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Volumn 10, Issue 2, 2012, Pages 141-150

Effects of bone matrix proteins on fracture and fragility in osteoporosis

Author keywords

Collagens; Extracellular bone matrix; Fragility fractures; Glycation; Noncollagenous proteins; Osteoporosis

Indexed keywords

BONE SIALOPROTEIN; COLLAGEN; COLLAGEN TYPE 1; COLLAGEN TYPE 3; COLLAGEN TYPE 5; COLLAGEN TYPE 6; DENTIN SIALOPHOSPHOPROTEIN; FIBRILLIN; FIBRONECTIN; MATRIX EXTRACELLULAR PHOSPHOGLYCOPROTEIN; MATRIX PROTEIN; NONCOLLAGENOUS PROTEIN; OSTEOCALCIN; OSTEONECTIN; OSTEOPONTIN; THROMBOSPONDIN 2; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG;

EID: 84865745554     PISSN: 15441873     EISSN: 15442241     Source Type: Journal    
DOI: 10.1007/s11914-012-0103-6     Document Type: Article
Times cited : (142)

References (98)
  • 1
    • 0141499870 scopus 로고    scopus 로고
    • Bone matrix proteins: Their function, regulation, and relationship to osteoporosis
    • Young MF. Bone matrix proteins: their function, regulation, and relationship to osteoporosis. Osteoporos Int. 2003;14 Suppl 3: S35-42.
    • (2003) Osteoporos Int. , vol.14 , Issue.SUPPL. 3
    • Young, M.F.1
  • 3
    • 0027274694 scopus 로고
    • When bone mass fails to predict bone failure
    • Ott SM. When bone mass fails to predict bone failure. Calcif Tissue Int. 1993;53:S7-S13. (Pubitemid 23277161)
    • (1993) Calcified Tissue International , vol.53 , Issue.SUPPL. 1
    • Ott, S.M.1
  • 4
    • 77957657154 scopus 로고    scopus 로고
    • Atypical fractures as a potential complication of long-termbisphosphonate therapy
    • Sellmeyer DE. Atypical fractures as a potential complication of long-termbisphosphonate therapy. J Am Med Assoc. 2010;304: 1480-3.
    • (2010) J Am Med Assoc. , vol.304 , pp. 1480-1483
    • Sellmeyer, D.E.1
  • 5
    • 80053525537 scopus 로고    scopus 로고
    • Long-term bisphosphonate usage and subtrochanteric insuffciency fractures: A cause for concern?
    • Yoon RS, Hwang JS, Beebe K. Long-term bisphosphonate usage and subtrochanteric insuffciency fractures: a cause for concern? J Bone Joint Surg Br. 2011;93:1289-95.
    • (2011) J Bone Joint Surg Br. , vol.93 , pp. 1289-1295
    • Yoon, R.S.1    Hwang, J.S.2    Beebe, K.3
  • 6
    • 84856133414 scopus 로고    scopus 로고
    • Evolution of bisphosphonate related atypical fracture retrospectively observed with DXA scanning
    • Ahlman MA, Rissing MS, Gordon L. Evolution of bisphosphonate related atypical fracture retrospectively observed with DXA scanning. J Bone Miner Res. 2012;27(2):496-8.
    • (2012) J Bone Miner Res. , vol.27 , Issue.2 , pp. 496-498
    • Ahlman, M.A.1    Rissing, M.S.2    Gordon, L.3
  • 8
    • 1942445379 scopus 로고    scopus 로고
    • Rising crack-growth-resistance behavior in cortical bone: Implications for toughness measurements
    • DOI 10.1016/j.jbiomech.2003.11.003, PII S0021929003004044
    • Vashishth D. Rising crack growth resistance behavior in cortical bone: Implications for toughness measurements. J Biomech. 2004;37(10):943-6. (Pubitemid 38521217)
    • (2004) Journal of Biomechanics , vol.37 , Issue.6 , pp. 943-946
    • Vashishth, D.1
  • 9
    • 33744974111 scopus 로고    scopus 로고
    • Reductions in degree of mineralization and enzymatic collagen cross-links and increases in glycation-induced pentosidine in the femoral neck cortex in cases of femoral neck fracture
    • DOI 10.1007/s00198-006-0087-0
    • Saito M, Fujii K, Soshi S, Tanaka T. Reductions in degree of mineralization and enzymatic collagen cross-links and increases in glycation-induced pentosidine in the femoral neck cortex in cases of femoral neck fracture. Osteoporos Int. 2006;17(7):986-95. (Pubitemid 43864852)
    • (2006) Osteoporosis International , vol.17 , Issue.7 , pp. 986-995
    • Saito, M.1    Fujii, K.2    Soshi, S.3    Tanaka, T.4
  • 10
    • 34250790094 scopus 로고    scopus 로고
    • The role of the collagen matrix in skeletal fragility
    • Vashishth D. The role of the collagen matrix in skeletal fragility. Curr Osteoporos Rep. 2007;5(2):62-6. (Pubitemid 46954743)
    • (2007) Current Osteoporosis Reports , vol.5 , Issue.2 , pp. 62-66
    • Vashishth, D.1
  • 11
    • 67349105623 scopus 로고    scopus 로고
    • Changes in non-enzymatic glycation and its association with altered mechanical properties following 1-year treatment with risedronate or alendronate
    • Tang SY, Allen MR, Phipps R, et al. Changes in non-enzymatic glycation and its association with altered mechanical properties following 1-year treatment with risedronate or alendronate. Osteoporosis Int. 2009;20(6):887-94.
    • (2009) Osteoporosis Int. , vol.20 , Issue.6 , pp. 887-894
    • Tang, S.Y.1    Allen, M.R.2    Phipps, R.3
  • 12
    • 34247197697 scopus 로고    scopus 로고
    • Alterations of cortical and trabecular architecture are associated with fractures in postmenopausal women, partially independent of decreased BMD measured by DXA: The OFELY study
    • DOI 10.1359/jbmr.061206
    • Sornay-Rendu E, Boutroy S, Munoz F, Delmas PD. Alterations of cortical and trabecular architecture are associated with fractures in postmenopausal women, partially independent of decreased BMD measured by DXA: the OFELY study. J Bone Miner Res. 2007;22 (3):425-33. (Pubitemid 46797126)
    • (2007) Journal of Bone and Mineral Research , vol.22 , Issue.3 , pp. 425-433
    • Sornay-Rendu, E.1    Boutroy, S.2    Munoz, F.3    Delmas, P.D.4
  • 13
    • 72449177328 scopus 로고    scopus 로고
    • Matricellular proteins: An overview
    • Bornstein P. Matricellular proteins: an overview. J Cell Commun Signal. 2009;3:163-5.
    • (2009) J Cell Commun Signal. , vol.3 , pp. 163-165
    • Bornstein, P.1
  • 14
    • 85003186936 scopus 로고
    • Transforming growth factor-beta gene family members and bone
    • Centrella M, Horowitz MC, Wozney JM, et al. Transforming growth factor-beta gene family members and bone. Endocr Rev. 1994;15:27-39.
    • (1994) Endocr Rev. , vol.15 , pp. 27-39
    • Centrella, M.1    Horowitz, M.C.2    Wozney, J.M.3
  • 15
    • 0024355048 scopus 로고
    • Insulin-like growth factors I and II. Peptide, messenger ribonucleic acid and gene structures, serum, and tissue concentrations
    • Daughaday W, Rotwein P. Insulin-like growth factors I and II. Peptide, messenger ribonucleic acid and gene structures, serum, and tissue concentrations. Endocr Rev. 1989;10(1):68-91. (Pubitemid 19156368)
    • (1989) Endocrine Reviews , vol.10 , Issue.1 , pp. 68-91
    • Daughaday, W.H.1    Rotwein, P.2
  • 16
    • 0028958031 scopus 로고
    • Insulin-like growth factors and their binding proteins: Biological actions
    • Jones JI, Clemmons DR. Insulin-like growth factors and their binding proteins: biological actions. Endocr Rev. 1995;16(1): 3-34.
    • (1995) Endocr Rev. , vol.16 , Issue.1 , pp. 3-34
    • Jones, J.I.1    Clemmons, D.R.2
  • 17
    • 79151473137 scopus 로고    scopus 로고
    • Bone morphogenetic proteins: A critical review
    • Bragdon B, Moseychuk O, Saldanha S, et al. Bone morphogenetic proteins: a critical review. Cell Signal. 2011;23:609-20.
    • (2011) Cell Signal. , vol.23 , pp. 609-620
    • Bragdon, B.1    Moseychuk, O.2    Saldanha, S.3
  • 18
    • 0028799672 scopus 로고
    • Calcitonin down-regulates immediate cell signals induced in human osteoclast-like cells by the bone sialoprotein-HA fragment through a post-integrin receptor mechanism
    • Pannicia R, Riccioni T, Zani BM, et al. calcitonin down-regulates immediate cell signals induced in human osteoclast-like cells by the bone sialoprotein-HA fragment through a post-integrin receptor mechanism. Endocrinology. 1995;136:1177-86.
    • (1995) Endocrinology , vol.136 , pp. 1177-1186
    • Pannicia, R.1    Riccioni, T.2    Zani, B.M.3
  • 19
    • 0028600614 scopus 로고
    • Bone matrix decorin binds transforming growth factor-beta and enhances its bioactivity
    • Takeuchi Y, Kodama Y, Matsumoto T. Bone matrix decorin binds transforming growth factor-beta and enhances its bioactivity J Biol Chem. 1994;269:32634-8.
    • (1994) J Biol Chem. , vol.269 , pp. 32634-32638
    • Takeuchi, Y.1    Kodama, Y.2    Matsumoto, T.3
  • 20
    • 0029874137 scopus 로고    scopus 로고
    • Antagonistic effects of transforming growth factor-beta on vitamin D3 enhancement of osteocalcin and osteopontin transcription: Reduced interactions of vitamin D receptor/retinoid X receptor complexes with vitamin E response elements
    • Staal A, Van Wijnen AJ, Desai RK, et al. Antagonistic effects of transforming growth factor-beta on vitamin D3 enhancement of osteocalcin and osteopontin transcription: reduced interactions of vitamin D receptor/retinoid X receptor complexes with vitamin E response elements. Endocrinology. 1996;137(5):2001-11.
    • (1996) Endocrinology , vol.137 , Issue.5 , pp. 2001-2011
    • Staal, A.1    Van Wijnen, A.J.2    Desai, R.K.3
  • 21
    • 0026071008 scopus 로고
    • Human bone contains type III collagen, type VI collagen, and fibrillin: Type III collagen is present onspecific fibers that may mediate attachment of tendons, ligaments, and periosteum to calcified bone cortex
    • Keene DR, Sakai LY, Burgeson RE. Human bone contains type III collagen, type VI collagen, and fibrillin: type III collagen is present onspecific fibers that may mediate attachment of tendons, ligaments, and periosteum to calcified bone cortex. J Histochem Cytochem. 1991;39(1):59-69.
    • (1991) J Histochem Cytochem. , vol.39 , Issue.1 , pp. 59-69
    • Keene, D.R.1    Sakai, L.Y.2    Burgeson, R.E.3
  • 22
    • 65549135176 scopus 로고    scopus 로고
    • Differences in chain usage and cross-linking specificities of cartilage type V/XI collagen isoforms with age and tissue
    • Wu JJ, Weis MA, Kim LS, et al. Differences in chain usage and cross-linking specificities of cartilage type V/XI collagen isoforms with age and tissue. J Biol Chem. 2009;284:5539-45.
    • (2009) J Biol Chem. , vol.284 , pp. 5539-5545
    • Wu, J.J.1    Weis, M.A.2    Kim, L.S.3
  • 23
    • 84855846948 scopus 로고    scopus 로고
    • A model for the ultrastructure of bone based on electron microscopy of ionmilled sections
    • doi:10.1371/journal. pone.0029258
    • McNally A, Henry Schwarcz HP, Botton GA et al.: A model for the ultrastructure of bone based on electron microscopy of ionmilled sections. PLoS One 7(1):e29258. doi:10.1371/journal. pone.0029258.
    • PLoS One , vol.7 , Issue.1
    • McNally, A.1    Henry Schwarcz, H.P.2    Botton, G.A.3
  • 25
    • 78049427279 scopus 로고    scopus 로고
    • Assembly of fibronectin extracellular matrix
    • doi:10.1146/annurev-cellbio-100109-104020
    • Singh P, Carraher C, Schwarzbauer JE. Assembly of fibronectin extracellular matrix. Annu Rev Cell Dev Biol. 2010;26:397-419. doi:10.1146/annurev-cellbio-100109-104020.
    • (2010) Annu Rev Cell Dev Biol. , vol.26 , pp. 397-419
    • Singh, P.1    Carraher, C.2    Schwarzbauer, J.E.3
  • 26
    • 8444247525 scopus 로고    scopus 로고
    • Laminin functions in tissue morphogenesis
    • DOI 10.1146/annurev.cellbio.20.010403.094555
    • Miner JH, Yurchenco PD. Laminin functions in tissue morphogenesis. Annu Rev Cell Dev Biol. 2004;20:255-84. doi:10.1146/annurev.cellbio.20.010403.094555. (Pubitemid 39488639)
    • (2004) Annual Review of Cell and Developmental Biology , vol.20 , pp. 255-284
    • Miner, J.H.1    Yurchenco, P.D.2
  • 27
    • 72449128021 scopus 로고    scopus 로고
    • doi:10.1007/s00441-009-0838-2
    • Durbeej M. Laminins. Cell Tissue Res. 2010;339(1):259-68. doi: 10.1007/s00441-009-0838-2.
    • (2010) Cell Tissue Res. , vol.339 , Issue.1 , pp. 259-268
    • Laminins, D.M.1
  • 28
    • 34547631499 scopus 로고    scopus 로고
    • Proteoglycans: Key partners in bone cell biology
    • DOI 10.1002/bies.20612
    • Lamoureux F, Baud'huin M, Duplomb L, et al. Proteoglycans: key partners in bone cell biology. Bioessays. 2007;29(8):758-71. (Pubitemid 47204281)
    • (2007) BioEssays , vol.29 , Issue.8 , pp. 758-771
    • Lamoureux, F.1    Baud'huin, M.2    Duplomb, L.3    Heymann, D.4    Redini, F.5
  • 29
    • 2942752227 scopus 로고    scopus 로고
    • Integrins as linker proteins between osteoblasts and bone replacing materials. A critical review
    • DOI 10.1016/j.biomaterials.2004.02.021, PII S0142961204001607
    • Siebers MC, ter Brugge PJ, Walboomers XF, et al. Integrins as linker proteins between osteoblasts and bone replacing materials. A critical review. Biomaterials. 2005;26(2):137-46. (Pubitemid 38789096)
    • (2005) Biomaterials , vol.26 , Issue.2 , pp. 137-146
    • Siebers, M.C.1    Ter Brugge, P.J.2    Walboomers, X.F.3    Jansen, J.A.4
  • 30
    • 0024371484 scopus 로고
    • Binding of heparin sulfate to type V collagen
    • LeBaron RG, Höök A, Esko JD, et al. Binding of heparin sulfate to type V collagen. J Biol Chem. 1989;264:7950-6.
    • (1989) J Biol Chem. , vol.264 , pp. 7950-7956
    • LeBaron, R.G.1    Höök, A.2    Esko, J.D.3
  • 31
    • 0033870125 scopus 로고    scopus 로고
    • In vitro studies of insulin-like growth factor I and bone
    • Conover CA. In vitro studies of insulin-like growth factor I and bone. Growth Horm IGF Res. 2000;Supplement B:S107-10. (Pubitemid 30637226)
    • (2000) Growth Hormone and IGF Research , vol.10 , Issue.SUPPL. B
    • Conover, C.A.1
  • 32
    • 0030443454 scopus 로고    scopus 로고
    • Regulation and physiological role of insulin-like growth factor binding proteins
    • Conover CA. Regulation and physiological role of insulin-like growth factor binding proteins. Endocr J. 1996;43(Suppl): S43-8. (Pubitemid 27014287)
    • (1996) Endocrine Journal , vol.43 , Issue.SUPPL.
    • Conover, C.A.1
  • 33
    • 67650717476 scopus 로고    scopus 로고
    • The biology of activin: Recent advances in structure, regulation and function
    • Xia Y, Schneyer AL. The biology of activin: recent advances in structure, regulation and function. J Endocrinol. 2009;202:1-12.
    • (2009) J Endocrinol. , vol.202 , pp. 1-12
    • Xia, Y.1    Schneyer, A.L.2
  • 34
    • 84857033273 scopus 로고    scopus 로고
    • When versatility matters: Activins/inhibins as key regulators of immunity
    • doi:10.1038/icb.2011.32
    • Aleman-Muench GR, Soldevila G. When versatility matters: activins/inhibins as key regulators of immunity. Immunol Cell Biol. 2012;90:137-48. doi:10.1038/icb.2011.32.
    • (2012) Immunol Cell Biol. , vol.90 , pp. 137-48
    • Aleman-Muench, G.R.1    Soldevila, G.2
  • 35
    • 32544458177 scopus 로고    scopus 로고
    • Anti-Müllerian hormone: A new marker for ovarian function
    • DOI 10.1530/rep.1.00529
    • Jenny A, Visser JA, de Jong FH, Laven JSE, et al. Anti-Müllerian hormone: a new marker for ovarian function. Reproduction. 2006;131:1-9. doi:rep.1.00529/rep.1.00529. (Pubitemid 43230697)
    • (2006) Reproduction , vol.131 , Issue.1 , pp. 1-9
    • Visser, J.A.1    De Jong, F.H.2    Laven, J.S.E.3    Themmen, A.P.N.4
  • 36
    • 84861330616 scopus 로고    scopus 로고
    • Anti-Müllerian hormone: An ovarian reserve marker in primary ovarian insufficiency
    • doi:10.1038/nrendo.2011.224
    • Visser JA, Schipper I, Laven JSE, et al.: Anti-Müllerian hormone: an ovarian reserve marker in primary ovarian insufficiency. Nat Rev Endocrinol. 2012: doi:10.1038/nrendo.2011.224
    • (2012) Nat Rev Endocrinol.
    • Visser, J.A.1    Schipper, I.2    Laven, J.S.E.3
  • 37
    • 0020576560 scopus 로고
    • Transforming growth factor-β in human platelets. Identification of a major storage site, purification, and characterization
    • Assoian RK, Komoriya A, Meyers CA, et al. Transforming growth factor-β in human platelets. Identification of a major storage site, purification, and characterization. J Biol Chem. 1983;258:7155-60. (Pubitemid 13059967)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.11 , pp. 7155-7160
    • Assoian, R.K.1    Komoriya, A.2    Meyers, C.A.3
  • 40
    • 2342488852 scopus 로고    scopus 로고
    • New insights into TGF-β-Smad signalling
    • ten Dijke P, Hill CS. New insights into TGF-β-Smad signalling. Trends Biochem Sci. 2004;29:265-73.
    • (2004) Trends Biochem Sci. , vol.29 , pp. 265-273
    • Ten Dijke, P.1    Hill, C.S.2
  • 41
    • 0034813396 scopus 로고    scopus 로고
    • The loss of Smad3 results in a lower rate of bone formation and osteopenia through dysregulation of osteoblast differentiation and apoptosis
    • Borton AJ, Frederick JP, Datto MB, et al. The loss of Smad3 results in a lower rate of bone formation and osteopenia through dysregulation of osteoblast differentiation and apoptosis. J Bone Miner Res. 2001;16:1754-64. (Pubitemid 32911480)
    • (2001) Journal of Bone and Mineral Research , vol.16 , Issue.10 , pp. 1754-1764
    • Borton, A.J.1    Frederick, J.P.2    Datto, M.B.3    Wang, X.-F.4    Weinstein, R.S.5
  • 42
    • 26444506000 scopus 로고    scopus 로고
    • Transforming growth factor-β1 to the bone
    • Janssens K, ten Dijke P, Janssens S, et al. Transforming growth factor-β1 to the bone. Endocr Rev. 2005;26(6):743-74.
    • (2005) Endocr Rev. , vol.26 , Issue.6 , pp. 743-774
    • Janssens, K.1    Ten Dijke, P.2    Janssens, S.3
  • 44
    • 0032710016 scopus 로고    scopus 로고
    • Inhibition of TGF-β receptor signaling in osteoblasts leads to decreased bone remodeling and increased trabecular bone mass
    • Filvaroff E, Erlebacher A, Ye J, et al. Inhibition of TGF-beta receptor signaling in osteoblasts leads to decreased bone remodeling and increased trabecular bone mass. Development (Cambridge, UK). 1999;126:4267-79. (Pubitemid 29509342)
    • (1999) Development , vol.126 , Issue.19 , pp. 4267-4279
    • Filvaroff, E.1    Erlebacher, A.2    Ye, J.-Q.3    Gitelman, S.E.4    Lotz, J.5    Heillman, M.6    Derynck, R.7
  • 51
    • 0030160527 scopus 로고    scopus 로고
    • Osteopontin deposition in remodeling bone: An osteoblast mediated event
    • McKee MD, Nanci A. Osteopontin deposition in remodeling bone: an osteoblast mediated event. J Bone Miner Res. 1996;11:873-4.
    • (1996) J Bone Miner Res. , vol.11 , pp. 873-874
    • McKee, M.D.1    Nanci, A.2
  • 55
    • 34548165105 scopus 로고    scopus 로고
    • Nanoscale ion mediated networks in bone: Osteopontin can repeatedly dissipate large amounts of energy
    • DOI 10.1021/nl0712769
    • Fantner GE, Adams J, Turner P, et al. Nanoscale ion mediated networks in bone: osteopontin can repeatedly dissipate large amounts of energy. Nano Lett. 2007;7:2491-8. (Pubitemid 47310151)
    • (2007) Nano Letters , vol.7 , Issue.8 , pp. 2491-2498
    • Fantner, G.E.1    Adams, J.2    Turner, P.3    Thurner, P.J.4    Fisher, L.W.5    Hansma, P.K.6
  • 56
    • 80052287509 scopus 로고    scopus 로고
    • Biochemical characterization of major bone-matrix proteins using nanoscale-size bone samples and proteomics methodology
    • doi:10.1074/mcp.M110.006718
    • Sroga GE, Karim L, Colón W, Vashishth D. Biochemical characterization of major bone-matrix proteins using nanoscale-size bone samples and proteomics methodology. Mol Cell Proteomics. 2011;10(9):1-12. doi:10.1074/mcp.M110.006718.
    • (2011) Mol Cell Proteomics , vol.10 , Issue.9 , pp. 1-12
    • Sroga, G.E.1    Karim, L.2    Colón, W.3    Vashishth, D.4
  • 57
    • 77953022873 scopus 로고    scopus 로고
    • Osteopontin deficiency increases bone fragility but preserves bone mass
    • Thurner PJ, Chen CG, Ionova-Martin S, et al. Osteopontin deficiency increases bone fragility but preserves bone mass. Bone. 2010;46:1564-73.
    • (2010) Bone , vol.46 , pp. 1564-1573
    • Thurner, P.J.1    Chen, C.G.2    Ionova-Martin, S.3
  • 58
    • 0025110930 scopus 로고
    • Different pattern of alkaline phosphatase, osteopontin, and osteocalcin expression in developing rat bone visualized by in situ hybridization
    • Weinreb M, Shinar D, Rodan GA. Different pattern of alkaline phosphatase, osteopontin, and osteoealcin expression in developing rat bone visualized by in situ hybridization. J Bone Miner Res. 1990;5:831-42. (Pubitemid 20294767)
    • (1990) Journal of Bone and Mineral Research , vol.5 , Issue.8 , pp. 831-842
    • Weinreb, M.1    Shinar, D.2    Rodan, G.A.3
  • 59
    • 0025652108 scopus 로고
    • Localization of endogenous osteocalcin in neonatal rat bone and its absence in articular cartilage: Effect of warfarin treatment
    • Boivin G, Morel G, Lian JB, et al. Localization of endogenous osteocalcin in neonatal rat bone and its absence in articular cartilage: effect of warfarin treatment. Virchows Arch A Pathol Anat. 1990;417:505-12.
    • (1990) Virchows Arch a Pathol Anat. , vol.417 , pp. 505-512
    • Boivin, G.1    Morel, G.2    Lian, J.B.3
  • 61
    • 35648934023 scopus 로고    scopus 로고
    • Control of osteopontin signaling and function by post-translational phosphorylation and protein folding
    • DOI 10.1002/jcb.21558
    • Kazanecki CC, Uzwiak DJ, Denhardt DT. Control of osteopontin signaling and function by post-translational phosphorylation and protein folding. J Cell Biochem. 2007;102:912-24. (Pubitemid 350036931)
    • (2007) Journal of Cellular Biochemistry , vol.102 , Issue.4 , pp. 912-924
    • Kazanecki, C.C.1    Uzwiak, D.J.2    Denhardt, D.T.3
  • 62
    • 0019785123 scopus 로고
    • Osteonectin, a bone-specific protein linking mineral to collagen
    • Termine JD, Kleinman HK, Whitson SW, et al. Osteonectin, a bone-specific protein linking mineral to collagen. Cell. 1981;26 (10, 1 Pt 1):99-105. (Pubitemid 12229368)
    • (1981) Cell , vol.26 , Issue.1 , pp. 99-105
    • Termine, J.D.1    Kleinman, H.K.2    Whitson, S.W.3
  • 64
    • 0026700932 scopus 로고
    • Structure, expression, and regulation of the major noncollagenous matrix proteins of bone
    • Young MF, Kerr JM, Ibaraki K, et al. Structure, expression, and regulation of the major noncollagenous matrix proteins of bone. Clin Orthop. 1992;281:275-94.
    • (1992) Clin Orthop. , vol.281 , pp. 275-294
    • Young, M.F.1    Kerr, J.M.2    Ibaraki, K.3
  • 65
    • 23444459571 scopus 로고
    • The biology of SPARC, a protein that modulates cell-matrix interactions
    • Lane TF, Sage EH. The biology of SPARC, a protein that modulated cell-matrix interactions. FASEB J. 1994;8:163-73. (Pubitemid 24067139)
    • (1994) FASEB Journal , vol.8 , Issue.2 , pp. 163-173
    • Lane, T.F.1    Helene Sage, E.2
  • 67
    • 0027297962 scopus 로고
    • SPARC, a secreted protein associated with morphogenesis and tissue remodeling, induces expression of metalloproteinases in fibroblasts through a novel extracellular matrix-dependent pathway
    • Tremble PM, Lane TF, Sage EH, Werb Z. SPARC, a secreted protein associated with morphogenesis and tissue remodeling, induces expression of metalloproteinases in fibroblasts through a novel extracellular matrix-dependent pathway. J Cell Biol. 1993;121:1433-44. (Pubitemid 23174558)
    • (1993) Journal of Cell Biology , vol.121 , Issue.6 , pp. 1433-1444
    • Tremble, P.M.1    Lane, T.F.2    Sage, E.H.3    Werb, Z.4
  • 68
    • 0026723390 scopus 로고
    • Immunological screening of SPARC/Osteonectin in nonmineralized tissues
    • Maillard C, Malaval L, Delmas PD. Immunological screening of SPARC/Osteonectin in nonmineralized tissues. Bone. 1992;13 (3):257-64.
    • (1992) Bone , vol.13 , Issue.3 , pp. 257-264
    • Maillard, C.1    Malaval, L.2    Delmas, P.D.3
  • 69
    • 0024780540 scopus 로고
    • The nature and significance of osteopontin
    • Butler W. The nature and significance of osteopontin. Connect Tiss Res. 1989;23:123-36.
    • (1989) Connect Tiss Res. , vol.23 , pp. 123-136
    • Butler, W.1
  • 75
    • 44649115131 scopus 로고    scopus 로고
    • Osteonectin/SPARC polymorphisms in Caucasian men with idiopathic osteoporosis
    • Delany AM, McMahon DJ, Powell JS, et al. Osteonectin/SPARC polymorphisms in Caucasian men with idiopathic osteoporosis. Osteoporos Int. 2008;19(7):969-78.
    • (2008) Osteoporos Int. , vol.19 , Issue.7 , pp. 969-978
    • Delany, A.M.1    McMahon, D.J.2    Powell, J.S.3
  • 76
    • 0025787103 scopus 로고
    • Morphological and biochemical studies of a mouse mutant (fro/fro) with bone fragility
    • Muriel MP, Bonaventure J, Stanescu R, et al. Morphological and biochemical studies of a mouse mutant (fro/fro) with bone fragility. Bone. 1991;12:241-8.
    • (1991) Bone , vol.12 , pp. 241-248
    • Muriel, M.P.1    Bonaventure, J.2    Stanescu, R.3
  • 77
    • 70349325817 scopus 로고    scopus 로고
    • Extracellular microfibrils: Contextual platforms for TGF-β and BMP signaling
    • Ramirez F, Rifkin DB. Extracellular microfibrils: contextual platforms for TGF-β and BMP signaling. Curr Opin Cell Biol. 2009; 21:616-22.
    • (2009) Curr Opin Cell Biol. , vol.21 , pp. 616-622
    • Ramirez, F.1    Rifkin, D.B.2
  • 78
    • 77957204548 scopus 로고    scopus 로고
    • Fibrillin-1 and -2 differentially modulate endogenous TGF-β and BMP bioavailability during bone formation
    • Nistala H, Lee-Arteaga S, Smaldone S, et al. Fibrillin-1 and -2 differentially modulate endogenous TGF-β and BMP bioavailability during bone formation. J Cell Biol. 2010;190:1107-21.
    • (2010) J Cell Biol. , vol.190 , pp. 1107-1121
    • Nistala, H.1    Lee-Arteaga, S.2    Smaldone, S.3
  • 79
    • 77957193785 scopus 로고    scopus 로고
    • Extracellular matrix in the skeleton
    • Pourquie O, editor Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Ramirez F. Extracellular matrix in the skeleton. In: Pourquie O, editor. The skeletal system. Cold Spring Harbor: Cold Spring Harbor Laboratory Press; 2009. p. 341-53.
    • (2009) The Skeletal System , pp. 341-353
    • Ramirez, F.1
  • 80
    • 77957195034 scopus 로고    scopus 로고
    • Extracellular microfibrils modulate osteoblast-supported osteoclastogenesis by restricting TGF-β stimulation of RANKL production
    • Nistala H, Lee-Arteaga S, Smaldone S, et al. Extracellular microfibrils modulate osteoblast-supported osteoclastogenesis by restricting TGF-β stimulation of RANKL production. J Biol Chem. 2010; 285:34126-33.
    • (2010) J Biol Chem. , vol.285 , pp. 34126-34133
    • Nistala, H.1    Lee-Arteaga, S.2    Smaldone, S.3
  • 81
    • 79955531352 scopus 로고    scopus 로고
    • Material and mechanical properties of bones deficient for fibrillin-1 or fibrillin-2 microfibrils
    • Arteaga-Solis E, Sui-Arteaga L, Kim M, et al. Material and mechanical properties of bones deficient for fibrillin-1 or fibrillin-2 microfibrils. Matrix Biol. 2011;30(3):188-94.
    • (2011) Matrix Biol. , vol.30 , Issue.3 , pp. 188-194
    • Arteaga-Solis, E.1    Sui-Arteaga, L.2    Kim, M.3
  • 82
    • 32844454532 scopus 로고    scopus 로고
    • Age-related change in the damage morphology of human cortical bone and its role in bone fragility
    • DOI 10.1016/j.bone.2005.09.002, PII S8756328205003789
    • Diab T, Condon KW, Burr DB, Vashishth D. Age-related change in the damage morphology of human cortical bone and its role in bone fragility. Bone. 2006;38(3):427-31. (Pubitemid 43255437)
    • (2006) Bone , vol.38 , Issue.3 , pp. 427-431
    • Diab, T.1    Condon, K.W.2    Burr, D.B.3    Vashishth, D.4
  • 83
    • 33846591373 scopus 로고    scopus 로고
    • Morphology, localization and accumulation of in vivo microdamage in human cortical bone
    • DOI 10.1016/j.bone.2006.09.027, PII S8756328206007435
    • Diab T, Vashishth D. Morphology, localization and accumulation of in vivo microdamage in human cortical bone. Bone. 2007; 40:612-8. (Pubitemid 46187218)
    • (2007) Bone , vol.40 , Issue.3 , pp. 612-618
    • Diab, T.1    Vashishth, D.2
  • 84
    • 52949099836 scopus 로고    scopus 로고
    • Microarchitecture influences microdamage accumulation in human vertebral trabecualr bone
    • Arlot M, Burt-Pichat B, Roux J-P, et al. Microarchitecture influences microdamage accumulation in human vertebral trabecualr bone. J Bone Miner Res. 2008;23(10):1613-8.
    • (2008) J Bone Miner Res. , vol.23 , Issue.10 , pp. 1613-1618
    • Arlot, M.1    Burt-Pichat, B.2    Roux, J.-P.3
  • 85
    • 0037595631 scopus 로고    scopus 로고
    • Trabecular shear stresses predict in vivo linear microcrack density but not diffuse damage in human vertebral cancellous bone
    • Yeni YN, Hou FJ, Ciarelli T, et al. Trabecular shear stresses predict in vivo linear microcrack density but not diffuse damage in human vertebral cancellous bone. Ann Biomed Eng. 2003;31 (6):726-32.
    • (2003) Ann Biomed Eng. , vol.31 , Issue.6 , pp. 726-732
    • Yeni, Y.N.1    Hou, F.J.2    Ciarelli, T.3
  • 86
    • 0024420261 scopus 로고
    • Bone creep-fatigue damage accumulation
    • Caler WE, Carter DR. Bone creep-fatigue damage accumulation. J Biomech. 1989;22:625-35. (Pubitemid 19266776)
    • (1989) Journal of Biomechanics , vol.22 , Issue.6-7 , pp. 625-635
    • Caler, W.E.1    Carter, D.R.2
  • 87
    • 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. Collagen cross-links as a determinant of bone quality: a possible explanation for bone fragility in aging, osteoporosis, and diabetes mellitus. Osteoporosis Int. 2010;21:195-214.
    • (2010) Osteoporosis Int. , vol.21 , pp. 195-214
    • Saito, M.1    Marumo, K.2
  • 89
    • 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, et al. Influence of nonenzymatic glycation on biomechanical properties of cortical bone. Bone. 2001;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
  • 90
    • 34250790094 scopus 로고    scopus 로고
    • The role of the collagen matrix in skeletal fragility
    • Vashishth D. The role of the collagen matrix in skeletal fragility. Curr Osteoporos Rep. 2007;5:62-6. (Pubitemid 46954743)
    • (2007) Current Osteoporosis Reports , vol.5 , Issue.2 , pp. 62-66
    • Vashishth, D.1
  • 91
    • 33847728657 scopus 로고    scopus 로고
    • Effects of non-enzymatic glycation on cancellous bone fragility
    • DOI 10.1016/j.bone.2006.12.056, PII S875632820600915X
    • Tang SY, Zeenath U, Vashishth D. Effects of non-enzymatic glycation on cancellous bone fragility. Bone. 2007;40(4):1144-51. (Pubitemid 46386561)
    • (2007) Bone , vol.40 , Issue.4 , pp. 1144-1151
    • Tang, S.Y.1    Zeenath, U.2    Vashishth, D.3
  • 92
    • 33947198261 scopus 로고    scopus 로고
    • Hierarchy of bone microdamage at multiple length scales
    • DOI 10.1016/j.ijfatigue.2006.09.010, PII S0142112306002647
    • Vashishth D. Hierarchy of bone microdamage at multiple length scales. Int J Fatigue. 2007;29:1024-33. (Pubitemid 46435702)
    • (2007) International Journal of Fatigue , vol.29 , Issue.6 , pp. 1024-1033
    • Vashishth, D.1
  • 93
    • 79451469002 scopus 로고    scopus 로고
    • UPLC methodology for identification and quantitation of naturally fluorescent crosslinks in proteins: A study of bone collagen
    • doi:10.1016/j.jchromb.2010.12.024
    • Sroga GE, Vashishth D. UPLC methodology for identification and quantitation of naturally fluorescent crosslinks in proteins: a study of bone collagen. J Chromatogr B. 2011;879:379-85. doi:10.1016/j.jchromb.2010.12.024.
    • (2011) J Chromatogr B. , vol.879 , pp. 379-85
    • Sroga, G.E.1    Vashishth, D.2
  • 94
    • 33749518488 scopus 로고    scopus 로고
    • Contribution of the advanced glycation end product pentosidine and of maturation of type I collagen to compressive biomechanical properties of human lumbar vertebrae
    • DOI 10.1016/j.bone.2006.05.013, PII S8756328206004947
    • Viguet-Carrin S, Roux JP, Arlot ME, et al. Contribution of the advanced glycation end product pentosidine and of maturation of type I collagen to compressive biomechanical properties of human lumbar vertebrae. Bone. 2006;39:1073-9. (Pubitemid 44528385)
    • (2006) Bone , vol.39 , Issue.5 , pp. 1073-1079
    • Viguet-Carrin, S.1    Roux, J.P.2    Arlot, M.E.3    Merabet, Z.4    Leeming, D.J.5    Byrjalsen, I.6    Delmas, P.D.7    Bouxsein, M.L.8
  • 95
    • 77449136859 scopus 로고    scopus 로고
    • Location of 3-hydroxyproline residues in collagen types I, II, II, and V/XI implies a role in fibril supramolecualr assembly
    • Weis MA, Hudson DM, Kim L, et al. Location of 3-hydroxyproline residues in collagen types I, II, II, and V/XI implies a role in fibril supramolecualr assembly. J Biol Chem. 2010;285(4):2580-90.
    • (2010) J Biol Chem. , vol.285 , Issue.4 , pp. 2580-2590
    • Weis, M.A.1    Hudson, D.M.2    Kim, L.3
  • 96
    • 0024370924 scopus 로고
    • Osteocalcin and matrix Gla protein: Vitamin K-dependent proteins in bone
    • Hauschka PV, Lian JB, Cole DEC, et al. Osteocalcin and matrix Gla protein: vitamin K-dependent proteins in bone. Physiol Rev. 1989;69(3):990-1047. (Pubitemid 19184853)
    • (1989) Physiological Reviews , vol.69 , Issue.3 , pp. 990-1047
    • Hauschka, P.V.1    Lian, J.B.2    Cole, D.E.3    Gundberg, C.M.4
  • 97
    • 0036181082 scopus 로고    scopus 로고
    • The secreted protein thrombospondin 2 is an autocrine inhibitor of marrow stromal cell proliferation
    • Hankenson KD, Bornstein P. The secreted protein thrombospondin-2 is an auticrin inhibitor of marrow stromal cell proliferation. J Bone Mineral Res. 2002;17:415-25. (Pubitemid 34171756)
    • (2002) Journal of Bone and Mineral Research , vol.17 , Issue.3 , pp. 415-425
    • Hankenson, K.D.1    Bornstein, P.2
  • 98
    • 57349158632 scopus 로고    scopus 로고
    • Phosphorylated proteins and control over apatite nucleation, crystal growth, and inhibition
    • George A, Veis A. Phosphorylated proteins and control over apatite nucleation, crystal growth, and inhibition. Chem Rev. 2008;108: 4670-93.
    • (2008) Chem Rev. , vol.108 , pp. 4670-4693
    • George, A.1    Veis, A.2


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