lindstedt K.A., Kokkonen J.O., Kovanen P.T. Regulation of the activity of secreted human lung mast cell tryptase by mast cell proteoglycans. Biochim. Biophys. Acta. 1425:1998;617-627.
    • (1998) Biochim. Biophys. Acta , vol.1425 , pp. 617-627
    • Lindstedt, K.A.1    Kokkonen, J.O.2    Kovanen, P.T.3
  • 37
    • 0029974125 scopus 로고    scopus 로고
    • Inactivation of human lung tryptase: Evidence for a re-activable tetrameric intermediate and active monomers
    • Addington K.A., Johnson D.A. Inactivation of human lung tryptase: evidence for a re-activable tetrameric intermediate and active monomers. Biochemistry. 35:1996;13511-13518.
    • (1996) Biochemistry , vol.35 , pp. 13511-13518
    • Addington, K.A.1    Johnson, D.A.2
  • 38
    • 0031806935 scopus 로고    scopus 로고
    • Spontaneous inactivation of human lung tryptase as probed by size-exclusion chromatography and chemical cross-linking: Dissociation of active tetrameric enzyme into inactive monomers is the primary event of the entire process
    • Kozik A., Potempa J., Travis J. Spontaneous inactivation of human lung tryptase as probed by size-exclusion chromatography and chemical cross-linking: dissociation of active tetrameric enzyme into inactive monomers is the primary event of the entire process. Biochim. Biophys. Acta. 1385:1998;139-148.
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 139-148
    • Kozik, A.1    Potempa, J.2    Travis, J.3
  • 39
    • 33947092515 scopus 로고
    • Structural basis of the activation and action of trypsin
    • Huber R., Bode W. Structural basis of the activation and action of trypsin. Acc. Chem. Res. 11:1978;114-122.
    • (1978) Acc. Chem. Res. , vol.11 , pp. 114-122
    • Huber, R.1    Bode, W.2
  • 40
    • 0018781771 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen
    • Bode W. The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen. J. Mol. Biol. 127:1979;357-374.
    • (1979) J. Mol. Biol. , vol.127 , pp. 357-374
    • Bode, W.1
  • 41
    • 0001440268 scopus 로고
    • Optical spectroscopy of proteins
    • in: H. Neurath, R.L. Hill (Eds.), Academic Press, New York
    • C.R. Cantor, S.N. Timasheff, Optical spectroscopy of proteins, in: H. Neurath, R.L. Hill (Eds.), The Proteins, 3rd edn., Vol. 5, Academic Press, New York, 1982, pp. 145-306.
    • (1982) The Proteins, 3rd Edn. , vol.5 , pp. 145-306
    • Cantor, C.R.1    Timasheff, S.N.2
  • 42
    • 0028716614 scopus 로고
    • Contributions of tryptophan side chains to the circular dichroism of globular proteins: Exciton couplets and coupled oscillators
    • Grishina I.B., Woody R.W. Contributions of tryptophan side chains to the circular dichroism of globular proteins: Exciton couplets and coupled oscillators. Faraday Discuss. 99:1994;245-262.
    • (1994) Faraday Discuss. , vol.99 , pp. 245-262
    • Grishina, I.B.1    Woody, R.W.2
  • 43
    • 0027070909 scopus 로고
    • Mast cell tryptases: Examination of unusual characteristics by multiple sequence alignment and molecular modeling
    • Johnson D.A., Barton G.J. Mast cell tryptases: examination of unusual characteristics by multiple sequence alignment and molecular modeling. Protein Sci. 1:1992;370-377.
    • (1992) Protein Sci. , vol.1 , pp. 370-377
    • Johnson, D.A.1    Barton, G.J.2
  • 44
    • 0025217194 scopus 로고
    • Immunologic and physicochemical evidence for conformational changes occuring on conversion of human mast cell tryptase from active tetramer to inactive monomer. Production of monoclonal antibodies recognizing active tryptase
    • Schwartz L.B., Bradford T.R., Lee D.C., Chlebowski J.F. Immunologic and physicochemical evidence for conformational changes occuring on conversion of human mast cell tryptase from active tetramer to inactive monomer. Production of monoclonal antibodies recognizing active tryptase. J. Immunol. 144:1990;2304-2311.
    • (1990) J. Immunol. , vol.144 , pp. 2304-2311
    • Schwartz, L.B.1    Bradford, T.R.2    Lee, D.C.3    Chlebowski, J.F.4
  • 45
    • 0029149499 scopus 로고
    • Structural changes associated with the spontaneous inactivation of the serine proteinase human tryptase
    • Schechter N.M., Eng G.Y., Selwood T., McCaslin D.R. Structural changes associated with the spontaneous inactivation of the serine proteinase human tryptase. Biochemistry. 34:1995;10628-10638.
    • (1995) Biochemistry , vol.34 , pp. 10628-10638
    • Schechter, N.M.1    Eng, G.Y.2    Selwood, T.3    McCaslin, D.R.4
  • 46
    • 0343980651 scopus 로고
    • Dog mast cell proteinases in models of airway secretion, bronchoconstriction, cutaneous vascular permeability, and tissue fibrosis
    • in: G.H. Caughey (Ed.), Marcel Dekker, New York
    • C.P. Sommerhoff, Dog mast cell proteinases in models of airway secretion, bronchoconstriction, cutaneous vascular permeability, and tissue fibrosis, in: G.H. Caughey (Ed.), Mast Cell Proteases in Immunology and Biology, Marcel Dekker, New York, 1995, pp. 145-167.
    • (1995) Mast Cell Proteases in Immunology and Biology , pp. 145-167
    • Sommerhoff, C.P.1
  • 47
    • 0031157105 scopus 로고    scopus 로고
    • Of mites and men - trypsin-like proteases in the lungs
    • Caughey G.H. Of mites and men - trypsin-like proteases in the lungs. Am. J. Respir. Cell Mol. Biol. 16:1997;621-628.
    • (1997) Am. J. Respir. Cell Mol. Biol. , vol.16 , pp. 621-628
    • Caughey, G.H.1
  • 51
    • 0030028575 scopus 로고    scopus 로고
    • Natural distribution of the mouse mast cell protease 7 gene in the C57BL/6 mouse
    • Hunt J.E., Stevens R.L., Austen K.F., Zhang J., Xia Z., Ghildyal N. Natural distribution of the mouse mast cell protease 7 gene in the C57BL/6 mouse. J. Biol Chem. 271:1996;2851-2855.
    • (1996) J. Biol Chem. , vol.271 , pp. 2851-2855
    • Hunt, J.E.1    Stevens, R.L.2    Austen, K.F.3    Zhang, J.4    Xia, Z.5    Ghildyal, N.6
  • 53
    • 0027759314 scopus 로고
    • Bis(5-amidino-2-benzimidazolyl)methane and related amidines are potent, reversible inhibitors of mast cell tryptases
    • Caughey G.H., Raymond W.W., Bacci E., Lombardy R.J., Tidwell R.R. Bis(5-amidino-2-benzimidazolyl)methane and related amidines are potent, reversible inhibitors of mast cell tryptases. J. Pharmacol. Exp. Ther. 264:1993;676-682.
    • (1993) J. Pharmacol. Exp. Ther. , vol.264 , pp. 676-682
    • Caughey, G.H.1    Raymond, W.W.2    Bacci, E.3    Lombardy, R.J.4    Tidwell, R.R.5
  • 58
    • 0028520933 scopus 로고
    • A Kazal-type inhibitor of human mast cell tryptase: Isolation from the medical leech Hirudo medicinalis, characterization, and sequence analysis
    • Sommerhoff C.P., Söllner C., Mentele R., Piechottka G.P., Auerswald E.A., Fritz H. A Kazal-type inhibitor of human mast cell tryptase: Isolation from the medical leech Hirudo medicinalis, characterization, and sequence analysis. Biol. Chem. 375:1994;685-694.
    • (1994) Biol. Chem. , vol.375 , pp. 685-694
    • Sommerhoff, C.P.1    Söllner, C.2    Mentele, R.3    Piechottka, G.P.4    Auerswald, E.A.5    Fritz, H.6
  • 59
    • 0014454095 scopus 로고
    • Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
    • Morrison J.F. Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors. Biochim. Biophys. Acta. 185:1969;269-286.
    • (1969) Biochim. Biophys. Acta , vol.185 , pp. 269-286
    • Morrison, J.F.1


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