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Volumn 429, Issue 2, 2010, Pages 379-389

Conformational flexibility and allosteric regulation of cathepsin K

Author keywords

Chondroitin sulfate; Conformational change; Dermatan sulfate; Heparin; Non essential activation; Substrate inhibition

Indexed keywords

7-AMINO-4-METHYLCOUMARIN; ACTIVATION SUBSTRATE; ACTIVE SITE; ALLOSTERIC REGULATION; CHONDROITIN SULFATES; CONFORMATIONAL CHANGE; CONFORMATIONAL FLEXIBILITY; CYSTEINE PEPTIDASE; DERMATAN SULFATE; EXTRACELLULAR SPACE; GLYCOSAMINOGLYCANS; HOMOEOSTASIS; IN-VITRO; K-FUNCTION; KEY ENZYMES; KINETIC PROPERTIES; MOLECULAR LEVELS; MULTIPLE CONFORMATIONS; PHYSIOLOGICAL FUNCTIONS; STABILIZING EFFECTS; SULFATED GLYCOSAMINOGLYCANS;

EID: 77954737401     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100337     Document Type: Article
Times cited : (61)

References (45)
  • 1
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland, Jr, D. E., Nemethy, G. and Filmer, D. (1966) Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5, 365-385
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland Jr., D.E.1    Nemethy, G.2    Filmer, D.3
  • 2
    • 73649152457 scopus 로고
    • Allosteric proteins and cellular control systems
    • Monod, J., Changeux, J. P. and Jacob, F. (1963) Allosteric proteins and cellular control systems. J. Mol. Biol. 6, 306-329
    • (1963) J. Mol. Biol. , vol.6 , pp. 306-329
    • Monod, J.1    Changeux, J.P.2    Jacob, F.3
  • 3
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J. and Changeux, J. P. (1965) On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12, 88-118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 4
    • 41149104308 scopus 로고    scopus 로고
    • Allostery: Absence of a change in shape does not imply that allostery is not at play
    • Tsai, C. J., del Sol, A. and Nussinov, R. (2008) Allostery: absence of a change in shape does not imply that allostery is not at play. J. Mol. Biol. 378, 1-11
    • (2008) J. Mol. Biol. , vol.378 , pp. 1-11
    • Tsai, C.J.1    Del Sol, A.2    Nussinov, R.3
  • 5
    • 17044379501 scopus 로고    scopus 로고
    • Proteinaceous cysteine protease inhibitors
    • Dubin, G. (2005) Proteinaceous cysteine protease inhibitors. Cell. Mol. Life Sci. 62, 653-669
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 653-669
    • Dubin, G.1
  • 6
    • 0029809357 scopus 로고    scopus 로고
    • Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency
    • Gelb, B. D., Shi, G. P., Chapman, H. A. and Desnick, R. J. (1996) Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency. Science 273, 1236-1238
    • (1996) Science , vol.273 , pp. 1236-1238
    • Gelb, B.D.1    Shi, G.P.2    Chapman, H.A.3    Desnick, R.J.4
  • 7
    • 38849159247 scopus 로고    scopus 로고
    • Biochemical properties and regulation of cathepsin K activity
    • Lecaille, F., Brömme, D. and Lalmanach, G. (2008) Biochemical properties and regulation of cathepsin K activity. Biochimie 90, 208-226
    • (2008) Biochimie , vol.90 , pp. 208-226
    • Lecaille, F.1    Brömme, D.2    Lalmanach, G.3
  • 10
    • 37549068912 scopus 로고    scopus 로고
    • Cathepsin K inhibitors: A novel target for osteoporosis therapy
    • Stoch, S. A. and Wagner, J. A. (2008) Cathepsin K inhibitors: a novel target for osteoporosis therapy. Clin. Pharmacol. Ther. 83, 172-176
    • (2008) Clin. Pharmacol. Ther. , vol.83 , pp. 172-176
    • Stoch, S.A.1    Wagner, J.A.2
  • 11
    • 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
  • 12
    • 52049126668 scopus 로고    scopus 로고
    • The crystal and molecular structures of a cathepsin K:chondroitin sulfate complex
    • Li, Z., Kienetz, M., Cherney, M. M., James, M. N. and Brömme, D. (2008) The crystal and molecular structures of a cathepsin K:chondroitin sulfate complex. J. Mol. Biol. 383, 78-91
    • (2008) J. Mol. Biol. , vol.383 , pp. 78-91
    • Li, Z.1    Kienetz, M.2    Cherney, M.M.3    James, M.N.4    Brömme, D.5
  • 15
    • 0017803307 scopus 로고
    • The influence of the type of sulphate bond and degree of sulphation of glycosaminoglycans on their interaction with lysosomal enzymes
    • Avila, J. L. (1978) The influence of the type of sulphate bond and degree of sulphation of glycosaminoglycans on their interaction with lysosomal enzymes. Biochem. J. 171, 489-491
    • (1978) Biochem. J. , vol.171 , pp. 489-491
    • Avila, J.L.1
  • 16
    • 0016817563 scopus 로고
    • Inhibition of leucocytic lysosomal enzymes by glycosaminoglycans in vitro
    • Avila, J. L. and Convit, J. (1975) Inhibition of leucocytic lysosomal enzymes by glycosaminoglycans in vitro. Biochem. J. 152, 57-64
    • (1975) Biochem. J. , vol.152 , pp. 57-64
    • Avila, J.L.1    Convit, J.2
  • 17
    • 0017177020 scopus 로고
    • Physicochemical characteristics of the glycosaminoglycan-lysosomal enzyme interaction in vitro: A model of control of leucocytic lysosomal activity
    • Avila, J. L. and Convit, J. (1976) Physicochemical characteristics of the glycosaminoglycan-lysosomal enzyme interaction in vitro: a model of control of leucocytic lysosomal activity. Biochem. J. 160, 129-136
    • (1976) Biochem. J. , vol.160 , pp. 129-136
    • Avila, J.L.1    Convit, J.2
  • 18
    • 36348941660 scopus 로고    scopus 로고
    • Glycosaminoglycans facilitate procathepsin B activation through disruption of propeptide-mature enzyme interactions
    • Caglič, D., Pungerčar, J. R., Pejler, G., Turk, V. and Turk, B. (2007) Glycosaminoglycans facilitate procathepsin B activation through disruption of propeptide-mature enzyme interactions. J. Biol. Chem. 282, 33076-33085
    • (2007) J. Biol. Chem. , vol.282 , pp. 33076-33085
    • Caglič, D.1    Pungerčar, J.R.2    Pejler, G.3    Turk, V.4    Turk, B.5
  • 19
    • 13844276525 scopus 로고    scopus 로고
    • Recombinant human procathepsin S is capable of autocatalytic processing at neutral pH in the presence of glycosaminoglycans
    • Vasiljeva, O., Dolinar, M., Pungerčar, J. R., Turk, V. and Turk, B. (2005) Recombinant human procathepsin S is capable of autocatalytic processing at neutral pH in the presence of glycosaminoglycans. FEBS Lett. 579, 1285-1290
    • (2005) FEBS Lett. , vol.579 , pp. 1285-1290
    • Vasiljeva, O.1    Dolinar, M.2    Pungerčar, J.R.3    Turk, V.4    Turk, B.5
  • 20
    • 0030026637 scopus 로고    scopus 로고
    • Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts: Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme
    • Brömme, D., Okamoto, K., Wang, B. B. and Biroc, S. (1996) Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts: functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme. J. Biol. Chem. 271, 2126-2132
    • (1996) J. Biol. Chem. , vol.271 , pp. 2126-2132
    • Brömme, D.1    Okamoto, K.2    Wang, B.B.3    Biroc, S.4
  • 21
    • 0033102214 scopus 로고    scopus 로고
    • Expression in Escherichia coli, refolding, and purification of human procathepsin K, an osteoclast-specific protease
    • D'Alessio K, J., McQueney, M. S., Brun, K. A., Orsini, M. J. and Debouck, C. M. (1999) Expression in Escherichia coli, refolding, and purification of human procathepsin K, an osteoclast-specific protease. Protein Expression Purif. 15, 213-220
    • (1999) Protein Expression Purif. , vol.15 , pp. 213-220
    • D'Alessio, K.J.1    McQueney, M.S.2    Brun, K.A.3    Orsini, M.J.4    Debouck, C.M.5
  • 23
    • 77952729445 scopus 로고    scopus 로고
    • Paradoxical interactions between modifiers and elastase-2
    • Schenker, P. and Baici, A. (2010) Paradoxical interactions between modifiers and elastase-2. FEBS J. 277, 2486-2495
    • (2010) FEBS J. , vol.277 , pp. 2486-2495
    • Schenker, P.1    Baici, A.2
  • 24
    • 0029101752 scopus 로고
    • Characterization by spectroscopic, kinetic and equilibrium methods of the interaction between recombinant human cystatin A (stefin A) and cysteine proteinases
    • Pol, E., Olsson, S. L., Estrada, S., Prasthofer, T. W. and Björk, I. (1995) Characterization by spectroscopic, kinetic and equilibrium methods of the interaction between recombinant human cystatin A (stefin A) and cysteine proteinases. Biochem. J. 311, 275-282
    • (1995) Biochem. J. , vol.311 , pp. 275-282
    • Pol, E.1    Olsson, S.L.2    Estrada, S.3    Prasthofer, T.W.4    Björk, I.5
  • 25
    • 34247213889 scopus 로고    scopus 로고
    • Interaction between human cathepsins K, L, and S and elastins: Mechanism of elastinolysis and inhibition by macromolecular inhibitors
    • Novinec, M., Grass, R. N., Stark, W. J., Turk, V., Baici, A. and Lenarčič, B. (2007) Interaction between human cathepsins K, L, and S and elastins: mechanism of elastinolysis and inhibition by macromolecular inhibitors. J. Biol. Chem. 282, 7893-7902
    • (2007) J. Biol. Chem. , vol.282 , pp. 7893-7902
    • Novinec, M.1    Grass, R.N.2    Stark, W.J.3    Turk, V.4    Baici, A.5    Lenarčič, B.6
  • 26
    • 0034110252 scopus 로고    scopus 로고
    • Glycosaminoglycan conformation: Do aqueous molecular dynamics simulations agree with X-ray fiber diffraction?
    • Almond, A. and Sheehan, J. K. (2000) Glycosaminoglycan conformation: do aqueous molecular dynamics simulations agree with X-ray fiber diffraction? Glycobiology 10, 329-338
    • (2000) Glycobiology , vol.10 , pp. 329-338
    • Almond, A.1    Sheehan, J.K.2
  • 29
    • 0014940726 scopus 로고
    • Kinetic aspects of regulation of metabolic processes: The hysteretic enzyme concept
    • Frieden, C. (1970) Kinetic aspects of regulation of metabolic processes: the hysteretic enzyme concept. J. Biol. Chem. 245, 5788-5799
    • (1970) J. Biol. Chem. , vol.245 , pp. 5788-5799
    • Frieden, C.1
  • 32
    • 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
  • 33
    • 70349776038 scopus 로고    scopus 로고
    • Simultaneous interaction of enzymes with two modifiers: Reappraisal of kinetic models and new paradigms
    • Schenker, P. and Baici, A. (2009) Simultaneous interaction of enzymes with two modifiers: reappraisal of kinetic models and new paradigms. J. Theor. Biol. 261, 318-329
    • (2009) J. Theor. Biol. , vol.261 , pp. 318-329
    • Schenker, P.1    Baici, A.2
  • 34
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland, D. E. (1958) Application of a theory of enzyme specificity to protein synthesis. Proc. Natl. Acad. Sci. U.S.A. 44, 98-104
    • (1958) Proc. Natl. Acad. Sci. U.S.A. , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 36
    • 0346220393 scopus 로고    scopus 로고
    • The role of dynamics in allosteric regulation
    • Kern, D. and Zuiderweg, E. R. (2003) The role of dynamics in allosteric regulation. Curr. Opin. Struct. Biol. 13, 748-757
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 748-757
    • Kern, D.1    Zuiderweg, E.R.2
  • 39
    • 0024021040 scopus 로고
    • Conformational flexibility: A new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans
    • Casu, B., Petitou, M., Provasoli, M. and Sinay, P. (1988) Conformational flexibility: a new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans. Trends Biochem. Sci. 13, 221-225
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 221-225
    • Casu, B.1    Petitou, M.2    Provasoli, M.3    Sinay, P.4
  • 40
    • 42449101298 scopus 로고    scopus 로고
    • Serglycin - Structure and biology
    • Kolset, S. O. and Tveit, H. (2008) Serglycin - structure and biology. Cell. Mol. Life Sci. 65, 1073-1085
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1073-1085
    • Kolset, S.O.1    Tveit, H.2
  • 41
    • 45849107647 scopus 로고    scopus 로고
    • The effects of heparin and low molecular weight heparins on bone
    • Rajgopal, R., Bear, M., Butcher, M. K. and Shaughnessy, S. G. (2008) The effects of heparin and low molecular weight heparins on bone. Thromb. Res. 122, 293-298
    • (2008) Thromb. Res. , vol.122 , pp. 293-298
    • Rajgopal, R.1    Bear, M.2    Butcher, M.K.3    Shaughnessy, S.G.4
  • 42
    • 34247610845 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans fine-tune mammalian physiology
    • Bishop, J. R., Schuksz, M. and Esko, J. D. (2007) Heparan sulphate proteoglycans fine-tune mammalian physiology. Nature 446, 1030-1037
    • (2007) Nature , vol.446 , pp. 1030-1037
    • Bishop, J.R.1    Schuksz, M.2    Esko, J.D.3
  • 43
    • 6344219895 scopus 로고    scopus 로고
    • Is allostery an intrinsic property of all dynamic proteins?
    • Gunasekaran, K., Ma, B. and Nussinov, R. (2004) Is allostery an intrinsic property of all dynamic proteins? Proteins 57, 433-443
    • (2004) Proteins , vol.57 , pp. 433-443
    • Gunasekaran, K.1    Ma, B.2    Nussinov, R.3
  • 45
    • 32344434479 scopus 로고    scopus 로고
    • The changing landscape of protein allostery
    • Swain, J. F. and Gierasch, L. M. (2006) The changing landscape of protein allostery. Curr. Opin. Struct. Biol. 16, 102-108
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 102-108
    • Swain, J.F.1    Gierasch, L.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.