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Volumn 91, Issue 1, 2012, Pages 32-39

Cathepsin K preferentially solubilizes matured bone matrix

Author keywords

Bone matrix solubilization; Cathepsin K; Type I collagen posttranslational modification

Indexed keywords

ADVANCED GLYCATION END PRODUCT; CARBOXY TERMINAL TELOPEPTIDE; CATHEPSIN K; COLLAGEN; COLLAGEN TYPE 1; DEOXYPYRIDINOLINE; HYDROXYPROLINE; PENTOSIDINE; PYRIDINOLINE;

EID: 84863471584     PISSN: 0171967X     EISSN: 14320827     Source Type: Journal    
DOI: 10.1007/s00223-012-9604-7     Document Type: Article
Times cited : (20)

References (46)
  • 1
    • 0018857304 scopus 로고
    • The hydroxypyridinium crosslinks of skeletal collagens: Their measurement, properties and a proposed pathway of formation
    • Eyre DR, Oguchi H (1980) The hydroxypyridinium cross-links of skeletal collagens: their measurement, properties and a proposed pathway of formation. Biochem Biophys Res Commun 92:403-410 (Pubitemid 10098580)
    • (1980) Biochemical and Biophysical Research Communications , vol.92 , Issue.2 , pp. 403-410
    • Eyre, D.R.1    Oguchi, H.2
  • 2
    • 0018858817 scopus 로고
    • Collagen: Molecular diversity in the body's protein scaffold
    • Eyre DR (1980) Collagen: molecular diversity in the body's protein scaffold. Science 207:1315-1322
    • (1980) Science , vol.207 , pp. 1315-1322
    • Eyre, D.R.1
  • 3
    • 0015502858 scopus 로고
    • Age-related changes in collagen: The identification of reducible lysine-carbohydrate condensation products
    • Robins SP, Bailey AJ (1972) Age-related changes in collagen: the identification of reducible lysine-carbohydrate condensation products. Biochem Biophys Res Commun 48:76-84
    • (1972) Biochem Biophys Res Commun , vol.48 , pp. 76-84
    • Robins, S.P.1    Bailey, A.J.2
  • 4
    • 0024852380 scopus 로고
    • Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process
    • Sell DR, Monnier VM (1989) Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process. J Biol Chem 264:21597-21602 (Pubitemid 20028722)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.36 , pp. 21597-21602
    • Sell, D.R.1    Monnir, V.M.2
  • 5
    • 2342648312 scopus 로고    scopus 로고
    • The AGE of the matrix: Chemistry, consequence and cure
    • DeGroot J (2004) The AGE of the matrix: chemistry, consequence and cure. Curr Opin Pharmacol 4:301-305
    • (2004) Curr Opin Pharmacol , vol.4 , pp. 301-305
    • DeGroot, J.1
  • 6
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation
    • Geiger T, Clarke S (1987) Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. J Biol Chem 262:785-794 (Pubitemid 17005254)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.2 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 7
    • 0034141218 scopus 로고    scopus 로고
    • Collagen fragments in urine derived from bone resorption are highly racemized and isomerized: A biological clock of protein aging with clinical potential
    • DOI 10.1042/0264-6021:3450473
    • Cloos PA, Fledelius C (2000) Collagen fragments in urine derived from bone resorption are highly racemized and isomerized: a biological clock of protein aging with clinical potential. Biochem J 345(Pt 3):473-480 (Pubitemid 30099075)
    • (2000) Biochemical Journal , vol.345 , Issue.3 , pp. 473-480
    • Cloos, P.A.C.1    Fledelius, C.2
  • 8
    • 0034141745 scopus 로고    scopus 로고
    • Racemization and isomerization of type I collagen C-telopeptides in human bone and soft tissues: Assessment of tissue turnover
    • DOI 10.1042/0264-6021:3450481
    • Gineyts E, Cloos PA, Borel O, Grimaud L, Delmas PD, Garnero P (2000) Racemization and isomerization of type I collagen C-telopeptides in human bone and soft tissues: assessment of tissue turnover. Biochem J 345(Pt 3):481-485 (Pubitemid 30099076)
    • (2000) Biochemical Journal , vol.345 , Issue.3 , pp. 481-485
    • Gineyts, E.1    Cloos, P.A.C.2    Borel, O.3    Grimaud, L.4    Delmas, P.D.5    Garnero, P.6
  • 9
    • 0030999235 scopus 로고    scopus 로고
    • Characterization of urinary degradation products derived from type I collagen. Identification of a beta-isomerized ASP-GLY sequence within the C- terminal telopeptide (alpha1) region
    • DOI 10.1074/jbc.272.15.9755
    • Fledelius C, Johnsen AH, Cloos PA, Bonde M, Qvist P (1997) Characterization of urinary degradation products derived from type I collagen. Identification of a beta-isomerized Asp-Gly sequence within the C-terminal telopeptide (alpha1) region. J Biol Chem 272:9755-9763 (Pubitemid 27171639)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.15 , pp. 9755-9763
    • Fledelius, C.1    Johnsen, A.H.2    Cloos, P.A.C.3    Bonde, M.4    Qvist, P.5
  • 10
    • 0036313364 scopus 로고    scopus 로고
    • Age-related changes in the collagen network and toughness of bone
    • DOI 10.1016/S8756-3282(01)00697-4, PII S8756328201006974
    • Wang X, Shen X, Li X, Agrawal CM (2002) Age-related changes in the collagen network and toughness of bone. Bone 31:1-7 (Pubitemid 34754417)
    • (2002) Bone , vol.31 , Issue.1 , pp. 1-7
    • Wang, X.1    Shen, X.2    Li, X.3    Mauli, A.C.4
  • 11
  • 12
    • 0031973823 scopus 로고    scopus 로고
    • Changes in the stiffness, strength, and toughness of human cortical bone with age
    • DOI 10.1016/S8756-3282(97)00228-7, PII S8756328297002287
    • Zioupos P, Currey JD (1998) Changes in the stiffness, strength, and toughness of human cortical bone with age. Bone 22:57-66 (Pubitemid 28033654)
    • (1998) Bone , vol.22 , Issue.1 , pp. 57-66
    • Zioupos, P.1    Currey, J.D.2
  • 13
    • 0032032089 scopus 로고    scopus 로고
    • Collagen cross-links in mineralizing tissues: A review of their chemistry, function, and clinical relevance
    • DOI 10.1016/S8756-3282(97)00279-2, PII S8756328297002792
    • Knott L, Bailey AJ (1998) Collagen cross-links in mineralizing tissues: a review of their chemistry, function, and clinical relevance. Bone 22:181-187 (Pubitemid 28127472)
    • (1998) Bone , vol.22 , Issue.3 , pp. 181-187
    • Knott, L.1    Bailey, A.J.2
  • 15
    • 0036233579 scopus 로고    scopus 로고
    • Type I collagen racemization and isomerization and the risk of fracture in postmenopausal women: The OFELY prospective study
    • Garnero P, Cloos P, Sornay-Rendu E, Qvist P, Delmas PD (2002) Type I collagen racemization and isomerization and the risk of fracture in postmenopausal women: the OFELY prospective study. J Bone Miner Res 17:826-833 (Pubitemid 34441899)
    • (2002) Journal of Bone and Mineral Research , vol.17 , Issue.5 , pp. 826-833
    • Garnero, P.1    Cloos, P.2    Sornay-Rendu, E.3    Qvist, P.4    Delmas, P.D.5
  • 16
    • 0035134299 scopus 로고    scopus 로고
    • Influence of nonenzymatic glycation on biomechanical properties of cortical bone
    • DOI 10.1016/S8756-3282(00)00434-8, PII S8756328200004348
    • Vashishth D, Gibson GJ, Khoury JI, Schaffler MB, Kimura J, Fyhrie DP (2001) Influence of nonenzymatic glycation on biomechanical properties of cortical bone. Bone 28:195-201 (Pubitemid 32140975)
    • (2001) Bone , vol.28 , Issue.2 , pp. 195-201
    • Vashishth, D.1    Gibson, G.J.2    Khoury, J.I.3    Schaffler, M.B.4    Kimura, J.5    Fyhrie, D.P.6
  • 17
    • 37349069143 scopus 로고    scopus 로고
    • An in vitro model to test the contribution of advanced glycation end products to bone biomechanical properties
    • DOI 10.1016/j.bone.2007.08.046, PII S8756328207006771
    • Viguet-Carrin S, Farlay D, Bala Y, Munoz F, Bouxsein ML, Delmas PD (2008) An in vitro model to test the contribution of advanced glycation end products to bone biomechanical properties. Bone 42:139-149 (Pubitemid 350302015)
    • (2008) Bone , vol.42 , Issue.1 , pp. 139-149
    • Viguet-Carrin, S.1    Farlay, D.2    Bala, Y.3    Munoz, F.4    Bouxsein, M.L.5    Delmas, P.D.6
  • 19
    • 32844468206 scopus 로고    scopus 로고
    • Extracellular post-translational modifications of collagen are major determinants of biomechanical properties of fetal bovine cortical bone
    • DOI 10.1016/j.bone.2005.09.014, PII S8756328205003856
    • Garnero P, Borel O, Gineyts E, Duboeuf F, Solberg H, Bouxsein ML, Christiansen C, Delmas PD (2006) Extracellular posttranslational modifications of collagen are major determinants of biomechanical properties of fetal bovine cortical bone. Bone 38:300-309 (Pubitemid 43255423)
    • (2006) Bone , vol.38 , Issue.3 , pp. 300-309
    • Garnero, P.1    Borel, O.2    Gineyts, E.3    Duboeuf, F.4    Solberg, H.5    Bouxsein, M.L.6    Christiansen, C.7    Delmas, P.D.8
  • 21
    • 0029809357 scopus 로고    scopus 로고
    • Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency
    • Gelb BD, Shi GP, Chapman HA, Desnick RJ (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
  • 25
    • 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, Bromme D, Buttle DJ, Croucher LJ, Hollander AP (1998) Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix. Biochem J 331(Pt 3):727-732 (Pubitemid 28211893)
    • (1998) Biochemical Journal , vol.331 , Issue.3 , pp. 727-732
    • Kafienah, W.1    Bromme, D.2    Buttle, D.J.3    Croucher, L.J.4    Hollander, A.P.5
  • 28
    • 0023882543 scopus 로고
    • Microelectrode studies on the acid microenvironment beneath adherent macrophages and osteoclasts
    • Silver IA, Murrills RJ, Etherington DJ (1988) Microelectrode studies on the acid microenvironment beneath adherent macrophages and osteoclasts. Exp Cell Res 175:266-276
    • (1988) Exp Cell Res , vol.175 , pp. 266-276
    • Silver, I.A.1    Murrills, R.J.2    Etherington, D.J.3
  • 29
    • 0037047275 scopus 로고    scopus 로고
    • Collagenase activity of cathepsin Kdepends on complex formation with chondroitin sulfate
    • Li Z, Hou WS, Escalante-Torres CR, Gelb BD, Bromme D (2002) Collagenase activity of cathepsin Kdepends 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    Bromme, D.5
  • 31
    • 57549088847 scopus 로고    scopus 로고
    • Simple and sensitive method for quantification of fluorescent enzymatic mature and senescent cross-links of collagen in bone hydrolysate using single-column high performance liquid chromatography
    • Viguet-Carrin S, Gineyts E, Bertholon C, Delmas PD (2009) Simple and sensitive method for quantification of fluorescent enzymatic mature and senescent cross-links of collagen in bone hydrolysate using single-column high performance liquid chromatography. J Chromatogr B Analyt Technol Biomed Life Sci 877:1-7
    • (2009) J Chromatogr B Analyt Technol Biomed Life Sci , vol.877 , pp. 1-7
    • Viguet-Carrin, S.1    Gineyts, E.2    Bertholon, C.3    Delmas, P.D.4
  • 32
    • 3042730990 scopus 로고    scopus 로고
    • An immunoassay for measuring fragments of newly synthesized collagen type I produced during metastatic invasion of bone
    • Cloos PA, Lyubimova N, Solberg H, Qvist P, Christiansen C, Byrjalsen I, Christgau S (2004) An immunoassay for measuring fragments of newly synthesized collagen type I produced during metastatic invasion of bone. Clin Lab 50:279-289 (Pubitemid 38877727)
    • (2004) Clinical Laboratory , vol.50 , Issue.5-6 , pp. 279-289
    • Cloos, P.A.C.1    Lyubimova, N.2    Solberg, H.3    Qvist, P.4    Christiansen, C.5    Byrjalsen, I.6    Christgau, S.7
  • 33
    • 0031282594 scopus 로고    scopus 로고
    • A simplified measurement of degraded collagen in tissues: Application in healthy, fibrillated and osteoarthritic cartilage
    • DOI 10.1016/S0945-053X(97)90012-3
    • Bank RA, Krikken M, Beekman B, Stoop R, Maroudas A, Lafeber FP, te Koppele JM (1997) A simplified measurement of degraded collagen in tissues: application in healthy, fibrillated and osteoarthritic cartilage. Matrix Biol 16:233-243 (Pubitemid 27503810)
    • (1997) Matrix Biology , vol.16 , Issue.5 , pp. 233-243
    • Bank, R.A.1    Krikken, M.2    Beekman, B.3    Stoop, R.4    Maroudas, A.5    Lafebers, F.P.J.G.6    Te, K.J.M.7
  • 35
    • 84889703933 scopus 로고    scopus 로고
    • Type I collagen isomerization (alpha/beta CTX ratio) and risk of clinical vertebral fracture in men: A prospective study. ASBMR 2010 Annual Meeting
    • Bauer D, Garnero P, Harrson SL, Cauley J, Eastell R, Orwoll E (2010) Type I collagen isomerization (alpha/beta CTX ratio) and risk of clinical vertebral fracture in men: a prospective study. ASBMR 2010 Annual Meeting. J Bone Miner Res 25 (Suppl 1):S8
    • (2010) J Bone Miner Res , vol.25 , Issue.SUPPL. 1
    • Bauer, D.1    Garnero, P.2    Harrson, S.L.3    Cauley, J.4    Eastell, R.5    Orwoll, E.6
  • 36
    • 0034711762 scopus 로고    scopus 로고
    • Collagenolytic activity of cathepsin K is specifically modulated by cartilage-resident chondroitin sulfates
    • DOI 10.1021/bi992251u
    • Li Z, Hou WS, Bromme D (2000) Collagenolytic activity of cathepsin K is specifically modulated by cartilage-resident chondroitin sulfates. Biochemistry 39:529-536 (Pubitemid 30077626)
    • (2000) Biochemistry , vol.39 , Issue.3 , pp. 529-536
    • Li, Z.1    Hou, W.-S.2    Bromme, D.3
  • 37
    • 76549123888 scopus 로고    scopus 로고
    • Collagen cross-links as a determinant of bone quality: A possible explanation for bone fragility in aging, osteoporosis, and diabetes mellitus
    • Saito M, Marumo K (2010) Collagen cross-links as a determinant of bone quality: a possible explanation for bone fragility in aging, osteoporosis, and diabetes mellitus. Osteoporos Int 21:195-214
    • (2010) Osteoporos Int , vol.21 , pp. 195-214
    • Saito, M.1    Marumo, K.2
  • 39
    • 0032401898 scopus 로고    scopus 로고
    • Mechanisms of maturation and ageing of collagen
    • DOI 10.1016/S0047-6374(98)00119-5, PII S0047637498001195
    • Bailey AJ, Paul RG, Knott L (1998) Mechanisms of maturation and ageing of collagen. Mech Ageing Dev 106:1-56 (Pubitemid 28559274)
    • (1998) Mechanisms of Ageing and Development , vol.106 , Issue.1-2 , pp. 1-56
    • Bailey, A.J.1    Paul, R.G.2    Knott, L.3
  • 40
    • 0033969472 scopus 로고    scopus 로고
    • Proteolysis of human bone collagen by cathepsin K: Characterization of the cleavage sites generating the cross-linked N-telopeptide neoepitope
    • DOI 10.1016/S8756-3282(99)00270-7, PII S8756328299002707
    • Atley LM, Mort JS, Lalumiere M, Eyre DR (2000) Proteolysis of human bone collagen by cathepsin K: characterization of the cleavage sites generating by cross-linked N-telopeptide neoepitope. Bone 26:241-247 (Pubitemid 30101647)
    • (2000) Bone , vol.26 , Issue.3 , pp. 241-247
    • Atley, L.M.1    Mort, J.S.2    Lalumiere, M.3    Eyre, D.R.4
  • 41
    • 0034012685 scopus 로고    scopus 로고
    • Immunochemical characterization of assay for carboxyterminal telopeptide of human type I collagen: loss of antigenicity by treatment with cathepsin K
    • DOI 10.1016/S8756-3282(00)00235-0, PII S8756328200002350
    • Sassi ML, Eriksen H, Risteli L, Niemi S, Mansell J, Gowen M, Risteli J (2000) Immunochemical characterization of assay for carboxyterminal telopeptide of human type I collagen: loss of antigenicity by treatment with cathepsin K. Bone 26:367-373 (Pubitemid 30136127)
    • (2000) Bone , vol.26 , Issue.4 , pp. 367-373
    • Sassi, M.-L.1    Eriksen, H.2    Risteli, L.3    Niemi, S.4    Mansell, J.5    Gowen, M.6    Risteli, J.7
  • 42
    • 0033545896 scopus 로고    scopus 로고
    • Rapid release and unusual stability of immunodominant peptide 45-89 from citrullinated myelin basic protein
    • Cao L, Goodin R, Wood D, Moscarello MA, Whitaker JN (1999) Rapid release and unusual stability of immunodominant peptide 45-89 from citrullinated myelin basic protein. Biochemistry 38:6157-6163
    • (1999) Biochemistry , vol.38 , pp. 6157-6163
    • Cao, L.1    Goodin, R.2    Wood, D.3    Moscarello, M.A.4    Whitaker, J.N.5
  • 43
    • 0034625091 scopus 로고    scopus 로고
    • Deimination of myelin basic protein. 1. Effect of deimination of arginyl residues of myelin basic protein on its structure and susceptibility to digestion by cathepsin D
    • DOI 10.1021/bi9925569
    • Pritzker LB, Joshi S, Gowan JJ, Harauz G, Moscarello MA (2000) Deimination of myelin basic protein. 1. Effect of deimination of arginyl residues of myelin basic protein on its structure and susceptibility to digestion by cathepsin D. Biochemistry 39:5374-5381 (Pubitemid 30257077)
    • (2000) Biochemistry , vol.39 , Issue.18 , pp. 5374-5381
    • Pritzker, L.B.1    Joshi, S.2    Gowan, J.J.3    Harauz, G.4    Moscarello, M.A.5
  • 44
    • 79955825984 scopus 로고    scopus 로고
    • Cellular mechanisms of bone remodeling
    • Eriksen EF (2010) Cellular mechanisms of bone remodeling. Rev Endocr Metab Disord 11:219-227
    • (2010) Rev Endocr Metab Disord , vol.11 , pp. 219-227
    • Eriksen, E.F.1
  • 45
    • 0030763499 scopus 로고    scopus 로고
    • Decreased beta-isomerization of the C-terminal telopeptide of type I collagen alpha1 chain in Paget's disease of bone
    • DOI 10.1359/jbmr.1997.12.9.1407
    • Garnero P, Fledelius C, Gineyts E, Serre CM, Vignot E, Delmas PD (1997) Decreased beta-isomerization of the C-terminal telopeptide of type I collagen alpha 1 chain in Paget's disease of bone. J Bone Miner Res 12:1407-1415 (Pubitemid 27375383)
    • (1997) Journal of Bone and Mineral Research , vol.12 , Issue.9 , pp. 1407-1415
    • Garnero, P.1    Fledelius, C.2    Gineyts, E.3    Serre, C.-M.4    Vignot, E.5    Delmas, P.D.6


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