메뉴 건너뛰기




Volumn 30, Issue 1, 2011, Pages 53-61

Dysfunctional tendon collagen fibrillogenesis in collagen VI null mice

Author keywords

Collagen VI; Collagen VI null mouse; Development; Fibrillogenesis; Tendon; Tendon biomechanics

Indexed keywords

COLLAGEN FIBRIL; COLLAGEN TYPE 6; COLLAGEN TYPE 6A1; LEUCINE; MATRIX METALLOPROTEINASE; PROTEOGLYCAN; UNCLASSIFIED DRUG;

EID: 78951490506     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.matbio.2010.10.001     Document Type: Article
Times cited : (88)

References (46)
  • 1
    • 61649119401 scopus 로고    scopus 로고
    • Developmental and osteoarthritic changes in Col6a1-knockout mice: biomechanics of type VI collagen in the cartilage pericellular matrix
    • Alexopoulos L.G., Youn I., Bonaldo P., Guilak F. Developmental and osteoarthritic changes in Col6a1-knockout mice: biomechanics of type VI collagen in the cartilage pericellular matrix. Arthritis Rheum. 2009, 60:771-779.
    • (2009) Arthritis Rheum. , vol.60 , pp. 771-779
    • Alexopoulos, L.G.1    Youn, I.2    Bonaldo, P.3    Guilak, F.4
  • 2
    • 0036235834 scopus 로고    scopus 로고
    • Abnormal collagen fibrils in tendons of biglycan/fibromodulin-deficient mice lead to gait impairment, ectopic ossification, and osteoarthritis
    • Ameye L., Aria D., Jepsen K., Oldberg A., Xu T., Young M.F. Abnormal collagen fibrils in tendons of biglycan/fibromodulin-deficient mice lead to gait impairment, ectopic ossification, and osteoarthritis. FASEB J. 2002, 16:673-680.
    • (2002) FASEB J. , vol.16 , pp. 673-680
    • Ameye, L.1    Aria, D.2    Jepsen, K.3    Oldberg, A.4    Xu, T.5    Young, M.F.6
  • 3
    • 0036744260 scopus 로고    scopus 로고
    • Mice deficient in small leucine-rich proteoglycans: novel in vivo models for osteoporosis, osteoarthritis, Ehlers-Danlos syndrome, muscular dystrophy, and corneal diseases
    • Ameye L., Young M.F. Mice deficient in small leucine-rich proteoglycans: novel in vivo models for osteoporosis, osteoarthritis, Ehlers-Danlos syndrome, muscular dystrophy, and corneal diseases. Glycobiology 2002, 12:107R-116R.
    • (2002) Glycobiology , vol.12
    • Ameye, L.1    Young, M.F.2
  • 5
    • 0003054974 scopus 로고
    • Collagen fibril assembly, depostion, and organization into tissue-specific matrices
    • Academic Press, NY, P.D. Yurchenco, D.E. Birk, R.P. Mecham (Eds.)
    • Birk D.E., Linsenmayer T.F. Collagen fibril assembly, depostion, and organization into tissue-specific matrices. Extracellular Matrix Assembly and Structure 1994, 91-128. Academic Press, NY. P.D. Yurchenco, D.E. Birk, R.P. Mecham (Eds.).
    • (1994) Extracellular Matrix Assembly and Structure , pp. 91-128
    • Birk, D.E.1    Linsenmayer, T.F.2
  • 6
    • 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
    • Birk D.E., Mayne R. 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. 1997, 72:352-361.
    • (1997) Eur. J. Cell Biol. , vol.72 , pp. 352-361
    • Birk, D.E.1    Mayne, R.2
  • 8
    • 0022470549 scopus 로고
    • Extracellular compartments in tendon morphogenesis: collagen fibril, bundle, and macroaggregate formation
    • Birk D.E., Trelstad R.L. Extracellular compartments in tendon morphogenesis: collagen fibril, bundle, and macroaggregate formation. J. Cell Biol. 1986, 103:231-240.
    • (1986) J. Cell Biol. , vol.103 , pp. 231-240
    • Birk, D.E.1    Trelstad, R.L.2
  • 9
    • 2542553125 scopus 로고
    • Collagen fibrillogenesis in situ: fibril segments are intermediates in matrix assembly
    • Birk D.E., Zycband E.I., Winkelmann D.A., Trelstad R.L. Collagen fibrillogenesis in situ: fibril segments are intermediates in matrix assembly. Proc. Natl Acad. Sci. USA 1989, 86:4549-4553.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 4549-4553
    • Birk, D.E.1    Zycband, E.I.2    Winkelmann, D.A.3    Trelstad, R.L.4
  • 10
    • 0031760509 scopus 로고    scopus 로고
    • Collagen VI deficiency induces early onset myopathy in the mouse: an animal model for Bethlem myopathy
    • Bonaldo P., Braghetta P., Zanetti M., Piccolo S., Volpin D., Bressan G.M. Collagen VI deficiency induces early onset myopathy in the mouse: an animal model for Bethlem myopathy. Hum. Mol. Genet. 1998, 7:2135-2140.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 2135-2140
    • Bonaldo, P.1    Braghetta, P.2    Zanetti, M.3    Piccolo, S.4    Volpin, D.5    Bressan, G.M.6
  • 11
    • 0025060809 scopus 로고
    • Structural and functional features of the alpha 3 chain indicate a bridging role for chicken collagen VI in connective tissues
    • Bonaldo P., Russo V., Bucciotti F., Doliana R., Colombatti A. Structural and functional features of the alpha 3 chain indicate a bridging role for chicken collagen VI in connective tissues. Biochemistry 1990, 29:1245-1254.
    • (1990) Biochemistry , vol.29 , pp. 1245-1254
    • Bonaldo, P.1    Russo, V.2    Bucciotti, F.3    Doliana, R.4    Colombatti, A.5
  • 12
    • 11844298904 scopus 로고    scopus 로고
    • The role of thrombospondins 1 and 2 in the regulation of cell-matrix interactions, collagen fibril formation, and the response to injury
    • Bornstein P., Agah A., Kyriakides T.R. The role of thrombospondins 1 and 2 in the regulation of cell-matrix interactions, collagen fibril formation, and the response to injury. Int. J. Biochem. Cell Biol. 2004, 36:1115-1125.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 1115-1125
    • Bornstein, P.1    Agah, A.2    Kyriakides, T.R.3
  • 14
    • 0022547414 scopus 로고
    • Type VI collagen in extracellular, 100-nm periodic filaments and fibrils: identification by immunoelectron microscopy
    • Bruns R.R., Press W., Engvall E., Timpl R., Gross J. Type VI collagen in extracellular, 100-nm periodic filaments and fibrils: identification by immunoelectron microscopy. J. Cell Biol. 1986, 103:393-404.
    • (1986) J. Cell Biol. , vol.103 , pp. 393-404
    • Bruns, R.R.1    Press, W.2    Engvall, E.3    Timpl, R.4    Gross, J.5
  • 16
    • 17844373840 scopus 로고    scopus 로고
    • Procollagen trafficking, processing and fibrillogenesis
    • Canty E.G., Kadler K.E. Procollagen trafficking, processing and fibrillogenesis. J. Cell Sci. 2005, 118:1341-1353.
    • (2005) J. Cell Sci. , vol.118 , pp. 1341-1353
    • Canty, E.G.1    Kadler, K.E.2
  • 17
    • 2542439729 scopus 로고    scopus 로고
    • Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon
    • Canty E.G., Lu Y., Meadows R.S., Shaw M.K., Holmes D.F., Kadler K.E. Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon. J. Cell Biol. 2004, 165:553-563.
    • (2004) J. Cell Biol. , vol.165 , pp. 553-563
    • Canty, E.G.1    Lu, Y.2    Meadows, R.S.3    Shaw, M.K.4    Holmes, D.F.5    Kadler, K.E.6
  • 20
    • 0031044872 scopus 로고    scopus 로고
    • Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
    • Danielson K.G., Baribault H., Holmes D.F., Graham H., Kadler K.E., Iozzo R.V. Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J. Cell Biol. 1997, 136:729-743.
    • (1997) J. Cell Biol. , vol.136 , 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
  • 21
    • 0028519254 scopus 로고
    • A new optical system for the determination of deformations and strains: calibration characteristics and experimental results
    • Derwin K.A., Soslowsky L.J., Green W.D., Elder S.H. A new optical system for the determination of deformations and strains: calibration characteristics and experimental results. J. Biomech. 1994, 27:1277-1285.
    • (1994) J. Biomech. , vol.27 , pp. 1277-1285
    • Derwin, K.A.1    Soslowsky, L.J.2    Green, W.D.3    Elder, S.H.4
  • 22
    • 0034645039 scopus 로고    scopus 로고
    • Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons
    • Ezura Y., Chakravarti S., Oldberg A., Chervoneva I., Birk D.E. Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons. J. Cell Biol. 2000, 151:779-788.
    • (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
  • 23
    • 78951482867 scopus 로고    scopus 로고
    • Scarless healing in the fetus: implications and strategies for postnatal tendon repair. Bioengineering 216. Philadelphia, PA, University of Pennsylvania. Ref Type: Thesis/Dissertation
    • Favata, M., 2006. Scarless healing in the fetus: implications and strategies for postnatal tendon repair. Bioengineering 216. Philadelphia, PA, University of Pennsylvania. Ref Type: Thesis/Dissertation.
    • (2006)
    • Favata, M.1
  • 24
    • 50649101286 scopus 로고    scopus 로고
    • Three novel collagen VI chains, alpha4(VI), alpha5(VI), and alpha6(VI)
    • Fitzgerald J., Rich C., Zhou F.H., Hansen U. Three novel collagen VI chains, alpha4(VI), alpha5(VI), and alpha6(VI). J. Biol. Chem. 2008, 283:20170-20180.
    • (2008) J. Biol. Chem. , vol.283 , pp. 20170-20180
    • Fitzgerald, J.1    Rich, C.2    Zhou, F.H.3    Hansen, U.4
  • 25
    • 0020632037 scopus 로고
    • Electron-microscopical approach to a structural model of intima collagen
    • Furthmayr H., Wiedemann H., Timpl R., Odermatt E., Engel J. Electron-microscopical approach to a structural model of intima collagen. Biochem. J. 1983, 211:303-311.
    • (1983) Biochem. J. , vol.211 , pp. 303-311
    • Furthmayr, H.1    Wiedemann, H.2    Timpl, R.3    Odermatt, E.4    Engel, J.5
  • 29
    • 79959350640 scopus 로고    scopus 로고
    • Collagen fibril growth during chicken tendon development: matrix metalloproteinase-2 and its activation
    • Jung J.C., Wang P.X., Zhang G., Ezura Y., Fini M.E., Birk D.E. Collagen fibril growth during chicken tendon development: matrix metalloproteinase-2 and its activation. Cell Tissue Res. 2009, 336:79-89.
    • (2009) Cell Tissue Res. , vol.336 , pp. 79-89
    • Jung, J.C.1    Wang, P.X.2    Zhang, G.3    Ezura, Y.4    Fini, M.E.5    Birk, D.E.6
  • 31
    • 0023821420 scopus 로고
    • Ultrastructure of type VI collagen in human skin and cartilage suggests an anchoring function for this filamentous network
    • Keene D.R., Engvall E., Glanville R.W. Ultrastructure of type VI collagen in human skin and cartilage suggests an anchoring function for this filamentous network. J. Cell Biol. 1988, 107:1995-2006.
    • (1988) J. Cell Biol. , vol.107 , pp. 1995-2006
    • Keene, D.R.1    Engvall, E.2    Glanville, R.W.3
  • 32
    • 0002846317 scopus 로고    scopus 로고
    • The collagen family: structure, assembly, and organization in the extracellular matrix
    • Wiley-Liss, New York, P.M. Royce, B. Steinmann (Eds.)
    • Kielty C.M., Grant M.E. The collagen family: structure, assembly, and organization in the extracellular matrix. Connective tissue and its heritable disorders 2002, 159-222. Wiley-Liss, New York. P.M. Royce, B. Steinmann (Eds.).
    • (2002) Connective tissue and its heritable disorders , pp. 159-222
    • Kielty, C.M.1    Grant, M.E.2
  • 34
    • 0032567684 scopus 로고    scopus 로고
    • Mice that lack thrombospondin 2 display connective tissue abnormalities that are associated with disordered collagen fibrillogenesis, an increased vascular density, and a bleeding diathesis
    • Kyriakides T.R., Zhu Y.H., Smith L.T., Bain S.D., Yang Z., Lin M.T., Danielson K.G., Iozzo R.V., LaMarca M., McKinney C.E., Ginns E.I., Bornstein P. Mice that lack thrombospondin 2 display connective tissue abnormalities that are associated with disordered collagen fibrillogenesis, an increased vascular density, and a bleeding diathesis. J. Cell Biol. 1998, 140:419-430.
    • (1998) J. Cell Biol. , vol.140 , pp. 419-430
    • Kyriakides, T.R.1    Zhu, Y.H.2    Smith, L.T.3    Bain, S.D.4    Yang, Z.5    Lin, M.T.6    Danielson, K.G.7    Iozzo, R.V.8    LaMarca, M.9    McKinney, C.E.10    Ginns, E.I.11    Bornstein, P.12
  • 35
    • 24944559356 scopus 로고    scopus 로고
    • Collagen VI related muscle disorders
    • Lampe A.K., Bushby K.M. Collagen VI related muscle disorders. J. Med. Genet. 2005, 42:673-685.
    • (2005) J. Med. Genet. , vol.42 , pp. 673-685
    • Lampe, A.K.1    Bushby, K.M.2
  • 36
    • 0029815475 scopus 로고    scopus 로고
    • Differential expression of fibromodulin mRNA associated with tendon fibril growth: isolation and characterization of a chicken fibromodulin cDNA
    • Nurminskaya M.V., Birk D.E. Differential expression of fibromodulin mRNA associated with tendon fibril growth: isolation and characterization of a chicken fibromodulin cDNA. Biochem. J. 1996, 317:785-789.
    • (1996) Biochem. J. , vol.317 , pp. 785-789
    • Nurminskaya, M.V.1    Birk, D.E.2
  • 37
    • 16244403925 scopus 로고    scopus 로고
    • Influence of decorin and biglycan on mechanical properties of multiple tendons in knockout mice
    • Robinson P.S., Huang T.F., Kazam E., Iozzo R.V., Birk D.E., Soslowsky L.J. Influence of decorin and biglycan on mechanical properties of multiple tendons in knockout mice. J. Biomech. Eng. 2005, 127:181-185.
    • (2005) J. Biomech. Eng. , vol.127 , pp. 181-185
    • Robinson, P.S.1    Huang, T.F.2    Kazam, E.3    Iozzo, R.V.4    Birk, D.E.5    Soslowsky, L.J.6
  • 38
    • 0040436000 scopus 로고    scopus 로고
    • Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon
    • Svensson L., Aszodi A., Reinholt F.P., Fassler R., Heinegard D., Oldberg A. Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon. J. Biol. Chem. 1999, 274:9636-9647.
    • (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
  • 39
    • 0027947233 scopus 로고
    • Recombinant expression and structural and binding properties of alpha 1(VI) and alpha 2(VI) chains of human collagen type VI
    • Tillet E., Wiedemann H., Golbik R., Pan T.C., Zhang R.Z., Mann K., Chu M.L., Timpl R. Recombinant expression and structural and binding properties of alpha 1(VI) and alpha 2(VI) chains of human collagen type VI. Eur. J. Biochem. 1994, 221:177-185.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 177-185
    • Tillet, E.1    Wiedemann, H.2    Golbik, R.3    Pan, T.C.4    Zhang, R.Z.5    Mann, K.6    Chu, M.L.7    Timpl, R.8
  • 40
    • 0018762445 scopus 로고
    • Tendon collagen fibrillogenesis: intracellular subassemblies and cell surface changes associated with fibril growth
    • Trelstad R.L., Hayashi K. Tendon collagen fibrillogenesis: intracellular subassemblies and cell surface changes associated with fibril growth. Dev. Biol. 1979, 71:228-242.
    • (1979) Dev. Biol. , vol.71 , pp. 228-242
    • Trelstad, R.L.1    Hayashi, K.2
  • 42
    • 0345894336 scopus 로고    scopus 로고
    • Biglycan organizes collagen VI into hexagonal-like networks resembling tissue structures
    • Wiberg C., Heinegard D., Wenglen C., Timpl R., Morgelin M. Biglycan organizes collagen VI into hexagonal-like networks resembling tissue structures. J. Biol. Chem. 2002, 277:49120-49126.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49120-49126
    • Wiberg, C.1    Heinegard, D.2    Wenglen, C.3    Timpl, R.4    Morgelin, M.5
  • 43
    • 0035896646 scopus 로고    scopus 로고
    • Extracellular matrix metalloproteinase 2 levels are regulated by the low density lipoprotein-related scavenger receptor and thrombospondin 2
    • Yang Z., Strickland D.K., Bornstein P. Extracellular matrix metalloproteinase 2 levels are regulated by the low density lipoprotein-related scavenger receptor and thrombospondin 2. J. Biol. Chem. 2001, 276:8403-8408.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8403-8408
    • Yang, Z.1    Strickland, D.K.2    Bornstein, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.