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Volumn 41, Issue 12, 1998, Pages 2100-2110

Specific and irreversible cyclopeptide inhibitors of dipeptidyl peptidase IV activity of the T-cell activation antigen CD26

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPEPTIDE; DIPEPTIDYL PEPTIDASE IV; DIPHENYL ETHER; ENZYME INHIBITOR; IMINE; PROLINE; PYRROLIDINE DERIVATIVE; QUINONE DERIVATIVE; SULFONIUM DERIVATIVE; TRIFLUOROACETIC ACID;

EID: 14444274339     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm970640l     Document Type: Article
Times cited : (16)

References (51)
  • 1
    • 0027439867 scopus 로고
    • Proline-Dependent Structural and Biological Properties of Peptides and Proteins
    • Yaron, A.; Naider, F. Proline-Dependent Structural and Biological Properties of Peptides and Proteins. Crit. Rev. Biochem. Mol. Biol. 1993, 28, 31-81.
    • (1993) Crit. Rev. Biochem. Mol. Biol. , vol.28 , pp. 31-81
    • Yaron, A.1    Naider, F.2
  • 4
    • 0028223435 scopus 로고
    • Human Imnunodificiency Virus 1 Tat Binds to Dipeptidyl Aminopeptidase IV (CD26): A Possible Mecanism for Tat's Immunosuppressive activity
    • Gutheil, W. G.; Subramanyam, M.; Flentke, G. R.; Sanford, D. G.; Munooz, E.; Huber, B. T.; Bachovchin, W. W. Human Imnunodificiency Virus 1 Tat Binds to Dipeptidyl Aminopeptidase IV (CD26): A Possible Mecanism for Tat's Immunosuppressive activity. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 6594-6598.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 6594-6598
    • Gutheil, W.G.1    Subramanyam, M.2    Flentke, G.R.3    Sanford, D.G.4    Munooz, E.5    Huber, B.T.6    Bachovchin, W.W.7
  • 5
    • 0029940265 scopus 로고    scopus 로고
    • Specific Binding of Adenosine Deaminase but not HIV-1 Transactivator Protein Tat to Human CD26
    • Blanco, J.; Marié, I.; Callebaut, C.; Jacotot, E.; Krust, B.; Hovanessian, A. G. Specific Binding of Adenosine Deaminase but not HIV-1 Transactivator Protein Tat to Human CD26. Exp. Cell. Res. 1996, 225, 102-111.
    • (1996) Exp. Cell. Res. , vol.225 , pp. 102-111
    • Blanco, J.1    Marié, I.2    Callebaut, C.3    Jacotot, E.4    Krust, B.5    Hovanessian, A.G.6
  • 7
    • 14444275674 scopus 로고
    • Direct Association of Adenosine Deaminase with a T Cell Activation Antigen, CD26
    • Kameoka, J.; Tanaka, T.; Nojima, Y.; Schlossman, S. F.; Morimoto, C. Direct Association of Adenosine Deaminase with a T Cell Activation Antigen, CD26. Science 1993, 267, 166-169.
    • (1993) Science , vol.267 , pp. 166-169
    • Kameoka, J.1    Tanaka, T.2    Nojima, Y.3    Schlossman, S.F.4    Morimoto, C.5
  • 8
    • 0025992545 scopus 로고
    • Coassociation of CD26 (Dipeptidyl Peptidase IV) with CD45 on the Surface of Human T Lymphocytes
    • Torimoto, Y.; Dang, N. H.; Vivier, E.; Tanaka, T.; Schlossman, S. F.; Morimoto, C. Coassociation of CD26 (Dipeptidyl Peptidase IV) with CD45 on the Surface of Human T Lymphocytes. J. Immunol. 1991, 147, 2514-2517.
    • (1991) J. Immunol. , vol.147 , pp. 2514-2517
    • Torimoto, Y.1    Dang, N.H.2    Vivier, E.3    Tanaka, T.4    Schlossman, S.F.5    Morimoto, C.6
  • 10
    • 0028323205 scopus 로고
    • CD26: A Surface Protease Involved in T-Cell Activation
    • Fleisher, B. CD26: a Surface Protease Involved in T-Cell Activation. Immunol. Today 1994, 15, 180-184.
    • (1994) Immunol. Today , vol.15 , pp. 180-184
    • Fleisher, B.1
  • 11
    • 0027270023 scopus 로고
    • The Costimulatory Activity of the CD26 Antigen Requires Dpeptidyl Peptidase IV Enzymatic Activity
    • Tanaka, T.; Kameoka, J.; Yaron, A.; Schlossman, S. F.; Morimoto, C. The Costimulatory Activity of the CD26 Antigen Requires Dpeptidyl Peptidase IV Enzymatic Activity. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 4586-4590.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 4586-4590
    • Tanaka, T.1    Kameoka, J.2    Yaron, A.3    Schlossman, S.F.4    Morimoto, C.5
  • 12
    • 0029086491 scopus 로고
    • Unchanged Signaling Capacity of Mutant CD26/Dipeptidylpeptidase IV Molecules Devoid of Enzymatic Activity
    • Steeg, C.; Hartwig, U.; Fleisher, B. Unchanged Signaling Capacity of Mutant CD26/Dipeptidylpeptidase IV Molecules Devoid of Enzymatic Activity. Cell Immunol. 1995, 164, 311-315.
    • (1995) Cell Immunol. , vol.164 , pp. 311-315
    • Steeg, C.1    Hartwig, U.2    Fleisher, B.3
  • 13
    • 0025976294 scopus 로고
    • Are Diprotin A (Ile-Pro-Ile) and Diprotin B (Val-Pro-Leu) Inhibitors or Substrates of Dipeptidyl Peptidase IV?
    • Rahfeld, J.; Schierhorn, M.; Hartrodt, B.; Neubert, K.; Heins, J. Are Diprotin A (Ile-Pro-Ile) and Diprotin B (Val-Pro-Leu) Inhibitors or Substrates of Dipeptidyl Peptidase IV? Biochim. Biophys. Acta 1991, 1076, 314-316.
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 314-316
    • Rahfeld, J.1    Schierhorn, M.2    Hartrodt, B.3    Neubert, K.4    Heins, J.5
  • 15
    • 0342560236 scopus 로고    scopus 로고
    • Competitive Inhibition of Proline Specific Enzymes by Amino Acid Thioxopyrrolidides and Thiazolidides
    • Stöckel, A.; Demuth, H.-U.; Neubert, K. Competitive Inhibition of Proline Specific Enzymes by Amino Acid Thioxopyrrolidides and Thiazolidides. Peptides: Chem., Struct. Biol. 1996, 709-710.
    • (1996) Peptides: Chem., Struct. Biol. , pp. 709-710
    • Stöckel, A.1    Demuth, H.-U.2    Neubert, K.3
  • 17
    • 0028803516 scopus 로고
    • Aminoacylpyrrolidine-2-Nitriles: Potent and Stable Inhibitors of Dipeptidyl-Peptidase IV (CD26)
    • Li, J.; Wilk, E.; Wilk, S. Aminoacylpyrrolidine-2-Nitriles: Potent and Stable Inhibitors of Dipeptidyl-Peptidase IV (CD26). Arch. Biochem. Biophys. 1995, 3, 148-154.
    • (1995) Arch. Biochem. Biophys. , vol.3 , pp. 148-154
    • Li, J.1    Wilk, E.2    Wilk, S.3
  • 23
    • 0027305358 scopus 로고
    • Separation of L-Pro-D-Pro-BoroPro into its Component Diastereomers and Kinetic Analysis of Their Inhibition of Dipeptidyl Peptidase IV. A New Method for the Analysis of Slow, Tight-Binding Inhibition
    • Gutheil, G. W.; Bachovchin, W. W. Separation of L-Pro-D-Pro-BoroPro into its Component Diastereomers and Kinetic Analysis of Their Inhibition of Dipeptidyl Peptidase IV. A New Method for the Analysis of Slow, Tight-Binding Inhibition. Biochemistry 1993, 32, 8723-8731.
    • (1993) Biochemistry , vol.32 , pp. 8723-8731
    • Gutheil, G.W.1    Bachovchin, W.W.2
  • 25
    • 0031026598 scopus 로고    scopus 로고
    • Inhibition of Dipeptidyl Peptidase IV (CD26) by Peptide Boronic Acid Dipeptides
    • Pargellis, C. A.; Campbell, S. J.; Pav, S.; Graham, E. T.; Pittner, T. P. Inhibition of Dipeptidyl Peptidase IV (CD26) by Peptide Boronic Acid Dipeptides. J. Enzyme Inhib. 1997, 11, 151-169.
    • (1997) J. Enzyme Inhib. , vol.11 , pp. 151-169
    • Pargellis, C.A.1    Campbell, S.J.2    Pav, S.3    Graham, E.T.4    Pittner, T.P.5
  • 28
    • 0024205414 scopus 로고
    • Dipeptidyl Peptidase IV-Inactivation with N-Peptidyl-O-aroyl Hydroxylamines
    • Demuth, H.-U.; Baumgrass, R.; Schaper, C.; Fischer, G.; Barth, A. Dipeptidyl Peptidase IV-Inactivation with N-Peptidyl-O-aroyl Hydroxylamines. J. Enzyme Inhib. 1988, 2, 129-142.
    • (1988) J. Enzyme Inhib. , vol.2 , pp. 129-142
    • Demuth, H.-U.1    Baumgrass, R.2    Schaper, C.3    Fischer, G.4    Barth, A.5
  • 29
    • 0027401646 scopus 로고
    • Design of [ω-N-(O-Acyl) Hydroxy Amide]Aminodicarboxylic Acid Pyrrolidides as Potent Inhibitors of Proline-Specific Peptidases
    • Demuth, H.-U.; Schlenzig, D.; Schierhorn, A.; Grosche, G.; Chapot-Chartier, M.-P.; Gripon, J. C. Design of [ω-N-(O-Acyl) Hydroxy Amide]Aminodicarboxylic Acid Pyrrolidides as Potent Inhibitors of Proline-Specific Peptidases. FEBS Lett. 1993, 320, 23-27.
    • (1993) FEBS Lett. , vol.320 , pp. 23-27
    • Demuth, H.-U.1    Schlenzig, D.2    Schierhorn, A.3    Grosche, G.4    Chapot-Chartier, M.-P.5    Gripon, J.C.6
  • 30
    • 0029655675 scopus 로고    scopus 로고
    • Fluoroolefin Containing Dipeptide Isosteres as Inhibitors of Dipeptidyi Peptidase IV (CD26)
    • Welch, J. T.; Lin, J. Fluoroolefin Containing Dipeptide Isosteres as Inhibitors of Dipeptidyi Peptidase IV (CD26). Tetrahedron 1996, 52, 291-304.
    • (1996) Tetrahedron , vol.52 , pp. 291-304
    • Welch, J.T.1    Lin, J.2
  • 32
    • 0002265609 scopus 로고
    • Catalytic Mechanism of Dipeptidyl Peptidase IV in Fleisher, B. Dipeptidyl peptidase IV (CD26)
    • Springer-Verlag: New York
    • Demuth, H.-U.; Heins, J. Catalytic Mechanism of Dipeptidyl Peptidase IV in Fleisher, B. Dipeptidyl peptidase IV (CD26) in Metabolism and in the Immune Response; Springer-Verlag: New York, 1995; pp 1-35.
    • (1995) Metabolism and in the Immune Response , pp. 1-35
    • Demuth, H.-U.1    Heins, J.2
  • 33
    • 0029051385 scopus 로고
    • Nature of the Inactivation of Elastase by N-Peptidyl-O-aroyl Hydroxylamine as a Function of pH
    • Ding, X.; Rasmussen, B. F.; Demuth, H.-U.; Ringe, D.; Steinmetz, A. C. U. Nature of the Inactivation of Elastase by N-Peptidyl-O-aroyl Hydroxylamine as a Function of pH. Biochemistry 1995, 34, 7749-7756.
    • (1995) Biochemistry , vol.34 , pp. 7749-7756
    • Ding, X.1    Rasmussen, B.F.2    Demuth, H.-U.3    Ringe, D.4    Steinmetz, A.C.U.5
  • 34
    • 0027270445 scopus 로고
    • New Mechanism-Based Inactivators of Trypsin-like Proteinases. Selective Inactivation of Urokinase by Functionalized Cyclopeptides Incorporating a Sulfoniomethyl-Substitued m-Aminobenzoic Acid Residue
    • Wakselman, M.; Xie, J.; Mazaleyrat, J.-P.; Bogetto, N.; Vilain, A.-C.; Montagne, J.-J.; Reboud-Ravaux, M. New Mechanism-Based Inactivators of Trypsin-like Proteinases. Selective Inactivation of Urokinase by Functionalized Cyclopeptides Incorporating a Sulfoniomethyl-Substitued m-Aminobenzoic Acid Residue. J. Med. Chem. 1993, 36, 1539-1547.
    • (1993) J. Med. Chem. , vol.36 , pp. 1539-1547
    • Wakselman, M.1    Xie, J.2    Mazaleyrat, J.-P.3    Bogetto, N.4    Vilain, A.-C.5    Montagne, J.-J.6    Reboud-Ravaux, M.7
  • 35
    • 0014211618 scopus 로고
    • On the Size of the Active Site in Proteases. I. Papain
    • Schechter, I.; Berger, A. On the Size of the Active Site in Proteases. I. Papain. Biochem. Biophys. Res. Commun. 1967, 27, 157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 36
    • 0030037462 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV-β, a Novel Form of Cell-Surface-Expressed Protein with Dipeptidyl-Peptidase IV Activity
    • Jacotot, E.; Callebaut, C.; Blanco, J.; Krust, B.; Neubert, K.; Barth, A.; Hovanessian, A. G. Dipeptidyl-peptidase IV-β, a Novel Form of Cell-Surface-Expressed Protein with Dipeptidyl-Peptidase IV Activity. Eur. J. Biochem. 1996, 239, 248-258.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 248-258
    • Jacotot, E.1    Callebaut, C.2    Blanco, J.3    Krust, B.4    Neubert, K.5    Barth, A.6    Hovanessian, A.G.7
  • 37
    • 0029759396 scopus 로고    scopus 로고
    • Oligoanthranilamides Non-Peptide Subunits that Show Formation of Specific Secondary Structure
    • Hamuro, Y.; Geib, S. J.; Hamilton, A. D. Oligoanthranilamides Non-Peptide Subunits that Show Formation of Specific Secondary Structure. J. Am. Chem. Soc. 1996, 118, 7529-7541.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7529-7541
    • Hamuro, Y.1    Geib, S.J.2    Hamilton, A.D.3
  • 39
    • 85008004893 scopus 로고
    • Efficient Removal Protecting group by a "Push-Pull" Mecanism. II. Deprotection of O-Benzyltyrosine with Thioanisole-Trifluoroacetic Acid System Without O to C Rearrangement
    • Kiso, Y.; Ukawa, K.; Ito, K.; Akita, T. Efficient Removal Protecting group by a "Push-Pull" Mecanism. II. Deprotection of O-Benzyltyrosine with Thioanisole-Trifluoroacetic Acid System Without O to C Rearrangement. Chem. Pharm. Bull. 1980, 28, 673-676.
    • (1980) Chem. Pharm. Bull. , vol.28 , pp. 673-676
    • Kiso, Y.1    Ukawa, K.2    Ito, K.3    Akita, T.4
  • 40
    • 31944447949 scopus 로고
    • Efficient Removal of N-benzyloxycarbonyl Group by a "Push-Pull" Mechanism Using Thioanisole-Trifluroroacetic Acid, Exemplified by a Synthesis of Met-Enkephalin
    • Kiso, Y.; Ukawa, K.; Akita, T. Efficient Removal of N-benzyloxycarbonyl Group by a "Push-Pull" Mechanism Using Thioanisole-Trifluroroacetic Acid, Exemplified by a Synthesis of Met-Enkephalin. J. Chem. Soc., Chem. Commun. 1980, 101-102.
    • (1980) J. Chem. Soc., Chem. Commun. , pp. 101-102
    • Kiso, Y.1    Ukawa, K.2    Akita, T.3
  • 41
    • 0028871408 scopus 로고
    • A Model of the Active Site of Dipeptidyl Peptidase IV Predicted by Comparative Molecular Field Analysis and Molecular Modelling Simulations
    • Brandt, W.; Lehmann, T.; Thondorf, L; Born, I.; Schutkowski M.; Rahfeld, J.-U.; Neubert, K.; Barth, A. A Model of the Active Site of Dipeptidyl Peptidase IV Predicted by Comparative Molecular Field Analysis and Molecular Modelling Simulations. Int. J. Pept. Protein Res. 1995, 46, 494-507.
    • (1995) Int. J. Pept. Protein Res. , vol.46 , pp. 494-507
    • Brandt, W.1    Lehmann, T.2    Thondorf, L.3    Born, I.4    Schutkowski, M.5    Rahfeld, J.-U.6    Neubert, K.7    Barth, A.8
  • 42
    • 0029995146 scopus 로고    scopus 로고
    • A New Mechanism in Serine Proteases Catalysis Exhibited by Dipeptidyl Peptidase IV (DP IV)
    • Brandt, W.; Ludwig, O.; Thondorf, I.; Barth, A. A New Mechanism in Serine Proteases Catalysis Exhibited by Dipeptidyl Peptidase IV (DP IV). Eur. J. Biochem. 1996, 236, 109-114.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 109-114
    • Brandt, W.1    Ludwig, O.2    Thondorf, I.3    Barth, A.4
  • 43
    • 4243664295 scopus 로고
    • A Survey of Hammett Substituent Constant and Resonnance and Field Parameters
    • Hansch, C.; Leo, A.; Taft, R. W. A Survey of Hammett Substituent Constant and Resonnance and Field Parameters. Chem. Rev. 1991, 97, 165-195.
    • (1991) Chem. Rev. , vol.97 , pp. 165-195
    • Hansch, C.1    Leo, A.2    Taft, R.W.3
  • 44
    • 0000231181 scopus 로고
    • 1,4- and 1,6-Eliminations from Hydroxy- and Amino-Substitued Benzyl Systems: Chemical and Biochemical Applications
    • Wakselman, M. 1,4- and 1,6-Eliminations From Hydroxy- and Amino-Substitued Benzyl Systems: Chemical and Biochemical Applications. Nouv. J. Chim. 1983, 7, 439-447.
    • (1983) Nouv. J. Chim. , vol.7 , pp. 439-447
    • Wakselman, M.1
  • 47
    • 0029045651 scopus 로고
    • CD26 Expression Correlates with Entry, Replication and Cytopathicity of Monocytotrophic HIV-1 Strains in a T-Cell Line
    • Oravecz, Z.; Rodriquez, G.; Koffi, J.; Wang, J.; Ditto, M.; Bou-Habid, D. C.; Lusso, P.; Norcross, M. A. CD26 Expression Correlates with Entry, Replication and Cytopathicity of Monocytotrophic HIV-1 Strains in a T-Cell Line. Nature Med. 1995, 1, 919.
    • (1995) Nature Med. , vol.1 , pp. 919
    • Oravecz, Z.1    Rodriquez, G.2    Koffi, J.3    Wang, J.4    Ditto, M.5    Bou-Habid, D.C.6    Lusso, P.7    Norcross, M.A.8
  • 50
    • 0030738451 scopus 로고    scopus 로고
    • Inhibition of Human Immunodeficiency Virus Type 1 Infection in T-Cell Line (CEM) by New Dipeptidyl-Peptidase IV (CD26) Inhibitors
    • Jiang, J. D.; Wilk, S.; Li, J.; Zhang, H.; Bekesi, J. G. Inhibition of Human Immunodeficiency Virus Type 1 Infection in T-Cell Line (CEM) by New Dipeptidyl-Peptidase IV (CD26) Inhibitors. Res. Virol. 1997, 148, 255-266.
    • (1997) Res. Virol. , vol.148 , pp. 255-266
    • Jiang, J.D.1    Wilk, S.2    Li, J.3    Zhang, H.4    Bekesi, J.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.