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Volumn 2 E, Issue 1, 2010, Pages 1-12

Molecular interactions in extracellular matrix of tendon

Author keywords

Collagen; Extracellular matrix; Gene expression; Matrix Metalloproteases; Review; Tendinopathy; Tendon; Tissue inhibitor of Matrix Metalloproteases

Indexed keywords

COLLAGEN; GLYCOSAMINOGLYCAN; MATRIX METALLOPROTEINASE;

EID: 77954496477     PISSN: 19450494     EISSN: 19450508     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (8)

References (145)
  • 2
    • 1642313674 scopus 로고    scopus 로고
    • Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading
    • DOI 10.1152/physrev.00031.2003
    • M. Kjaer: Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading. Physiol Rev, 84, 649-98 (2004) (Pubitemid 38365495)
    • (2004) Physiological Reviews , vol.84 , Issue.2 , pp. 649-698
    • Kjaer, M.1
  • 3
    • 0014685163 scopus 로고
    • The mechanism of muscular contraction
    • H. E. Huxley: The mechanism of muscular contraction. Science, 164, 1356-65 (1969)
    • (1969) Science , vol.164 , pp. 1356-1365
    • Huxley, H.E.1
  • 4
    • 0017338764 scopus 로고
    • Storage of elastic strain energy in muscle and other tissues
    • DOI 10.1038/265114a0
    • R. M. Alexander and H. C. Bennet-Clark: Storage of elastic strain energy in muscle and other tissues. Nature, 265, 114-7 (1977) (Pubitemid 8010648)
    • (1977) Nature , vol.265 , Issue.5590 , pp. 114-117
    • Alexander, R.M.1    Bennet Clark, H.C.2
  • 5
    • 0031953092 scopus 로고    scopus 로고
    • Nonmyotendinous force transmission in rat extensor digitorum longus muscle
    • P. A. Huijing, G. C. Baan and G. T. Rebel: Nonmyotendinous force transmission in rat extensor digitorum longus muscle. J Exp Biol, 201, 683-91 (1998)
    • (1998) J Exp Biol , vol.201 , pp. 683-691
    • Huijing, P.A.1    Baan, G.C.2    Rebel, G.T.3
  • 6
    • 0029957527 scopus 로고    scopus 로고
    • Regulation of extracellular matrix by mechanical stress in rat glomerular mesangial cells
    • T. Yasuda, S. Kondo, T. Homma and R. C. Harris: Regulation of extracellular matrix by mechanical stress in rat glomerular mesangial cells. J Clin Invest, 98, 1991-2000 (1996) (Pubitemid 26376286)
    • (1996) Journal of Clinical Investigation , vol.98 , Issue.9 , pp. 1991-2000
    • Yasuda, T.1    Kondo, S.2    Homma, T.3    Harris, R.C.4
  • 8
    • 0030460585 scopus 로고    scopus 로고
    • Tendon cells in vivo form a three dimensional network of cell processes linked by gap junctions
    • C. M. McNeilly, A. J. Banes, M. Benjamin and J. R. Ralphs: Tendon cells in vivo form a three dimensional network of cell processes linked by gap junctions. J Anat, 189 (Pt 3), 593-600 (1996) (Pubitemid 27011014)
    • (1996) Journal of Anatomy , vol.189 , Issue.3 , pp. 593-600
    • McNeilly, C.M.1    Banes, A.J.2    Benjamin, M.3    Ralphs, J.R.4
  • 9
    • 0031724316 scopus 로고    scopus 로고
    • Regional differences in cell shape and gap junction expression in rat Achilles tendon: Relation to fibrocartilage differentiation
    • DOI 10.1017/S0021878298003902
    • J. R. Ralphs, M. Benjamin, A. D. Waggett, D. C. Russell, K. Messner and J. Gao: Regional differences in cell shape and gap junction expression in rat Achilles tendon: relation to fibrocartilage differentiation. J Anat, 193 (Pt 2), 215-22 (1998) (Pubitemid 28479045)
    • (1998) Journal of Anatomy , vol.193 , Issue.2 , pp. 215-222
    • Ralphs, J.R.1    Benjamin, M.2    Waggett, A.D.3    Russell, D.C.4    Messner, K.5    Gao, J.6
  • 11
    • 0035058027 scopus 로고    scopus 로고
    • Proteoglycans and glycosaminoglycan fine structure in the mouse tail tendon fascicle
    • DOI 10.1016/S0736-0266(00)00032-2
    • K. A. Derwin, L. J. Soslowsky, J. H. Kimura and A. H. Plaas: Proteoglycans and glycosaminoglycan fine structure in the mouse tail tendon fascicle. J Orthop Res, 19, 269-77 (2001) (Pubitemid 32331703)
    • (2001) Journal of Orthopaedic Research , vol.19 , Issue.2 , pp. 269-277
    • Derwin, K.A.1    Soslowsky, L.J.2    Kimura, J.H.3    Plaas, A.H.4
  • 12
    • 0026652062 scopus 로고
    • Supramolecular organization of extracellular matrix glycosaminoglycans, in vitro and in the tissues
    • J. E. Scott: Supramolecular organization of extracellular matrix glycosaminoglycans, in vitro and in the tissues. Faseb J, 6, 2639-45 (1992)
    • (1992) Faseb J , vol.6 , pp. 2639-2645
    • Scott, J.E.1
  • 13
    • 0018378643 scopus 로고
    • Identification and change of collagen types in differentiating myoblasts and developing chick muscle
    • A. J. Bailey, G. B. Shellswell and V. C. Duance: Identification and change of collagen types in differentiating myoblasts and developing chick muscle. Nature, 278, 67-9 (1979) (Pubitemid 9105113)
    • (1979) Nature , vol.278 , Issue.5699 , pp. 67-69
    • Bailey, A.J.1    Shellswell, G.B.2    Duance, V.C.3
  • 14
    • 0026234179 scopus 로고
    • Energy-saving mechanisms in walking and running
    • R. M. Alexander: Energy-saving mechanisms in walking and running. J Exp Biol, 160, 55-69 (1991)
    • (1991) J Exp Biol , vol.160 , pp. 55-69
    • Alexander, R.M.1
  • 15
    • 0023198987 scopus 로고
    • Chemistry of the collagen cross-links. Origin and partial characterization of a putative mature cross-link of collagen
    • K. Barnard, N. D. Light, T. J. Sims and A. J. Bailey: Chemistry of the collagen cross-links. Origin and partial characterization of a putative mature cross-link of collagen. Biochem J, 244, 303-9 (1987) (Pubitemid 17087093)
    • (1987) Biochemical Journal , vol.244 , Issue.2 , pp. 303-309
    • Barnard, K.1    Light, N.D.2    Sims, T.J.3    Bailey, A.J.4
  • 16
    • 78651192479 scopus 로고
    • Structure and function of mammalian tendon
    • D. H. Elliott: Structure and Function of Mammalian Tendon. Biol Rev Camb Philos Soc, 40, 392-421 (1965)
    • (1965) Biol Rev Camb Philos Soc , vol.40 , pp. 392-421
    • Elliott, D.H.1
  • 17
    • 0032198563 scopus 로고    scopus 로고
    • Macroscopic 'degeneration' of equine superficial digital flexor tendon is accompanied by a change in extracellular matrix composition
    • H. L. Birch, A. J. Bailey and A. E. Goodship: Macroscopic 'degeneration' of equine superficial digital flexor tendon is accompanied by a change in extracellular matrix composition. Equine Vet J, 30, 534-9 (1998) (Pubitemid 128527090)
    • (1998) Equine Veterinary Journal , vol.30 , Issue.6 , pp. 534-539
    • Birch, H.L.1    Bailey, A.J.2    Goodship, A.E.3
  • 19
    • 0033571427 scopus 로고    scopus 로고
    • Type i collagen synthesis and degradation in peritendinous tissue after exercise determined by microdialysis in humans
    • H. Langberg, D. Skovgaard, L. J. Petersen, J. Bulow and M. Kjaer: Type I collagen synthesis and degradation in peritendinous tissue after exercise determined by microdialysis in humans. J Physiol, 521 Pt 1, 299-306 (1999)
    • (1999) J Physiol , vol.521 , Issue.PART 1 , pp. 299-306
    • Langberg, H.1    Skovgaard, D.2    Petersen, L.J.3    Bulow, J.4    Kjaer, M.5
  • 20
    • 0032456952 scopus 로고    scopus 로고
    • COMP (cartilage oligomeric matrix protein) is synthesized in ligament, tendon, meniscus, and articular cartilage
    • G. Muller, A. Michel and E. Altenburg: COMP (cartilage oligomeric matrix protein) is synthesized in ligament, tendon, meniscus, and articular cartilage. Connect Tissue Res, 39, 233-44 (1998) (Pubitemid 29060093)
    • (1998) Connective Tissue Research , vol.39 , Issue.4 , pp. 233-244
    • Muller, G.1    Michel, A.2    Altenburg, E.3
  • 25
    • 0031657808 scopus 로고    scopus 로고
    • Matrix proteoglycans: From molecular design to cellular function
    • DOI 10.1146/annurev.biochem.67.1.609
    • R. V. Iozzo: Matrix proteoglycans: from molecular design to cellular function. Annu Rev Biochem, 67, 609- 52 (1998) (Pubitemid 28411140)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 609-652
    • Iozzo, R.V.1
  • 26
    • 0033516558 scopus 로고    scopus 로고
    • The biology of the small leucine-rich proteoglycans. Functional network of interactive proteins
    • R. V. Iozzo: The biology of the small leucine-rich proteoglycans. Functional network of interactive proteins. J Biol Chem, 274, 18843-6 (1999)
    • (1999) J Biol Chem , vol.274 , pp. 18843-19186
    • Iozzo, R.V.1
  • 27
    • 4444330751 scopus 로고    scopus 로고
    • Binding of von Willebrand factor to the small proteoglycan decorin
    • DOI 10.1016/j.febslet.2004.08.011, PII S001457930401004X
    • G. F. Guidetti, B. Bartolini, B. Bernardi, M. E. Tira, M. C. Berndt, C. Balduini and M. Torti: Binding of von Willebrand factor to the small proteoglycan decorin. FEBS Lett, 574, 95- 100 (2004) (Pubitemid 39200901)
    • (2004) FEBS Letters , vol.574 , Issue.1-3 , pp. 95-100
    • Guidetti, G.F.1    Bartolini, B.2    Bernardi, B.3    Tira, M.E.4    Berndt, M.C.5    Balduini, C.6    Torti, M.7
  • 29
    • 0017228302 scopus 로고
    • The route of secretion of procollagen. The influence of alphaalpha'- bipyridyl, colchicine and antimycin A on the secretory process in embryonic-chick tendon and cartilage cells
    • R. Harwood, M. E. Grant and D. S. Jackson: The route of secretion of procollagen. The influence of alphaalpha'- bipyridyl, colchicine and antimycin A on the secretory process in embryonic-chick tendon and cartilage cells. Biochem J, 156, 81-90 (1976)
    • (1976) Biochem J , vol.156 , pp. 81-90
    • Harwood, R.1    Grant, M.E.2    Jackson, D.S.3
  • 31
    • 0031940912 scopus 로고    scopus 로고
    • Procollagen n-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important: Roles in development and cell signaling
    • DOI 10.1016/S0945-053X(98)90013-0
    • D. J. Prockop, A. L. Sieron and S. W. Li: Procollagen N-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important roles in development and cell signaling. Matrix Biol, 16, 399-408 (1998) (Pubitemid 28069866)
    • (1998) Matrix Biology , vol.16 , Issue.7 , pp. 399-408
    • Prockop, D.J.1    Sieron, A.L.2    Li, S.-W.3
  • 32
    • 0037358282 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis
    • DOI 10.1016/S0945-053X(03)00006-4, PII S0945053X03000064
    • J. Myllyharju: Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis. Matrix Biol, 22, 15-24 (2003) (Pubitemid 36444503)
    • (2003) Matrix Biology , vol.22 , Issue.1 , pp. 15-24
    • Myllyharju, J.1
  • 33
    • 0022998819 scopus 로고
    • Folding of carboxyl domain and assembly of procollagen I
    • K. J. Doege and J. H. Fessler: Folding of carboxyl domain and assembly of procollagen I. J Biol Chem, 261, 8924-35 (1986) (Pubitemid 17205097)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.19 , pp. 8924-8935
    • Doege, K.J.1    Fessler, J.H.2
  • 34
    • 0032814336 scopus 로고    scopus 로고
    • MRNA levels for α-subunit of prolyl 4-hydroxylase and fibrillar collagens in immobilized rat skeletal muscle
    • X. Y. Han, W. Wang, R. Myllyla, P. Virtanen, J. Karpakka and T. E. Takala: mRNA levels for alpha-subunit of prolyl 4-hydroxylase and fibrillar collagens in immobilized rat skeletal muscle. J Appl Physiol, 87, 90-6 (1999) (Pubitemid 29330667)
    • (1999) Journal of Applied Physiology , vol.87 , Issue.1 , pp. 90-96
    • Han, X.-Y.1    Wang, W.2    Myllyla, R.3    Virtanen, P.4    Karpakka, J.5    Takala, T.E.S.6
  • 36
    • 0036253136 scopus 로고    scopus 로고
    • 2-terminal propeptides of fibrillar collagens: Highly conserved domains with poorly understood functions
    • DOI 10.1016/S0945-053X(02)00008-2, PII S0945053X02000082
    • P. Bornstein: The NH (2)-terminal propeptides of fibrillar collagens: highly conserved domains with poorly understood functions. Matrix Biol, 21, 217-26 (2002) (Pubitemid 34497013)
    • (2002) Matrix Biology , vol.21 , Issue.3 , pp. 217-226
    • Bornstein, P.1
  • 37
  • 38
    • 0018219823 scopus 로고
    • A comparison of the size distribution of collagen fibrils in connective tissues as a function of age and a possible relation between fibril size distribution and mechanical properties
    • D. A. Parry, G. R. Barnes and A. S. Craig: A comparison of the size distribution of collagen fibrils in connective tissues as a function of age and a possible relation between fibril size distribution and mechanical properties. Proc R Soc Lond B Biol Sci, 203, 305-21 (1978) (Pubitemid 9092950)
    • (1978) Proceedings of the Royal Society of London - Biological Sciences , vol.203 , Issue.1152 , pp. 305-321
    • Parry, D.A.D.1    Barnes, G.R.G.2    Craig, A.S.3
  • 41
    • 0034723148 scopus 로고    scopus 로고
    • Identification of collagen fibril fusion during vertebrate tendon morphogenesis. The process relies on unipolar fibrils and is regulated by collagen-proteoglycan interaction
    • H. K. Graham, D. F. Holmes, R. B. Watson and K. E. Kadler: Identification of collagen fibril fusion during vertebrate tendon morphogenesis. The process relies on unipolar fibrils and is regulated by collagen-proteoglycan interaction. J Mol Biol, 295, 891-902 (2000)
    • (2000) J Mol Biol , vol.295 , pp. 891-902
    • Graham, H.K.1    Holmes, D.F.2    Watson, R.B.3    Kadler, K.E.4
  • 42
    • 0030945384 scopus 로고    scopus 로고
    • Localization of collagen types I, III and V during tendon development. Changes in collagen types I and III are correlated with changes in fibril diameter
    • D. E. Birk and R. Mayne: Localization of collagen types I, III and V during tendon development. Changes in collagen types I and III are correlated with changes in fibril diameter. Eur J Cell Biol, 72, 352-61 (1997) (Pubitemid 27170632)
    • (1997) European Journal of Cell Biology , vol.72 , Issue.4 , pp. 352-361
    • Birk, D.E.1    Mayne, R.2
  • 43
    • 0031042279 scopus 로고    scopus 로고
    • Collagen fibrillogenesis in situ: Fibril segments become long fibrils as the developing tendon matures
    • DOI 10.1002/(SICI)1097-0177(199703)208:3<291::AID-AJA1>3.0.CO;2-D
    • D. E. Birk, E. I. Zycband, S. Woodruff, D. A. Winkelmann and R. L. Trelstad: Collagen fibrillogenesis in situ: fibril segments become long fibrils as the developing tendon matures. Dev Dyn, 208, 291-8 (1997) (Pubitemid 27114284)
    • (1997) Developmental Dynamics , vol.208 , Issue.3 , pp. 291-298
    • Birk, D.E.1    Zycband, E.I.2    Woodruff, S.3    Winkelmann, D.A.4    Trelstad, R.L.5
  • 44
    • 0033813556 scopus 로고    scopus 로고
    • Assembly of type i collagen: Fusion of fibril subunits and the influence of fibril diameter on mechanical properties
    • D. L. Christiansen, E. K. Huang and F. H. Silver: Assembly of type I collagen: fusion of fibril subunits and the influence of fibril diameter on mechanical properties. Matrix Biol, 19, 409-20 (2000)
    • (2000) Matrix Biol , vol.19 , pp. 409-420
    • Christiansen, D.L.1    Huang, E.K.2    Silver, F.H.3
  • 45
    • 0034820913 scopus 로고    scopus 로고
    • Force deficits after stretches of activated rat muscle-tendon complex with reduced collagen cross-linking
    • DOI 10.1007/s004210100480
    • M. E. Willems, G. R. Miller and W. T. Stauber: Force deficits after stretches of activated rat muscle-tendon complex with reduced collagen cross-linking. Eur J Appl Physiol, 85, 405-11 (2001) (Pubitemid 32894557)
    • (2001) European Journal of Applied Physiology , vol.85 , Issue.5 , pp. 405-411
    • Willems, M.E.T.1    Miller, G.R.2    Stauber, W.T.3
  • 47
    • 0031044872 scopus 로고    scopus 로고
    • Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
    • DOI 10.1083/jcb.136.3.729
    • K. G. Danielson, H. Baribault, D. F. Holmes, H. Graham, K. E. Kadler and R. V. Iozzo: Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J Cell Biol, 136, 729-43 (1997) (Pubitemid 27083772)
    • (1997) Journal of Cell Biology , vol.136 , Issue.3 , pp. 729-743
    • Danielson, K.G.1    Baribault, H.2    Holmes, D.F.3    Graham, H.4    Kadler, K.E.5    Iozzo, R.V.6
  • 49
    • 0031044967 scopus 로고    scopus 로고
    • Chemistry of collagen cross-linking: Biochemical changes in collagen during the partial mineralization of turkey leg tendon
    • L. Knott, J. F. Tarlton and A. J. Bailey: Chemistry of collagen cross-linking: biochemical changes in collagen during the partial mineralization of turkey leg tendon. Biochem J, 322 (Pt 2), 535-42 (1997) (Pubitemid 27116581)
    • (1997) Biochemical Journal , vol.322 , Issue.2 , pp. 535-542
    • Knott, L.1    Tarlton, J.F.2    Bailey, A.J.3
  • 50
    • 0035818480 scopus 로고    scopus 로고
    • Enzyme interactions in heparan sulfate biosynthesis: Uronosyl 5-epimerase and 2-Osulfotransferase interact in vivo
    • M. A. Pinhal, B. Smith, S. Olson, J. Aikawa, K. Kimata and J. D. Esko: Enzyme interactions in heparan sulfate biosynthesis: uronosyl 5-epimerase and 2-Osulfotransferase interact in vivo. Proc Natl Acad Sci U S A, 98, 12984-9 (2001)
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12984-13129
    • Pinhal, M.A.1    Smith, B.2    Olson, S.3    Aikawa, J.4    Kimata, K.5    Esko, J.D.6
  • 51
    • 0036846183 scopus 로고    scopus 로고
    • Sulfotransferases and sulfated oligosaccharides
    • DOI 10.1002/med.10020
    • K. Honke and N. Taniguchi: Sulfotransferases and sulfated oligosaccharides. Med Res Rev, 22, 637-54 (2002) (Pubitemid 35299536)
    • (2002) Medicinal Research Reviews , vol.22 , Issue.6 , pp. 637-654
    • Honke, K.1
  • 52
    • 0026585325 scopus 로고
    • Circulatory half-life but not interaction with the lutropin/chorionic gonadotropin receptor is modulated by sulfation of bovine lutropin oligosaccharides
    • J. U. Baenziger, S. Kumar, R. M. Brodbeck, P. L. Smith and M. C. Beranek: Circulatory half-life but not interaction with the lutropin/chorionic gonadotropin receptor is modulated by sulfation of bovine lutropin oligosaccharides. Proc Natl Acad Sci U S A, 89, 334-8 (1992)
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 334-338
    • Baenziger, J.U.1    Kumar, S.2    Brodbeck, R.M.3    Smith, P.L.4    Beranek, M.C.5
  • 55
    • 0035849873 scopus 로고    scopus 로고
    • The heparin-binding haemagglutinin of M. Tuberculosis is required for extrapulmonary dissemination
    • DOI 10.1038/35084083
    • K. Pethe, S. Alonso, F. Biet, G. Delogu, M. J. Brennan, C. Locht and F. D. Menozzi: The heparin-binding haemagglutinin of M. tuberculosis is required for extrapulmonary dissemination. Nature, 412, 190-4 (2001) (Pubitemid 32674716)
    • (2001) Nature , vol.412 , Issue.6843 , pp. 190-194
    • Pethe, K.1    Alonso, S.2    Biet, F.3    Delogu, G.4    Brennan, M.J.5    Locht, C.6    Menozzi, F.D.7
  • 57
    • 0032900316 scopus 로고    scopus 로고
    • Thermal instability of the trimeric structure of the N-terminal propeptide of human procollagen type I in relation to assay technology
    • J. Brandt, T. N. Krogh, C. H. Jensen, J. K. Frederiksen and B. Teisner: Thermal instability of the trimeric structure of the N-terminal propeptide of human procollagen type I in relation to assay technology. Clin Chem, 45, 47-53 (1999) (Pubitemid 29036384)
    • (1999) Clinical Chemistry , vol.45 , Issue.1 , pp. 47-53
    • Brandt, J.1    Krogh, T.N.2    Jensen, C.H.3    Frederiksen, J.K.4    Teisner, B.5
  • 58
    • 0035395097 scopus 로고    scopus 로고
    • Training-induced changes in peritendinous type I collagen turnover determined by microdialysis in humans
    • DOI 10.1111/j.1469-7793.2001.00297.x
    • H. Langberg, L. Rosendal and M. Kjaer: Traininginduced changes in peritendinous type I collagen turnover determined by microdialysis in humans. J Physiol, 534, 297-302 (2001) (Pubitemid 32631774)
    • (2001) Journal of Physiology , vol.534 , Issue.1 , pp. 297-302
    • Langberg, H.1    Rosendal, L.2    Kjaer, M.3
  • 59
    • 0033834961 scopus 로고    scopus 로고
    • Protein and amino acid metabolism during and after exercise and the effects of nutrition
    • M. J. Rennie and K. D. Tipton: Protein and amino acid metabolism during and after exercise and the effects of nutrition. Annu Rev Nutr, 20, 457-83 (2000)
    • (2000) Annu Rev Nutr , vol.20 , pp. 457-483
    • Rennie, M.J.1    Tipton, K.D.2
  • 61
    • 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
    • E. Gineyts, P. A. Cloos, O. Borel, L. Grimaud, P. D. Delmas and P. Garnero: Racemization and isomerization of type I collagen C-telopeptides in human bone and soft tissues: assessment of tissue turnover. Biochem J, 345 Pt 3, 481-5 (2000) (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
  • 62
    • 0033926526 scopus 로고    scopus 로고
    • Time pattern of exercise-induced changes in type I collagen turnover after prolonged endurance exercise in humans
    • H. Langberg, D. Skovgaard, S. Asp and M. Kjaer: Time pattern of exercise-induced changes in type I collagen turnover after prolonged endurance exercise in humans. Calcif Tissue Int, 67, 41-4 (2000) (Pubitemid 30460947)
    • (2000) Calcified Tissue International , vol.67 , Issue.1 , pp. 41-44
    • Langberg, H.1    Skovgaard, D.2    Asp, S.3    Kjaer, M.4
  • 63
    • 0028041254 scopus 로고
    • Regional expression of mRNA for proteoglycans and collagen in tendon
    • J. R. Robbins and K. G. Vogel: Regional expression of mRNA for proteoglycans and collagen in tendon. Eur J Cell Biol, 64, 264-70 (1994) (Pubitemid 24258186)
    • (1994) European Journal of Cell Biology , vol.64 , Issue.2 , pp. 264-270
    • Robbins, J.R.1    Vogel, K.G.2
  • 64
  • 65
    • 0023935587 scopus 로고
    • Effects of denervation and immobilization on collagen synthesis in rat skeletal muscle and tendon
    • J. Savolainen, V. Myllyla, R. Myllyla, V. Vihko, K. Vaananen and T. E. Takala: Effects of denervation and immobilization on collagen synthesis in rat skeletal muscle and tendon. Am J Physiol, 254, R897-902 (1988)
    • (1988) Am J Physiol , vol.254
    • Savolainen, J.1    Myllyla, V.2    Myllyla, R.3    Vihko, V.4    Vaananen, K.5    Takala, T.E.6
  • 66
    • 0036308681 scopus 로고    scopus 로고
    • Fgf4 positively regulates scleraxis and tenascin expression in chick limb tendons
    • DOI 10.1006/dbio.2002.0707
    • F. Edom-Vovard, B. Schuler, M. A. Bonnin, M. A. Teillet and D. Duprez: Fgf4 positively regulates scleraxis and tenascin expression in chick limb tendons. Dev Biol, 247, 351-66 (2002) (Pubitemid 34734870)
    • (2002) Developmental Biology , vol.247 , Issue.2 , pp. 351-366
    • Edom-Vovard, F.1    Schuler, B.2    Bonnin, M.-A.3    Teillet, M.-A.4    Duprez, D.5
  • 67
    • 0034850235 scopus 로고    scopus 로고
    • Regulation of synthesis of fibrillar collagens in rat skeletal muscle during immobilization in shortened and lengthened positions
    • DOI 10.1046/j.1365-201X.2001.00848.x
    • A. M. Ahtikoski, S. O. Koskinen, P. Virtanen, V. Kovanen and T. E. Takala: Regulation of synthesis of fibrillar collagens in rat skeletal muscle during immobilization in shortened and lengthened positions. Acta Physiol Scand, 172, 131-40 (2001) (Pubitemid 32848228)
    • (2001) Acta Physiologica Scandinavica , vol.172 , Issue.2 , pp. 131-140
    • Ahtikoski, A.M.1    Koskinen, S.O.A.2    Virtanen, P.3    Kovanen, V.4    Takala, T.E.S.5
  • 68
    • 0037383253 scopus 로고    scopus 로고
    • Synthesis and degradation of type IV collagen in rat skeletal muscle during immobilization in shortened and lengthened positions
    • DOI 10.1046/j.1365-201X.2003.01061.x
    • A. M. Ahtikoski, S. O. Koskinen, P. Virtanen, V. Kovanen, J. Risteli and T. E. Takala: Synthesis and degradation of type IV collagen in rat skeletal muscle during immobilization in shortened and lengthened positions. Acta Physiol Scand, 177, 473-81 (2003) (Pubitemid 36411585)
    • (2003) Acta Physiologica Scandinavica , vol.177 , Issue.4 , pp. 473-481
    • Ahtikoski, A.M.1    Koskinen, S.O.A.2    Virtanen, P.3    Kovanen, V.4    Risteli, J.5    Takala, T.E.S.6
  • 69
    • 11844274558 scopus 로고    scopus 로고
    • Tendon injury and tendinopathy: Healing and repair
    • DOI 10.2106/JBJS.D.01850
    • P. Sharma and N. Maffulli: Tendon injury and tendinopathy: healing and repair. J Bone Joint Surg Am, 87, 187-202 (2005) (Pubitemid 40094160)
    • (2005) Journal of Bone and Joint Surgery - Series A , vol.87 , Issue.1 , pp. 187-202
    • Sharma, P.1    Maffulli, N.2
  • 70
    • 27144542133 scopus 로고    scopus 로고
    • Basic biology of tendon injury and healing
    • P. Sharma and N. Maffulli: Basic biology of tendon injury and healing. Surgeon, 3, 309-16 (2005) (Pubitemid 41488685)
    • (2005) Surgeon , vol.3 , Issue.5 , pp. 309-316
    • Sharma, P.1    Maffulli, N.2
  • 72
    • 0031908852 scopus 로고    scopus 로고
    • Structure and biological activity of the extracellular matrix
    • DOI 10.1007/s001090050215
    • M. Aumailley and B. Gayraud: Structure and biological activity of the extracellular matrix. J Mol Med, 76, 253-65 (1998) (Pubitemid 28098711)
    • (1998) Journal of Molecular Medicine , vol.76 , Issue.3-4 , pp. 253-265
    • Aumailley, M.1    Gayraud, B.2
  • 73
    • 85047691853 scopus 로고    scopus 로고
    • Identification and enzymatic characterization of two diverging murine counterparts of human interstitial collagenase (MMP-1) expressed at sites of embryo implantation
    • M. Balbin, A. Fueyo, V. Knauper, J. M. Lopez, J. Alvarez, L. M. Sanchez, V. Quesada, J. Bordallo, G. Murphy and C. Lopez-Otin: Identification and enzymatic characterization of two diverging murine counterparts of human interstitial collagenase (MMP-1) expressed at sites of embryo implantation. J Biol Chem, 276, 10253-62 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 10253-11162
    • Balbin, M.1    Fueyo, A.2    Knauper, V.3    Lopez, J.M.4    Alvarez, J.5    Sanchez, L.M.6    Quesada, V.7    Bordallo, J.8    Murphy, G.9    Lopez-Otin, C.10
  • 74
    • 0036169329 scopus 로고    scopus 로고
    • Matrix metalloproteinase activities and their relationship with collagen remodelling in tendon pathology
    • DOI 10.1016/S0945-053X(01)00196-2, PII S0945053X01001962
    • G. P. Riley, V. Curry, J. DeGroot, B. van El, N. Verzijl, B. L. Hazleman and R. A. Bank: Matrix metalloproteinase activities and their relationship with collagen remodelling in tendon pathology. Matrix Biol, 21, 185-95 (2002) (Pubitemid 34145243)
    • (2002) Matrix Biology , vol.21 , Issue.2 , pp. 185-195
    • Riley, G.P.1    Curry, V.2    DeGroot, J.3    Van El, B.4    Verzijl, N.5    Hazleman, B.L.6    Bank, R.A.7
  • 75
    • 0141620354 scopus 로고    scopus 로고
    • Flexor tendon healing in the rat: A histologic and gene expression study
    • DOI 10.1016/S0363-5023(03)00366-6
    • W. Oshiro, J. Lou, X. Xing, Y. Tu and P. R. Manske: Flexor tendon healing in the rat: a histologic and gene expression study. J Hand Surg (Am), 28, 814-23 (2003) (Pubitemid 37175365)
    • (2003) Journal of Hand Surgery , vol.28 , Issue.5 , pp. 814-823
    • Oshiro, W.1    Lou, J.2    Xing, X.3    Tu, Y.4    Manske, P.R.5
  • 77
    • 0029739494 scopus 로고    scopus 로고
    • Determination of stromelysin-1, 72 and 92 kDa type IV collagenase, tissue inhibitor of metalloproteinase-1 (TIMP-1), and TIMP-2 in synovial fluid and serum from patients with rheumatoid arthritis
    • N. Ishiguro, T. Ito, K. Obata, N. Fujimoto and H. Iwata: Determination of stromelysin-1, 72 and 92 kDa type IV collagenase, tissue inhibitor of metalloproteinase-1 (TIMP- 1), and TIMP-2 in synovial fluid and serum from patients with rheumatoid arthritis. J Rheumatol, 23, 1599-604 (1996) (Pubitemid 26290588)
    • (1996) Journal of Rheumatology , vol.23 , Issue.9 , pp. 1599-1604
    • Ishiguro, N.1    Ito, T.2    Obata, K.-I.3    Fujimoto, N.4    Iwata, H.5
  • 79
    • 0029113780 scopus 로고
    • Levels of circulating collagenase, stromelysin-1, and tissue inhibitor of matrix metalloproteinases 1 in patients with rheumatoid arthritis. Relationship to serum levels of antigenic keratan sulfate and systemic parameters of inflammation
    • D. H. Manicourt, N. Fujimoto, K. Obata and E. J. Thonar: Levels of circulating collagenase, stromelysin-1, and tissue inhibitor of matrix metalloproteinases 1 in patients with rheumatoid arthritis. Relationship to serum levels of antigenic keratan sulfate and systemic parameters of inflammation. Arthritis Rheum, 38, 1031-9 (1995)
    • (1995) Arthritis Rheum , vol.38 , pp. 1031-1119
    • Manicourt, D.H.1    Fujimoto, N.2    Obata, K.3    Thonar, E.J.4
  • 80
    • 0032800206 scopus 로고    scopus 로고
    • The sensitivity of versican from rabbit lung to gelatinase A (MMP-2) and B (MMP-9) and its involvement in the development of hydraulic lung edema
    • DOI 10.1016/S0014-5793(99)00929-1, PII S0014579399009291
    • A. Passi, D. Negrini, R. Albertini, G. Miserocchi and G. De Luca: The sensitivity of versican from rabbit lung to gelatinase A (MMP-2) and B (MMP-9) and its involvement in the development of hydraulic lung edema. FEBS Lett, 456, 93-6 (1999) (Pubitemid 29339048)
    • (1999) FEBS Letters , vol.456 , Issue.1 , pp. 93-96
    • Passi, A.1    Negrini, D.2    Albertini, R.3    Miserocchi, G.4    De Luca, G.5
  • 81
    • 0028947020 scopus 로고
    • Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitorfree enzyme catalyzes the cleavage of collagen fibrils and soluble native type i collagen generating the specific 3/4- and 1/4-length fragments
    • R. T. Aimes and J. P. Quigley: Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitorfree enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments. J Biol Chem, 270, 5872-6 (1995)
    • (1995) J Biol Chem , vol.270 , pp. 5872-5956
    • Aimes, R.T.1    Quigley, J.P.2
  • 82
    • 0035903020 scopus 로고    scopus 로고
    • Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain
    • DOI 10.1016/S0014-5793(01)02723-5, PII S0014579301027235
    • M. L. Patterson, S. J. Atkinson, V. Knauper and G. Murphy: Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain. FEBS Lett, 503, 158-62 (2001) (Pubitemid 32763197)
    • (2001) FEBS Letters , vol.503 , Issue.2-3 , pp. 158-162
    • Patterson, M.L.1    Atkinson, S.J.2    Knauper, V.3    Murphy, G.4
  • 83
    • 1342346644 scopus 로고    scopus 로고
    • Physical exercise can influence local levels of matrix metalloproteinases and their inhibitors in tendon-related connective tissue
    • DOI 10.1152/japplphysiol.00489.2003
    • S. O. Koskinen, K. M. Heinemeier, J. L. Olesen, H. Langberg and M. Kjaer: Physical exercise can influence local levels of matrix metalloproteinases and their inhibitors in tendon-related connective tissue. J Appl Physiol, 96, 861-4 (2004) (Pubitemid 38248655)
    • (2004) Journal of Applied Physiology , vol.96 , Issue.3 , pp. 861-864
    • Koskinen, S.O.A.1    Heinemeier, K.M.2    Olesen, J.L.3    Langberg, H.4    Kjaer, M.5
  • 84
    • 0032483327 scopus 로고    scopus 로고
    • An interleukin-1 loop is induced in human skin fibroblasts upon stress relaxation in a three-dimensional collagen gel but is not involved in the up-regulation of matrix metalloproteinase 1
    • C. A. Lambert, C. M. Lapiere and B. V. Nusgens: An interleukin-1 loop is induced in human skin fibroblasts upon stress relaxation in a three-dimensional collagen gel but is not involved in the up-regulation of matrix metalloproteinase 1. J Biol Chem, 273, 23143-9 (1998)
    • (1998) J Biol Chem , vol.273 , pp. 23143-23239
    • Lambert, C.A.1    Lapiere, C.M.2    Nusgens, B.V.3
  • 85
    • 0036007105 scopus 로고    scopus 로고
    • Stretch and interleukin-1β induce matrix metalloproteinases in rabbit tendon cells in vitro
    • DOI 10.1016/S0736-0266(01)00075-4
    • J. Archambault, M. Tsuzaki, W. Herzog and A. J. Banes: Stretch and interleukin-1beta induce matrix metalloproteinases in rabbit tendon cells in vitro. J Orthop Res, 20, 36-9 (2002) (Pubitemid 34071419)
    • (2002) Journal of Orthopaedic Research , vol.20 , Issue.1 , pp. 36-39
    • Archambault, J.1    Tsuzaki, M.2    Herzog, W.3    Banes, A.J.4
  • 87
    • 0034714202 scopus 로고    scopus 로고
    • TIMP-2 is required for efficient activation of proMMP-2 in vivo
    • Z. Wang, R. Juttermann and P. D. Soloway: TIMP-2 is required for efficient activation of proMMP-2 in vivo. J Biol Chem, 275, 26411-5 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 26411-27265
    • Wang, Z.1    Juttermann, R.2    Soloway, P.D.3
  • 88
    • 0034253758 scopus 로고    scopus 로고
    • Tip-mediated fusion involving unipolar collagen fibrils accounts for rapid fibril elongation, the occurrence of fibrillar branched networks in skin and the paucity of collagen fibril ends in vertebrates
    • DOI 10.1016/S0945-053X(00)00082-2, PII S0945053X00000822
    • K. E. Kadler, D. F. Holmes, H. Graham and T. Starborg: Tip-mediated fusion involving unipolar collagen fibrils accounts for rapid fibril elongation, the occurrence of fibrillar branched networks in skin and the paucity of collagen fibril ends in vertebrates. Matrix Biol, 19, 359-65 (2000) (Pubitemid 30665660)
    • (2000) Matrix Biology , vol.19 , Issue.4 , pp. 359-365
    • Kadler, K.E.1    Holmes, D.F.2    Graham, H.3    Starborg, T.4
  • 89
    • 0031810434 scopus 로고    scopus 로고
    • Localization of leukemia inhibitory factor and interleukin-6 messenger ribonucleic acids in regenerating rat skeletal muscle
    • DOI 10.1002/(SICI)1097-4598(199806)21:6<819::AID-MUS20>3.0.CO;2-M
    • K. Kami and E. Senba: Localization of leukemia inhibitory factor and interleukin-6 messenger ribonucleic acids in regenerating rat skeletal muscle. Muscle Nerve, 21, 819-22 (1998) (Pubitemid 28248693)
    • (1998) Muscle and Nerve , vol.21 , Issue.6 , pp. 819-822
    • Kami, K.1    Senba, E.2
  • 91
    • 0027955194 scopus 로고
    • The structure and vascularization of the biceps brachii long head tendon
    • I. Kolts, B. Tillmann and R. Lullmann-Rauch: The structure and vascularization of the biceps brachii long head tendon. Ann Anat, 176, 75-80 (1994) (Pubitemid 24022712)
    • (1994) Annals of Anatomy , vol.176 , Issue.1 , pp. 75-80
    • Kolts, I.1    Tillmann, B.2    Lullmann-Rauch, R.3
  • 93
    • 0025851131 scopus 로고
    • Blood flow in chronic Achilles tendinosis. Radioactive microsphere study in rabbits
    • C. Backman, J. Friden and A. Widmark: Blood flow in chronic Achilles tendinosis. Radioactive microsphere study in rabbits. Acta Orthop Scand, 62, 386-7 (1991)
    • (1991) Acta Orthop Scand , vol.62 , pp. 386-387
    • Backman, C.1    Friden, J.2    Widmark, A.3
  • 94
    • 0033758819 scopus 로고    scopus 로고
    • Regional blood flow during exercise in humans measured by near-infrared spectroscopy and indocyanine green
    • R. Boushel, H. Langberg, J. Olesen, M. Nowak, L. Simonsen, J. Bulow and M. Kjaer: Regional blood flow during exercise in humans measured by near-infrared spectroscopy and indocyanine green. J Appl Physiol, 89, 1868-78 (2000)
    • (2000) J Appl Physiol , vol.89 , pp. 1868-1878
    • Boushel, R.1    Langberg, H.2    Olesen, J.3    Nowak, M.4    Simonsen, L.5    Bulow, J.6    Kjaer, M.7
  • 95
    • 0034177956 scopus 로고    scopus 로고
    • Blood flow and oxygenation in peritendinous tissue and calf muscle during dynamic exercise in humans
    • R. Boushel, H. Langberg, S. Green, D. Skovgaard, J. Bulow and M. Kjaer: Blood flow and oxygenation in peritendinous tissue and calf muscle during dynamic exercise in humans. J Physiol, 524 Pt 1, 305-13 (2000) (Pubitemid 30195322)
    • (2000) Journal of Physiology , vol.524 , Issue.1 , pp. 305-313
    • Boushel, R.1    Langberg, H.2    Green, S.3    Skovgaard, D.4    Bulow, J.5    Kjaer, M.6
  • 96
    • 0031840923 scopus 로고    scopus 로고
    • Blood flow in the peritendinous space of the human achilles tendon during exercise
    • DOI 10.1046/j.1365-201X.1998.00361.x
    • H. Langberg, J. Bulow and M. Kjaer: Blood flow in the peritendinous space of the human Achilles tendon during exercise. Acta Physiol Scand, 163, 149-53 (1998) (Pubitemid 28270900)
    • (1998) Acta Physiologica Scandinavica , vol.163 , Issue.2 , pp. 149-153
    • Langberg, H.1    Bulow, J.2    Kjaer, M.3
  • 97
    • 0032938365 scopus 로고    scopus 로고
    • Standardized intermittent static exercise increases peritendinous blood flow in human leg
    • DOI 10.1046/j.1365-2281.1999.00148.x
    • H. Langberg, J. Bulow and M. Kjaer: Standardized intermittent static exercise increases peritendinous blood flow in human leg. Clin Physiol, 19, 89-93 (1999) (Pubitemid 29057331)
    • (1999) Clinical Physiology , vol.19 , Issue.1 , pp. 89-93
    • Langberg, H.1    Bulow, J.2    Kjaer, M.3
  • 98
    • 0035091116 scopus 로고    scopus 로고
    • Age related blood flow around the Achilles tendon during exercise in humans
    • DOI 10.1007/s004210170013
    • H. Langberg, J. Olesen, D. Skovgaard and M. Kjaer: Age related blood flow around the Achilles tendon during exercise in humans. Eur J Appl Physiol, 84, 246- 8 (2001) (Pubitemid 32229402)
    • (2001) European Journal of Applied Physiology , vol.84 , Issue.3 , pp. 246-248
    • Langberg, H.1    Olesen, J.2    Skovgaard, D.3    Kjaer, M.4
  • 99
    • 0036687457 scopus 로고    scopus 로고
    • Exercise-induced increase in interstitial bradykinin and adenosine concentrations in skeletal muscle and peritendinous tissue in humans
    • DOI 10.1113/jphysiol.2002.018077
    • H. Langberg, C. Bjorn, R. Boushel, Y. Hellsten and M. Kjaer: Exercise-induced increase in interstitial bradykinin and adenosine concentrations in skeletal muscle and peritendinous tissue in humans. J Physiol, 542, 977-83 (2002) (Pubitemid 34947288)
    • (2002) Journal of Physiology , vol.542 , Issue.3 , pp. 977-983
    • Langberg, H.1    Bjorn, C.2    Boushel, R.3    Hellsten, Y.4    Kjaer, M.5
  • 100
    • 0030045673 scopus 로고    scopus 로고
    • Molecular responses of endothelial tissue to kinins
    • R. Busse and I. Fleming: Molecular responses of endothelial tissue to kinins. Diabetes, 45 Suppl 1, S8-13 (1996) (Pubitemid 26011982)
    • (1996) Diabetes , vol.45 , Issue.1 SUPPL.
    • Busse, R.1    Fleming, I.2
  • 101
    • 0028519231 scopus 로고
    • Local L-NG-monomethyl-arginine attenuates the vasodilator action of bradykinin in the human forearm
    • K. P. O'Kane, D. J. Webb, J. G. Collier and P. J. Vallance: Local L-NG-monomethyl-arginine attenuates the vasodilator action of bradykinin in the human forearm. Br J Clin Pharmacol, 38, 311-5 (1994)
    • (1994) Br J Clin Pharmacol , vol.38 , pp. 311-315
    • O'Kane, K.P.1    Webb, D.J.2    Collier, J.G.3    Vallance, P.J.4
  • 102
    • 0022651005 scopus 로고
    • Effect of vasoactive peptides on prostacyclin synthesis in man
    • S. E. Barrow, C. T. Dollery, D. J. Heavey, N. E. Hickling, J. M. Ritter and J. Vial: Effect of vasoactive peptides on prostacyclin synthesis in man. Br J Pharmacol, 87, 243-7 (1986) (Pubitemid 16165908)
    • (1986) British Journal of Pharmacology , vol.87 , Issue.1 , pp. 243-247
    • Barrow, S.E.1    Dollery, C.T.2    Heavey, D.J.3
  • 103
    • 0034119983 scopus 로고    scopus 로고
    • Bradykinin-induced vasodilation of human forearm resistance vessels is primarily mediated by endothelium-dependent hyperpolarization
    • M. L. Honing, P. Smits, P. J. Morrison and T. J. Rabelink: Bradykinin-induced vasodilation of human forearm resistance vessels is primarily mediated by endothelium-dependent hyperpolarization. Hypertension, 35, 1314-8 (2000) (Pubitemid 30413670)
    • (2000) Hypertension , vol.35 , Issue.6 , pp. 1314-1318
    • Honing, M.L.H.1    Smits, P.2    Morrison, P.J.3    Rabelink, T.J.4
  • 105
    • 0036711945 scopus 로고    scopus 로고
    • Combined inhibition of nitric oxide and prostaglandins reduces human skeletal muscle blood flow during exercise
    • DOI 10.1113/jphysiol.2002.021477
    • R. Boushel, H. Langberg, C. Gemmer, J. Olesen, R. Crameri, C. Scheede, M. Sander and M. Kjaer: Combined inhibition of nitric oxide and prostaglandins reduces human skeletal muscle blood flow during exercise. J Physiol, 543, 691-8 (2002) (Pubitemid 35012220)
    • (2002) Journal of Physiology , vol.543 , Issue.2 , pp. 691-698
    • Boushel, R.1    Langberg, H.2    Gemmer, C.3    Olesen, J.4    Crameri, R.5    Scheede, C.6    Sander, M.7    Kjaer, M.8
  • 107
    • 0035013885 scopus 로고    scopus 로고
    • Control of microtubule assembly by extracellular matrix and externally applied strain
    • A. J. Putnam, K. Schultz and D. J. Mooney: Control of microtubule assembly by extracellular matrix and externally applied strain. Am J Physiol Cell Physiol, 280, C556-64 (2001)
    • (2001) Am J Physiol Cell Physiol , vol.280
    • Putnam, A.J.1    Schultz, K.2    Mooney, D.J.3
  • 108
    • 0020698866 scopus 로고
    • Lateral transmission of tension in frog myofibers: A myofibrillar network and transverse cytoskeletal connections are possible transmitters
    • DOI 10.1002/jcp.1041140314
    • S. F. Street: Lateral transmission of tension in frog myofibers: a myofibrillar network and transverse cytoskeletal connections are possible transmitters. J Cell Physiol, 114, 346-64 (1983) (Pubitemid 13161556)
    • (1983) Journal of Cellular Physiology , vol.114 , Issue.3 , pp. 346-364
    • Street, S.F.1
  • 109
    • 0034220133 scopus 로고    scopus 로고
    • Muscle and tendon contributions to force, work, and elastic energy savings: A comparative perspective
    • A. A. Biewener and T. J. Roberts: Muscle and tendon contributions to force, work, and elastic energy savings: a comparative perspective. Exerc Sport Sci Rev, 28, 99-107 (2000)
    • (2000) Exerc Sport Sci Rev , vol.28 , pp. 99-107
    • Biewener, A.A.1    Roberts, T.J.2
  • 112
    • 0040436000 scopus 로고    scopus 로고
    • Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon
    • L. Svensson, A. Aszodi, F. P. Reinholt, R. Fassler, D. Heinegard and A. Oldberg: Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon. J Biol Chem, 274, 9636-47 (1999)
    • (1999) J Biol Chem , vol.274 , pp. 9636-9647
    • Svensson, L.1    Aszodi, A.2    Reinholt, F.P.3    Fassler, R.4    Heinegard, D.5    Oldberg, A.6
  • 113
    • 0036235834 scopus 로고    scopus 로고
    • Abnormal collagen fibrils in tendons of biglycan/fibromodulin-deficient mice lead to gait impairment, ectopic ossification, and osteoarthritis
    • DOI 10.1096/fj.01-0848com
    • L. Ameye, D. Aria, K. Jepsen, A. Oldberg, T. Xu and M. F. Young: Abnormal collagen fibrils in tendons of biglycan/fibromodulin-deficient mice lead to gait impairment, ectopic ossification, and osteoarthritis. Faseb J, 16, 673-80 (2002) (Pubitemid 34465431)
    • (2002) FASEB Journal , vol.16 , Issue.7 , pp. 673-680
    • Ameye, L.1    Aria, D.2    Jepsen, K.3    Oldberg, A.K.E.4    Xu, T.5    Young, M.F.6
  • 114
    • 0031693482 scopus 로고    scopus 로고
    • Characterization of cartilage oligomeric matrix protein (COMP) in human normal and pseudoachondroplasia musculoskeletal tissues
    • DOI 10.1016/S0945-053X(98)90080-4
    • J. T. Hecht, M. Deere, E. Putnam, W. Cole, B. Vertel, H. Chen and J. Lawler: Characterization of cartilage oligomeric matrix protein (COMP) in human normal and pseudoachondroplasia musculoskeletal tissues. Matrix Biol, 17, 269-78 (1998) (Pubitemid 28403341)
    • (1998) Matrix Biology , vol.17 , Issue.4 , pp. 269-278
    • Hecht, J.T.1    Deere, M.2    Putnam, E.3    Cole, W.4    Vertel, B.5    Chen, H.6    Lawler, J.7
  • 116
    • 0025214344 scopus 로고
    • Proteoglycan: Collagen interactions and subfibrillar structure in collagen fibrils. Implications in the development and ageing of connective tissues
    • J. E. Scott: Proteoglycan:collagen interactions and subfibrillar structure in collagen fibrils. Implications in the development and ageing of connective tissues. J Anat, 169, 23-35 (1990) (Pubitemid 20136598)
    • (1990) Journal of Anatomy , vol.169 , pp. 23-35
    • Scott, J.E.1
  • 117
    • 0035011343 scopus 로고    scopus 로고
    • Structure and function in extracellular matrices depend on interactions between anionic glycosaminoglycans
    • DOI 10.1016/S0369-8114(01)00152-3
    • J. E. Scott: Structure and function in extracellular matrices depend on interactions between anionic glycosaminoglycans. Pathol Biol (Paris), 49, 284-9 (2001) (Pubitemid 32494253)
    • (2001) Pathologie Biologie , vol.49 , Issue.4 , pp. 284-289
    • Scott, J.E.1
  • 118
    • 0034232654 scopus 로고    scopus 로고
    • Decorin antisense gene therapy improves functional healing of early rabbit ligament scar with enhanced collagen fibrillogenesis in vivo
    • N. Nakamura, D. A. Hart, R. S. Boorman, Y. Kaneda, N. G. Shrive, L. L. Marchuk, K. Shino, T. Ochi and C. B. Frank: Decorin antisense gene therapy improves functional healing of early rabbit ligament scar with enhanced collagen fibrillogenesis in vivo. J Orthop Res, 18, 517-23 (2000)
    • (2000) J Orthop Res , vol.18 , pp. 517-523
    • Nakamura, N.1    Hart, D.A.2    Boorman, R.S.3    Kaneda, Y.4    Shrive, N.G.5    Marchuk, L.L.6    Shino, K.7    Ochi, T.8    Frank, C.B.9
  • 119
    • 0027717615 scopus 로고
    • Binding of fibromodulin and decorin to separate sites on fibrillar collagens
    • E. Hedbom and D. Heinegard: Binding of fibromodulin and decorin to separate sites on fibrillar collagens. J Biol Chem, 268, 27307-12 (1993)
    • (1993) J Biol Chem , vol.268 , pp. 27307-28212
    • Hedbom, E.1    Heinegard, D.2
  • 120
    • 0343851686 scopus 로고    scopus 로고
    • Fibromodulin and lumican bind to the same region on collagen type I fibrils
    • DOI 10.1016/S0014-5793(00)01314-4, PII S0014579300013144
    • L. Svensson, I. Narlid and A. Oldberg: Fibromodulin and lumican bind to the same region on collagen type I fibrils. FEBS Lett, 470, 178-82 (2000) (Pubitemid 30151092)
    • (2000) FEBS Letters , vol.470 , Issue.2 , pp. 178-182
    • Svensson, L.1    Narlid, I.2    Oldberg, A.3
  • 121
    • 0034645039 scopus 로고    scopus 로고
    • Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons
    • Y. Ezura, S. Chakravarti, A. Oldberg, I. Chervoneva and D. E. Birk: Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons. J Cell Biol, 151, 779-88 (2000)
    • (2000) J Cell Biol , vol.151 , pp. 779-788
    • Ezura, Y.1    Chakravarti, S.2    Oldberg, A.3    Chervoneva, I.4    Birk, D.E.5
  • 122
    • 0031570755 scopus 로고    scopus 로고
    • Mechanical loading and TGF-β regulate proteoglycan synthesis in tendon
    • DOI 10.1006/abbi.1997.0102
    • J. R. Robbins, S. P. Evanko and K. G. Vogel: Mechanical loading and TGF-beta regulate proteoglycan synthesis in tendon. Arch Biochem Biophys, 342, 203-11 (1997) (Pubitemid 27251240)
    • (1997) Archives of Biochemistry and Biophysics , vol.342 , Issue.2 , pp. 203-211
    • Robbins, J.R.1    Evanko, S.P.2    Vogel, K.G.3
  • 123
    • 0029560104 scopus 로고
    • Fibrocartilage associated with human tendons and their pulleys
    • M. Benjamin, S. Qin and J. R. Ralphs: Fibrocartilage associated with human tendons and their pulleys. J Anat, 187 (Pt 3), 625-33 (1995) (Pubitemid 26015734)
    • (1995) Journal of Anatomy , vol.187 , Issue.3 , pp. 625-633
    • Benjamin, M.1    Qin, S.2    Ralphs, J.R.3
  • 124
    • 0032414655 scopus 로고    scopus 로고
    • Fibrocartilage in tendons and ligaments - An adaptation to compressive load
    • DOI 10.1017/S0021878298004300
    • M. Benjamin and J. R. Ralphs: Fibrocartilage in tendons and ligaments-an adaptation to compressive load. J Anat, 193 (Pt 4), 481-94 (1998) (Pubitemid 29026948)
    • (1998) Journal of Anatomy , vol.193 , Issue.4 , pp. 481-494
    • Benjamin, M.1    Ralphs, J.R.2
  • 125
    • 0033112846 scopus 로고    scopus 로고
    • Identification and distribution of type VI collagen in tendon fibrocartilages
    • S. L. Felisbino and H. F. Carvalho: Identification and distribution of type VI collagen in tendon fibrocartilages. J Submicrosc Cytol Pathol, 31, 187-95 (1999) (Pubitemid 129553491)
    • (1999) Journal of Submicroscopic Cytology and Pathology , vol.31 , Issue.2 , pp. 187-195
    • Felisbino, S.L.1    Carvalho, H.F.2
  • 126
    • 0029096337 scopus 로고
    • Structure and histopathology of the insertional region of the human Achilles tendon
    • A. Rufai, J. R. Ralphs and M. Benjamin: Structure and histopathology of the insertional region of the human Achilles tendon. J Orthop Res, 13, 585-93 (1995)
    • (1995) J Orthop Res , vol.13 , pp. 585-593
    • Rufai, A.1    Ralphs, J.R.2    Benjamin, M.3
  • 127
    • 0029762075 scopus 로고    scopus 로고
    • Ultrastructure of fibrocartilages at the insertion of the rat Achilles tendon
    • A. Rufai, J. R. Ralphs and M. Benjamin: Ultrastructure of fibrocartilages at the insertion of the rat Achilles tendon. J Anat, 189 (Pt 1), 185-91 (1996) (Pubitemid 26280549)
    • (1996) Journal of Anatomy , vol.189 , Issue.1 , pp. 185-191
    • Rufai, A.1    Ralphs, J.R.2    Benjamin, M.3
  • 128
    • 0031952079 scopus 로고    scopus 로고
    • Characterization of collagens and proteoglycans at the insertion of the human Achilles tendon
    • DOI 10.1016/S0945-053X(98)90017-8
    • A. D. Waggett, J. R. Ralphs, A. P. Kwan, D. Woodnutt and M. Benjamin: Characterization of collagens and proteoglycans at the insertion of the human Achilles tendon. Matrix Biol, 16, 457-70 (1998) (Pubitemid 28132525)
    • (1998) Matrix Biology , vol.16 , Issue.8 , pp. 457-470
    • Waggett, A.D.1    Ralphs, J.R.2    Kwan, A.P.L.3    Woodnutt, D.4    Benjamin, M.5
  • 129
    • 2442661886 scopus 로고    scopus 로고
    • Contralateral tendon rupture risk is increased in individuals with a previous Achilles tendon rupture
    • DOI 10.1111/j.1600-0838.2004.00344.x
    • A. Aroen, D. Helgo, O. G. Granlund and R. Bahr: Contralateral tendon rupture risk is increased in individuals with a previous Achilles tendon rupture. Scand J Med Sci Sports, 14, 30-3 (2004) (Pubitemid 38655999)
    • (2004) Scandinavian Journal of Medicine and Science in Sports , vol.14 , Issue.1 , pp. 30-33
    • Aroen, A.1    Helgo, D.2    Granlund, O.G.3    Bahr, R.4
  • 130
    • 34447324100 scopus 로고    scopus 로고
    • Genetics: Does it play a role in tendinopathy?
    • DOI 10.1097/JSM.0b013e3180425879, PII 0004275220070700000001
    • M. Magra and N. Maffulli: Genetics: does it play a role in tendinopathy? Clin J Sport Med, 17, 231-3 (2007) (Pubitemid 47051781)
    • (2007) Clinical Journal of Sport Medicine , vol.17 , Issue.4 , pp. 231-233
    • Magra, M.1    Maffulli, N.2
  • 132
    • 0035097947 scopus 로고    scopus 로고
    • Histopathological assessment and pathological significance of matrix degeneration in supraspinatus tendons [4]
    • G. P. Riley, M. J. Goddard and B. L. Hazleman: Histopathological assessment and pathological significance of matrix degeneration in supraspinatus tendons. Rheumatology (Oxford), 40, 229-30 (2001) (Pubitemid 32229649)
    • (2001) Rheumatology , vol.40 , Issue.2 , pp. 229-230
    • Riley, G.P.1    Goddard, M.J.2    Hazleman, B.L.3
  • 133
    • 0035213312 scopus 로고    scopus 로고
    • Ruptured Achilles tendons are significantly more degenerated than tendinopathic tendons
    • C. Tallon, N. Maffulli and S. W. Ewen: Ruptured Achilles tendons are significantly more degenerated than tendinopathic tendons. Med Sci Sports Exerc, 33, 1983-90 (2001) (Pubitemid 33126687)
    • (2001) Medicine and Science in Sports and Exercise , vol.33 , Issue.12 , pp. 1983-1990
    • Tallon, C.1    Maffulli, N.2    Ewen, S.W.B.3
  • 134
    • 0026339892 scopus 로고
    • Histopathological changes preceding spontaneous rupture of a tendon. A controlled study of 891 patients
    • P. Kannus and L. Jozsa: Histopathological changes preceding spontaneous rupture of a tendon. A controlled study of 891 patients. J Bone Joint Surg Am, 73, 1507-25 (1991)
    • (1991) J Bone Joint Surg Am , vol.73 , pp. 1507-1525
    • Kannus, P.1    Jozsa, L.2
  • 135
    • 0028243182 scopus 로고
    • Tendon degeneration and chronic shoulder pain: Changes in the collagen composition of the human rotator cuff tendons in rotator cuff tendinitis
    • G. P. Riley, R. L. Harrall, C. R. Constant, M. D. Chard, T. E. Cawston and B. L. Hazleman: Tendon degeneration and chronic shoulder pain: changes in the collagen composition of the human rotator cuff tendons in rotator cuff tendinitis. Ann Rheum Dis, 53, 359-66 (1994) (Pubitemid 24198922)
    • (1994) Annals of the Rheumatic Diseases , vol.53 , Issue.6 , pp. 359-366
    • Riley, G.P.1    Harrall, H.2    Constant, C.R.3    Chard, M.D.4    Cawston, T.E.5    Hazleman, B.L.6
  • 136
    • 0033033926 scopus 로고    scopus 로고
    • Lysylhydroxylation and non-reducible crosslinking of human supraspinatus tendon collagen: Changes with age and in chronic rotator cuff tendinitis
    • R. A. Bank, J. M. TeKoppele, G. Oostingh, B. L. Hazleman and G. P. Riley: Lysylhydroxylation and nonreducible crosslinking of human supraspinatus tendon collagen: changes with age and in chronic rotator cuff tendinitis. Ann Rheum Dis, 58, 35-41 (1999) (Pubitemid 29112948)
    • (1999) Annals of the Rheumatic Diseases , vol.58 , Issue.1 , pp. 35-41
    • Bank, R.A.1    Tekoppele, J.M.2    Oostingh, G.3    Hazleman, B.L.4    Riley, G.P.5
  • 137
    • 0017405466 scopus 로고
    • Interaction between collagen type I and type III in conditioning bundles organization
    • C. M. Lapiere, B. Nusgens and G. E. Pierard: Interaction between collagen type I and type III in conditioning bundles organization. Connect Tissue Res, 5, 21-9 (1977) (Pubitemid 8107770)
    • (1977) Connective Tissue Research , vol.5 , Issue.1 , pp. 21-29
    • Lapiere Ch., M.1    Nusgens, B.2    Pierard, G.E.3
  • 138
    • 0036067595 scopus 로고    scopus 로고
    • Collagen fibril size and crimp morphology in ruptured and intact Achilles tendons
    • DOI 10.1016/S0945-053X(02)00011-2, PII S0945053X02000112
    • S. P. Magnusson, K. Qvortrup, J. O. Larsen, S. Rosager, P. Hanson, P. Aagaard, M. Krogsgaard and M. Kjaer: Collagen fibril size and crimp morphology in ruptured and intact Achilles tendons. Matrix Biol, 21, 369-77 (2002) (Pubitemid 34786473)
    • (2002) Matrix Biology , vol.21 , Issue.4 , pp. 369-377
    • Magnusson, S.P.1    Qvortrup, K.2    Larsen, J.O.3    Rosager, S.4    Hanson, P.5    Aagaard, P.6    Krogsgaard, M.7    Kjaer, M.8
  • 140
    • 0034985628 scopus 로고    scopus 로고
    • Multiple changes in gene expression in chronic human Achilles tendinopathy
    • DOI 10.1016/S0945-053X(01)00128-7, PII S0945053X01001287
    • D. Ireland, R. Harrall, V. Curry, G. Holloway, R. Hackney, B. Hazleman and G. Riley: Multiple changes in gene expression in chronic human Achilles tendinopathy. Matrix Biol, 20, 159-69 (2001) (Pubitemid 32564929)
    • (2001) Matrix Biology , vol.20 , Issue.3 , pp. 159-169
    • Ireland, D.1    Harrall, R.2    Curry, V.3    Holloway, G.4    Hackney, R.5    Hazleman, B.6    Riley, G.7
  • 141
    • 0141634183 scopus 로고    scopus 로고
    • CDNA-arrays and real-time quantitative PCR techniques in the investigation of chronic achilles tendinosis
    • DOI 10.1016/S0736-0266(03)00107-4
    • H. Alfredson, M. Lorentzon, S. Backman, A. Backman and U. H. Lerner: cDNA-arrays and real-time quantitative PCR techniques in the investigation of chronic Achilles tendinosis. J Orthop Res, 21, 970-5 (2003) (Pubitemid 37322376)
    • (2003) Journal of Orthopaedic Research , vol.21 , Issue.6 , pp. 970-975
    • Alfredson, H.1    Lorentzon, M.2    Backman, S.3    Backman, A.4    Lerner, U.H.5
  • 142
    • 4243057336 scopus 로고    scopus 로고
    • Versican splice variant messenger RNA expression in normal human Achilles tendon and tendinopathies
    • DOI 10.1093/rheumatology/keh222
    • A. N. Corps, A. H. Robinson, T. Movin, M. L. Costa, D. C. Ireland, B. L. Hazleman and G. P. Riley: Versican splice variant messenger RNA expression in normal human Achilles tendon and tendinopathies. Rheumatology (Oxford), 43, 969-72 (2004) (Pubitemid 39144442)
    • (2004) Rheumatology , vol.43 , Issue.8 , pp. 969-972
    • Corps, A.N.1    Robinson, A.H.N.2    Movin, T.3    Costa, M.L.4    Ireland, D.C.5    Hazleman, B.L.6    Riley, G.P.7
  • 143
    • 0034858448 scopus 로고    scopus 로고
    • In vivo microdialysis and immunohistochemical analyses of tendon tissue demonstrated high amounts of free glutamate and glutamate NMDAR1 receptors, but no signs of inflammation, in Jumper's knee
    • DOI 10.1016/S0736-0266(01)00016-X, PII S073602660100016X
    • H. Alfredson, S. Forsgren, K. Thorsen and R. Lorentzon: In vivo microdialysis and immunohistochemical analyses of tendon tissue demonstrated high amounts of free glutamate and glutamate NMDAR1 receptors, but no signs of inflammation, in Jumper's knee. J Orthop Res, 19, 881-6 (2001) (Pubitemid 32799078)
    • (2001) Journal of Orthopaedic Research , vol.19 , Issue.5 , pp. 881-886
    • Alfredson, H.1    Forsgren, S.2    Thorsen, K.3    Lorentzon, R.4
  • 144
    • 27644464348 scopus 로고    scopus 로고
    • Matrix metalloproteases: A role in overuse tendinopathies
    • DOI 10.1136/bjsm.2005.017855
    • M. Magra and N. Maffulli: Matrix metalloproteases: a role in overuse tendinopathies. Br J Sports Med, 39, 789-91 (2005) (Pubitemid 41564911)
    • (2005) British Journal of Sports Medicine , vol.39 , Issue.11 , pp. 789-791
    • Magra, M.1    Maffulli, N.2
  • 145
    • 31044442569 scopus 로고    scopus 로고
    • Chronic tendon pathology: Molecular basis and therapeutic implications
    • G. Riley: Chronic tendon pathology: molecular basis and therapeutic implications. Expert Rev Mol Med, 7, 1-25 (2005)
    • (2005) Expert Rev Mol Med , vol.7 , pp. 1-25
    • Riley, G.1


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