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Volumn 10, Issue 12, 2015, Pages 2716-2724

Selective Targeting of Extracellular Insulin-Degrading Enzyme by Quasi-Irreversible Thiol-Modifying Inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; METALLOPROTEINASE INHIBITOR; ENZYME INHIBITOR; HYPERGLYCEMIC AGENT; INSULINASE; THIOL DERIVATIVE;

EID: 84952641633     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.5b00334     Document Type: Article
Times cited : (23)

References (39)
  • 1
    • 84884885060 scopus 로고    scopus 로고
    • Insulysin
    • (Rawlings, N. D. and Salvesen, G. Eds.) 3 rd ed. pp, Academic Press, Boston, MA
    • Leal, M. C. and Morelli, L. (2013) Insulysin, in Handbook of Proteolytic Enzymes (Rawlings, N. D. and Salvesen, G., Eds.) 3 rd ed., pp 1415-1420, Academic Press, Boston, MA.
    • (2013) Handbook of Proteolytic Enzymes , pp. 1415-1420
    • Leal, M.C.1    Morelli, L.2
  • 2
    • 33750870063 scopus 로고    scopus 로고
    • The insulysin (insulin degrading enzyme) enigma
    • Hersh, L. B. (2006) The insulysin (insulin degrading enzyme) enigma Cell. Mol. Life Sci. 63, 2432-2434 10.1007/s00018-006-6238-9
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 2432-2434
    • Hersh, L.B.1
  • 3
    • 0022445076 scopus 로고
    • Inhibition of insulin degradation by hepatoma cells after microinjection of monoclonal antibodies to a specific cytosolic protease
    • Shii, K. and Roth, R. A. (1986) Inhibition of insulin degradation by hepatoma cells after microinjection of monoclonal antibodies to a specific cytosolic protease Proc. Natl. Acad. Sci. U. S. A. 83, 4147-4151 10.1073/pnas.83.12.4147
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 4147-4151
    • Shii, K.1    Roth, R.A.2
  • 4
    • 0037134505 scopus 로고    scopus 로고
    • Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD)
    • Edbauer, D., Willem, M., Lammich, S., Steiner, H., and Haass, C. (2002) Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD) J. Biol. Chem. 277, 13389-13393 10.1074/jbc.M111571200
    • (2002) J. Biol. Chem. , vol.277 , pp. 13389-13393
    • Edbauer, D.1    Willem, M.2    Lammich, S.3    Steiner, H.4    Haass, C.5
  • 5
    • 79958769915 scopus 로고    scopus 로고
    • Post-proteasomal and proteasome-independent generation of MHC class i ligands
    • van Endert, P. (2011) Post-proteasomal and proteasome-independent generation of MHC class I ligands Cell. Mol. Life Sci. 68, 1553-1567 10.1007/s00018-011-0662-1
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 1553-1567
    • Van Endert, P.1
  • 7
    • 0033543723 scopus 로고    scopus 로고
    • The Zn-peptidase superfamily: Functional convergence after evolutionary divergence
    • Makarova, K. S. and Grishin, N. V. (1999) The Zn-peptidase superfamily: functional convergence after evolutionary divergence J. Mol. Biol. 292, 11-17 10.1006/jmbi.1999.3059
    • (1999) J. Mol. Biol. , vol.292 , pp. 11-17
    • Makarova, K.S.1    Grishin, N.V.2
  • 8
    • 0026516458 scopus 로고
    • An unusual active site identified in a family of zinc metalloendopeptidases
    • Becker, A. B. and Roth, R. A. (1992) An unusual active site identified in a family of zinc metalloendopeptidases Proc. Natl. Acad. Sci. U. S. A. 89, 3835-3839 10.1073/pnas.89.9.3835
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 3835-3839
    • Becker, A.B.1    Roth, R.A.2
  • 9
    • 0025397066 scopus 로고
    • [125I]-insulin metabolism by the rat liver in vivo: Evidence that a neutral thiol-protease mediates rapid intracellular insulin degradation
    • Williams, F. G., Johnson, D. E., and Bauer, G. E. (1990) [125I]-insulin metabolism by the rat liver in vivo: evidence that a neutral thiol-protease mediates rapid intracellular insulin degradation Metab., Clin. Exp. 39, 231-241 10.1016/0026-0495(90)90041-A
    • (1990) Metab., Clin. Exp. , vol.39 , pp. 231-241
    • Williams, F.G.1    Johnson, D.E.2    Bauer, G.E.3
  • 10
    • 57049166021 scopus 로고    scopus 로고
    • Molecular bases for the recognition of short peptide substrates and cysteine-directed modifications of human insulin-degrading enzyme
    • Malito, E., Ralat, L. A., Manolopoulou, M., Tsay, J. L., Wadlington, N. L., and Tang, W. J. (2008) Molecular bases for the recognition of short peptide substrates and cysteine-directed modifications of human insulin-degrading enzyme Biochemistry 47, 12822-12834 10.1021/bi801192h
    • (2008) Biochemistry , vol.47 , pp. 12822-12834
    • Malito, E.1    Ralat, L.A.2    Manolopoulou, M.3    Tsay, J.L.4    Wadlington, N.L.5    Tang, W.J.6
  • 12
    • 9144260111 scopus 로고    scopus 로고
    • Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria
    • Leissring, M. A., Farris, W., Wu, X., Christodoulou, D. C., Haigis, M. C., Guarente, L., and Selkoe, D. J. (2004) Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria Biochem. J. 383, 439-446 10.1042/BJ20041081
    • (2004) Biochem. J. , vol.383 , pp. 439-446
    • Leissring, M.A.1    Farris, W.2    Wu, X.3    Christodoulou, D.C.4    Haigis, M.C.5    Guarente, L.6    Selkoe, D.J.7
  • 13
    • 60349088206 scopus 로고    scopus 로고
    • Insulin-degrading enzyme is exported via an unconventional protein secretion pathway
    • Zhao, J., Li, L., and Leissring, M. A. (2009) Insulin-degrading enzyme is exported via an unconventional protein secretion pathway Mol. Neurodegener. 4, 4 10.1186/1750-1326-4-4
    • (2009) Mol. Neurodegener. , vol.4 , pp. 4
    • Zhao, J.1    Li, L.2    Leissring, M.A.3
  • 14
    • 75149166216 scopus 로고    scopus 로고
    • Insulin-degrading enzyme sorting in exosomes: A secretory pathway for a key brain amyloid-beta degrading protease
    • Bulloj, A., Leal, M. C., Xu, H., Castano, E. M., and Morelli, L. (2010) Insulin-degrading enzyme sorting in exosomes: a secretory pathway for a key brain amyloid-beta degrading protease J. Alzheimers Dis. 19, 79-95 10.3233/JAD-2010-1206
    • (2010) J. Alzheimers Dis. , vol.19 , pp. 79-95
    • Bulloj, A.1    Leal, M.C.2    Xu, H.3    Castano, E.M.4    Morelli, L.5
  • 15
    • 0021353578 scopus 로고
    • Degradation of insulin by isolated mouse pancreatic acini. Evidence for cell surface protease activity
    • Goldfine, I. D., Williams, J. A., Bailey, A. C., Wong, K. Y., Iwamoto, Y., Yokono, K., Baba, S., and Roth, R. A. (1984) Degradation of insulin by isolated mouse pancreatic acini. Evidence for cell surface protease activity Diabetes 33, 64-72 10.2337/diab.33.1.64
    • (1984) Diabetes , vol.33 , pp. 64-72
    • Goldfine, I.D.1    Williams, J.A.2    Bailey, A.C.3    Wong, K.Y.4    Iwamoto, Y.5    Yokono, K.6    Baba, S.7    Roth, R.A.8
  • 16
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski, C. A., Lombardo, F., Dominy, B. W., and Feeney, P. J. (2001) Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings Adv. Drug Delivery Rev. 46, 3-26 10.1016/S0169-409X(00)00129-0
    • (2001) Adv. Drug Delivery Rev. , vol.46 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 17
    • 0141621234 scopus 로고    scopus 로고
    • Kinetics of amyloid beta-protein degradation determined by novel fluorescence- and fluorescence polarization-based assays
    • Leissring, M. A., Lu, A., Condron, M. M., Teplow, D. B., Stein, R. L., Farris, W., and Selkoe, D. J. (2003) Kinetics of amyloid beta-protein degradation determined by novel fluorescence- and fluorescence polarization-based assays J. Biol. Chem. 278, 37314-37320 10.1074/jbc.M305627200
    • (2003) J. Biol. Chem. , vol.278 , pp. 37314-37320
    • Leissring, M.A.1    Lu, A.2    Condron, M.M.3    Teplow, D.B.4    Stein, R.L.5    Farris, W.6    Selkoe, D.J.7
  • 18
    • 33750302461 scopus 로고    scopus 로고
    • Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism
    • Shen, Y., Joachimiak, A., Rosner, M. R., and Tang, W. J. (2006) Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism Nature 443, 870-874 10.1038/nature05143
    • (2006) Nature , vol.443 , pp. 870-874
    • Shen, Y.1    Joachimiak, A.2    Rosner, M.R.3    Tang, W.J.4
  • 19
    • 0033003760 scopus 로고    scopus 로고
    • A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays
    • Zhang, J. H., Chung, T. D., and Oldenburg, K. R. (1999) A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays J. Biomol. Screening 4, 67-73 10.1177/108705719900400206
    • (1999) J. Biomol. Screening , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 21
    • 0033605661 scopus 로고    scopus 로고
    • Organophosphorylation of acetylcholinesterase in the presence of peripheral site ligands. Distinct effects of propidium and fasciculin
    • Mallender, W. D., Szegletes, T., and Rosenberry, T. L. (1999) Organophosphorylation of acetylcholinesterase in the presence of peripheral site ligands. Distinct effects of propidium and fasciculin J. Biol. Chem. 274, 8491-8499 10.1074/jbc.274.13.8491
    • (1999) J. Biol. Chem. , vol.274 , pp. 8491-8499
    • Mallender, W.D.1    Szegletes, T.2    Rosenberry, T.L.3
  • 22
    • 79960622162 scopus 로고    scopus 로고
    • Discovery and optimization of sulfonyl acrylonitriles as selective, covalent inhibitors of protein phosphatase methylesterase-1
    • Bachovchin, D. A., Zuhl, A. M., Speers, A. E., Wolfe, M. R., Weerapana, E., Brown, S. J., Rosen, H., and Cravatt, B. F. (2011) Discovery and optimization of sulfonyl acrylonitriles as selective, covalent inhibitors of protein phosphatase methylesterase-1 J. Med. Chem. 54, 5229-5236 10.1021/jm200502u
    • (2011) J. Med. Chem. , vol.54 , pp. 5229-5236
    • Bachovchin, D.A.1    Zuhl, A.M.2    Speers, A.E.3    Wolfe, M.R.4    Weerapana, E.5    Brown, S.J.6    Rosen, H.7    Cravatt, B.F.8
  • 25
    • 0037204544 scopus 로고    scopus 로고
    • Prediction of drug solubility from structure
    • Jorgensen, W. L. and Duffy, E. M. (2002) Prediction of drug solubility from structure Adv. Drug Delivery Rev. 54, 355-366 10.1016/S0169-409X(02)00008-X
    • (2002) Adv. Drug Delivery Rev. , vol.54 , pp. 355-366
    • Jorgensen, W.L.1    Duffy, E.M.2
  • 26
    • 0032600640 scopus 로고    scopus 로고
    • A knowledge-based approach in designing combinatorial or medicinal chemistry libraries for drug discovery. 1. A qualitative and quantitative characterization of known drug databases
    • Ghose, A. K., Viswanadhan, V. N., and Wendoloski, J. J. (1999) A knowledge-based approach in designing combinatorial or medicinal chemistry libraries for drug discovery. 1. A qualitative and quantitative characterization of known drug databases J. Comb. Chem. 1, 55-68 10.1021/cc9800071
    • (1999) J. Comb. Chem. , vol.1 , pp. 55-68
    • Ghose, A.K.1    Viswanadhan, V.N.2    Wendoloski, J.J.3
  • 27
    • 0037030653 scopus 로고    scopus 로고
    • Molecular properties that influence the oral bioavailability of drug candidates
    • Veber, D. F., Johnson, S. R., Cheng, H. Y., Smith, B. R., Ward, K. W., and Kopple, K. D. (2002) Molecular properties that influence the oral bioavailability of drug candidates J. Med. Chem. 45, 2615-2623 10.1021/jm020017n
    • (2002) J. Med. Chem. , vol.45 , pp. 2615-2623
    • Veber, D.F.1    Johnson, S.R.2    Cheng, H.Y.3    Smith, B.R.4    Ward, K.W.5    Kopple, K.D.6
  • 30
    • 57449090909 scopus 로고    scopus 로고
    • Analysis of the reaction of carbachol with acetylcholinesterase using thioflavin T as a coupled fluorescence reporter
    • Rosenberry, T. L., Sonoda, L. K., Dekat, S. E., Cusack, B., and Johnson, J. L. (2008) Analysis of the reaction of carbachol with acetylcholinesterase using thioflavin T as a coupled fluorescence reporter Biochemistry 47, 13056-13063 10.1021/bi8015197
    • (2008) Biochemistry , vol.47 , pp. 13056-13063
    • Rosenberry, T.L.1    Sonoda, L.K.2    Dekat, S.E.3    Cusack, B.4    Johnson, J.L.5
  • 31
    • 0035847089 scopus 로고    scopus 로고
    • Analysis of the subsite specificity of rat insulysin using fluorogenic peptide substrates
    • Song, E. S., Mukherjee, A., Juliano, M. A., Pyrek, J. S., Goodman, J. P., Jr., Juliano, L., and Hersh, L. B. (2001) Analysis of the subsite specificity of rat insulysin using fluorogenic peptide substrates J. Biol. Chem. 276, 1152-1155 10.1074/jbc.M008702200
    • (2001) J. Biol. Chem. , vol.276 , pp. 1152-1155
    • Song, E.S.1    Mukherjee, A.2    Juliano, M.A.3    Pyrek, J.S.4    Goodman, J.P.5    Juliano, L.6    Hersh, L.B.7
  • 33
    • 33645941402 scopus 로고
    • The OPLS Potential Functions for Proteins - Energy Minimizations for Crystals of Cyclic-Peptides and Crambin
    • Jorgensen, W. L. and Tiradorives, J. (1988) The OPLS Potential Functions for Proteins-Energy Minimizations for Crystals of Cyclic-Peptides and Crambin J. Am. Chem. Soc. 110, 1657-1666 10.1021/ja00214a001
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tiradorives, J.2
  • 34
    • 84867219321 scopus 로고    scopus 로고
    • Motion of transfer RNA from the A/T state into the A-site using docking and simulations
    • Caulfield, T. R. and Devkota, B. (2012) Motion of transfer RNA from the A/T state into the A-site using docking and simulations Proteins: Struct., Funct., Genet. 80, 2489-2500 10.1002/prot.24131
    • (2012) Proteins: Struct., Funct., Genet. , vol.80 , pp. 2489-2500
    • Caulfield, T.R.1    Devkota, B.2
  • 35
    • 67651002876 scopus 로고    scopus 로고
    • Energetic analysis of fragment docking and application to structure-based pharmacophore hypothesis generation
    • Loving, K., Salam, N. K., and Sherman, W. (2009) Energetic analysis of fragment docking and application to structure-based pharmacophore hypothesis generation J. Comput.-Aided Mol. Des. 23, 541-554 10.1007/s10822-009-9268-1
    • (2009) J. Comput.-Aided Mol. Des. , vol.23 , pp. 541-554
    • Loving, K.1    Salam, N.K.2    Sherman, W.3
  • 36
    • 84857395820 scopus 로고    scopus 로고
    • Inhibition of prohormone convertases PC1/3 and PC2 by 2,5-dideoxystreptamine derivatives
    • Vivoli, M., Caulfield, T. R., Martinez-Mayorga, K., Johnson, A. T., Jiao, G. S., and Lindberg, I. (2012) Inhibition of prohormone convertases PC1/3 and PC2 by 2,5-dideoxystreptamine derivatives Mol. Pharmacol. 81, 440-454 10.1124/mol.111.077040
    • (2012) Mol. Pharmacol. , vol.81 , pp. 440-454
    • Vivoli, M.1    Caulfield, T.R.2    Martinez-Mayorga, K.3    Johnson, A.T.4    Jiao, G.S.5    Lindberg, I.6
  • 37
    • 33750124980 scopus 로고    scopus 로고
    • Extra precision glide: Docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes
    • Friesner, R. A., Murphy, R. B., Repasky, M. P., Frye, L. L., Greenwood, J. R., Halgren, T. A., Sanschagrin, P. C., and Mainz, D. T. (2006) Extra precision glide: docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes J. Med. Chem. 49, 6177-6196 10.1021/jm051256o
    • (2006) J. Med. Chem. , vol.49 , pp. 6177-6196
    • Friesner, R.A.1    Murphy, R.B.2    Repasky, M.P.3    Frye, L.L.4    Greenwood, J.R.5    Halgren, T.A.6    Sanschagrin, P.C.7    Mainz, D.T.8
  • 38
    • 70350513554 scopus 로고    scopus 로고
    • Novel method for generating structure-based pharmacophores using energetic analysis
    • Salam, N. K., Nuti, R., and Sherman, W. (2009) Novel method for generating structure-based pharmacophores using energetic analysis J. Chem. Inf. Model. 49, 2356-2368 10.1021/ci900212v
    • (2009) J. Chem. Inf. Model. , vol.49 , pp. 2356-2368
    • Salam, N.K.1    Nuti, R.2    Sherman, W.3
  • 39
    • 80053383964 scopus 로고    scopus 로고
    • Molecular dynamics simulations of human DNA methyltransferase 3B with selective inhibitor nanaomycin A
    • Caulfield, T. and Medina-Franco, J. L. (2011) Molecular dynamics simulations of human DNA methyltransferase 3B with selective inhibitor nanaomycin A J. Struct. Biol. 176, 185-191 10.1016/j.jsb.2011.07.015.
    • (2011) J. Struct. Biol. , vol.176 , pp. 185-191
    • Caulfield, T.1    Medina-Franco, J.L.2


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