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Volumn 16, Issue 4, 2007, Pages 662-670

The S2 subsites of cathepsins K and L and their contribution to collagen degradation

Author keywords

Cathepsin; Collagen; Cysteine protease; Peptide inhibitor; Substrate specificity

Indexed keywords

1 (N BENZYLOXYCARBONYL LEUCYL) 5 (N BOC PHENYLALANYL LEUCYL)CARBOHYDRAZIDE; AMIDE; CATHEPSIN K; CATHEPSIN L; COLLAGEN TYPE 1; COLLAGEN TYPE 2; COLLAGEN TYPE 4; CONGO RED; ELASTIN; HYDRAZIDE DERIVATIVE; N (4 BIPHENYLACETYL) S METHYLCYSTEINE (D) ARG PHE BETA PHENETHYLAMIDE; UNCLASSIFIED DRUG;

EID: 33947718470     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062666607     Document Type: Article
Times cited : (51)

References (43)
  • 2
    • 0019948262 scopus 로고
    • L-Trans-epoxysuccinyl-leucylamido(4-guanidino) butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
    • Barrett, A.J., Kembhavi, A.A., Brown, M.A., Kirschke, H., Knight, C.G., Tamai, M., and Hanada, K. 1982. L-Trans-epoxysuccinyl-leucylamido(4-guanidino) butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem. J. 201: 189-198.
    • (1982) Biochem. J , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3    Kirschke, H.4    Knight, C.G.5    Tamai, M.6    Hanada, K.7
  • 3
    • 0035986223 scopus 로고    scopus 로고
    • Thiol-dependent cathepsins: Pathophysiological implications and recent advances in inhibitor design
    • Brömme, D. and Kaleta, J. 2002. Thiol-dependent cathepsins: Pathophysiological implications and recent advances in inhibitor design. Curr. Pharm. Des. 8: 1639-1658.
    • (2002) Curr. Pharm. Des , vol.8 , pp. 1639-1658
    • Brömme, D.1    Kaleta, J.2
  • 4
    • 0029911570 scopus 로고    scopus 로고
    • Peptidyl vinyl sulphones: A new class of potent and selective cysteine protease inhibitors: S2P2 specificity of human cathepsin O2 in comparison with cathepsins S and L
    • Brömme, D., Klaus, J.L., Okamoto, K., Rasnick, D., and Palmer, J.T. 1996. Peptidyl vinyl sulphones: A new class of potent and selective cysteine protease inhibitors: S2P2 specificity of human cathepsin O2 in comparison with cathepsins S and L. Biochem. J. 315: 85-89.
    • (1996) Biochem. J , vol.315 , pp. 85-89
    • Brömme, D.1    Klaus, J.L.2    Okamoto, K.3    Rasnick, D.4    Palmer, J.T.5
  • 6
    • 0343091361 scopus 로고    scopus 로고
    • Protease injury in the development of COPD: Thomas A. Neff Lecture
    • Chapman Jr., H.A. and Shi, G.P. 2000. Protease injury in the development of COPD: Thomas A. Neff Lecture. Chest 117: 295S-299S.
    • (2000) Chest , vol.117
    • Chapman Jr., H.A.1    Shi, G.P.2
  • 7
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • Chapman, H.A., Riese, R.J., and Shi, G.P. 1997. Emerging roles for cysteine proteases in human biology. Annu. Rev. Physiol. 59: 63-88.
    • (1997) Annu. Rev. Physiol , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.P.3
  • 8
    • 33744961634 scopus 로고    scopus 로고
    • Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities
    • Choe, Y., Leonetti, F., Greenbaum, D.C., Lecaille, F., Bogyo, M., Brömme, D., Ellman, J.A., and Craik, C.S. 2006. Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities. J. Biol. Chem. 281: 12824-12832.
    • (2006) J. Biol. Chem , vol.281 , pp. 12824-12832
    • Choe, Y.1    Leonetti, F.2    Greenbaum, D.C.3    Lecaille, F.4    Bogyo, M.5    Brömme, D.6    Ellman, J.A.7    Craik, C.S.8
  • 13
    • 17144394796 scopus 로고    scopus 로고
    • Multiple roles for cysteine cathepsins in cancer
    • Joyce, J.A. and Hanahan, D. 2004. Multiple roles for cysteine cathepsins in cancer. Cell Cycle 3: 1516-1519.
    • (2004) Cell Cycle , vol.3 , pp. 1516-1519
    • Joyce, J.A.1    Hanahan, D.2
  • 14
    • 0032080113 scopus 로고    scopus 로고
    • Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix
    • Kafienah, W., Brömme, D., Buttle, D.J., Croucher, L.J., and Hollander, A.P. 1998. Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix. Biochem. J. 331: 727-732.
    • (1998) Biochem. J , vol.331 , pp. 727-732
    • Kafienah, W.1    Brömme, D.2    Buttle, D.J.3    Croucher, L.J.4    Hollander, A.P.5
  • 15
    • 0036882393 scopus 로고    scopus 로고
    • Human and parasitic papain-like cysteine proteases: Their role in physiology and pathology and recent developments in inhibitor design
    • Lecaille, F., Kaleta, J., and Brömme, D. 2002a. Human and parasitic papain-like cysteine proteases: Their role in physiology and pathology and recent developments in inhibitor design. Chem. Rev. 102: 4459-4488.
    • (2002) Chem. Rev , vol.102 , pp. 4459-4488
    • Lecaille, F.1    Kaleta, J.2    Brömme, D.3
  • 16
    • 0037007965 scopus 로고    scopus 로고
    • Selective inhibition of the collagenolytic activity of human cathepsin K by altering its S2 subsite specificity
    • Lecaille, F., Choe, Y., Brandt, W., Li, Z., Craik, C.S., and Brömme, D. 2002b. Selective inhibition of the collagenolytic activity of human cathepsin K by altering its S2 subsite specificity. Biochemistry 41: 8447-8454.
    • (2002) Biochemistry , vol.41 , pp. 8447-8454
    • Lecaille, F.1    Choe, Y.2    Brandt, W.3    Li, Z.4    Craik, C.S.5    Brömme, D.6
  • 18
    • 0023430366 scopus 로고
    • Monte Carlo-minimization approach to the multiple-minima problem in protein folding
    • Li, Z. and Scheraga, H.A. 1987. Monte Carlo-minimization approach to the multiple-minima problem in protein folding. Proc. Natl. Acad. Sci. 84: 6611-6615.
    • (1987) Proc. Natl. Acad. Sci , vol.84 , pp. 6611-6615
    • Li, Z.1    Scheraga, H.A.2
  • 19
    • 0034711762 scopus 로고    scopus 로고
    • Collagenolytic activity of cathepsin K is specifically modulated by cartilage-resident chondroitin sulfates
    • Li, Z., Hou, W.S., and Brömme, D. 2000. Collagenolytic activity of cathepsin K is specifically modulated by cartilage-resident chondroitin sulfates. Biochemistry 39: 529-536.
    • (2000) Biochemistry , vol.39 , pp. 529-536
    • Li, Z.1    Hou, W.S.2    Brömme, D.3
  • 20
    • 0037047275 scopus 로고    scopus 로고
    • Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate
    • Li, Z., Hou, W.S., Escalante-Torres, C.R., Gelb, B.D., and Brömme, D. 2002. Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate. J. Biol. Chem. 277: 28669-28676.
    • (2002) J. Biol. Chem , vol.277 , pp. 28669-28676
    • Li, Z.1    Hou, W.S.2    Escalante-Torres, C.R.3    Gelb, B.D.4    Brömme, D.5
  • 22
    • 0037810410 scopus 로고    scopus 로고
    • Family C1 cysteine proteases: Biological diversity or redundancy?
    • Nägler, D.K. and Menard, R. 2003. Family C1 cysteine proteases: Biological diversity or redundancy? Biol. Chem. 384: 837-843.
    • (2003) Biol. Chem , vol.384 , pp. 837-843
    • Nägler, D.K.1    Menard, R.2
  • 24
    • 0021676681 scopus 로고
    • Inhibition of cysteine proteinases and dipeptidyl peptidase I by egg-white cystatin
    • Nicklin, M.J. and Barrett, A.J. 1984. Inhibition of cysteine proteinases and dipeptidyl peptidase I by egg-white cystatin. Biochem. J. 223: 245-253.
    • (1984) Biochem. J , vol.223 , pp. 245-253
    • Nicklin, M.J.1    Barrett, A.J.2
  • 25
    • 0037212163 scopus 로고    scopus 로고
    • A polymorphism in the angiogenesis inhibitor, endostatin, in multiple myeloma
    • Ortega, M.M., Nascimento, H., Costa, F.F., Teori, M.T., and Lima, C.S. 2003. A polymorphism in the angiogenesis inhibitor, endostatin, in multiple myeloma. Leuk. Res. 27: 93-94.
    • (2003) Leuk. Res , vol.27 , pp. 93-94
    • Ortega, M.M.1    Nascimento, H.2    Costa, F.F.3    Teori, M.T.4    Lima, C.S.5
  • 26
    • 0029006974 scopus 로고
    • Collagens: Molecular biology, diseases, and potentials for therapy
    • Prockop, D.J. and Kivirikko, K.I. 1995. Collagens: Molecular biology, diseases, and potentials for therapy. Annu. Rev. Biochem. 64: 403-434.
    • (1995) Annu. Rev. Biochem , vol.64 , pp. 403-434
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 27
    • 0005652597 scopus 로고    scopus 로고
    • Fast summation boundary element methods for calculating solvation free energies of macromolecules
    • Purisima, E.O. 1998. Fast summation boundary element methods for calculating solvation free energies of macromolecules. J. Comput. Chem. 19: 1494-1505.
    • (1998) J. Comput. Chem , vol.19 , pp. 1494-1505
    • Purisima, E.O.1
  • 28
    • 84986456126 scopus 로고
    • A simple yet accurate boundary element method for continuum dielectric calculations
    • Purisima, E.O. and Nilar, S.H. 1995. A simple yet accurate boundary element method for continuum dielectric calculations. J. Comput. Chem. 16: 681-689.
    • (1995) J. Comput. Chem , vol.16 , pp. 681-689
    • Purisima, E.O.1    Nilar, S.H.2
  • 31
    • 0033966413 scopus 로고    scopus 로고
    • Cathepsins and compartmentalization in antigen presentation
    • Riese, R.J. and Chapman, H.A. 2000. Cathepsins and compartmentalization in antigen presentation. Curr. Opin. Immunol. 12: 107-113.
    • (2000) Curr. Opin. Immunol , vol.12 , pp. 107-113
    • Riese, R.J.1    Chapman, H.A.2
  • 33
    • 0034495208 scopus 로고    scopus 로고
    • A single amino acid substitution affects substrate specificity in cysteine proteinases from Fasciola hepatica
    • Smooker, P.M., Whisstock, J.C., Irving, J.A., Siyaguna, S., Spithill, T.W., and Pike, R.N. 2000. A single amino acid substitution affects substrate specificity in cysteine proteinases from Fasciola hepatica. Protein Sci. 9: 2567-2572.
    • (2000) Protein Sci , vol.9 , pp. 2567-2572
    • Smooker, P.M.1    Whisstock, J.C.2    Irving, J.A.3    Siyaguna, S.4    Spithill, T.W.5    Pike, R.N.6
  • 35
    • 0034502852 scopus 로고    scopus 로고
    • Cathepsin K in thyroid epithelial cells: Sequence, localization and possible function in extracellular proteolysis of thyroglobulin
    • Tepel, C., Brömme, D., Herzog, V., and Brix, K. 2000. Cathepsin K in thyroid epithelial cells: Sequence, localization and possible function in extracellular proteolysis of thyroglobulin. J. Cell Sci. 113: 4487-4498.
    • (2000) J. Cell Sci , vol.113 , pp. 4487-4498
    • Tepel, C.1    Brömme, D.2    Herzog, V.3    Brix, K.4
  • 37
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • Turk, V., Turk, B., and Turk, D. 2001. Lysosomal cysteine proteases: Facts and opportunities. EMBO J. 20: 4629-4633.
    • (2001) EMBO J , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 38
    • 0037118691 scopus 로고    scopus 로고
    • Inhibition of cathepsin K with lysosomotropic macromolecular inhibitors
    • Wang, D., Pechar, M., Li, W., Kopeckova, P., Brömme, D., and Kopecek, J. 2002. Inhibition of cathepsin K with lysosomotropic macromolecular inhibitors. Biochemistry 41: 8849-8859.
    • (2002) Biochemistry , vol.41 , pp. 8849-8859
    • Wang, D.1    Pechar, M.2    Li, W.3    Kopeckova, P.4    Brömme, D.5    Kopecek, J.6
  • 39
    • 0018699952 scopus 로고
    • The kinetics of reversible tight-binding inhibition
    • Williams, J.W. and Morrison, J.F. 1979. The kinetics of reversible tight-binding inhibition. Methods Enzymol. 63: 437-467.
    • (1979) Methods Enzymol , vol.63 , pp. 437-467
    • Williams, J.W.1    Morrison, J.F.2
  • 40
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word, J.M., Lovell, S.C., Richardson, J.S., and Richardson, D.C. 1999. Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation. J. Mol. Biol. 285: 1735-1747.
    • (1999) J. Mol. Biol , vol.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 41
    • 0033030776 scopus 로고    scopus 로고
    • Localization of rat cathepsin K in osteoclasts and resorption pits: Inhibition of bone resorption cathepsin K-activity by peptidyl vinyl sulfones
    • Xia, L., Kilb, J., Wex, H., Lipyansky, A., Breuil, V., Stein, L., Palmer, J.T., Dempster, D.W., and Brömme, D. 1999. Localization of rat cathepsin K in osteoclasts and resorption pits: Inhibition of bone resorption cathepsin K-activity by peptidyl vinyl sulfones. Biol. Chem. 380: 679-687.
    • (1999) Biol. Chem , vol.380 , pp. 679-687
    • Xia, L.1    Kilb, J.2    Wex, H.3    Lipyansky, A.4    Breuil, V.5    Stein, L.6    Palmer, J.T.7    Dempster, D.W.8    Brömme, D.9
  • 43
    • 4344670363 scopus 로고    scopus 로고
    • Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages
    • Yasuda, Y., Li, Z., Greenbaum, D., Bogyo, M., Weber, E., and Brömme, D. 2004. Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. J. Biol. Chem. 279: 36761-36770.
    • (2004) J. Biol. Chem , vol.279 , pp. 36761-36770
    • Yasuda, Y.1    Li, Z.2    Greenbaum, D.3    Bogyo, M.4    Weber, E.5    Brömme, D.6


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