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Volumn 37, Issue , 2014, Pages 183-191

Matricellular proteins and biomaterials

Author keywords

Biocompatible; Biomaterials; Decellularization; Extracellular matrix; Foreign body response; Matricellular

Indexed keywords

BIOMIMETIC MATERIAL; CCN PROTEIN; MATRICELLULAR PROTEIN; OSTEONECTIN; OSTEOPONTIN; PROTEIN; TENASCIN; THROMBOSPONDIN 1; THROMBOSPONDIN 2; TRANSCRIPTION FACTOR RUNX2; UNCLASSIFIED DRUG; BIOMATERIAL; CELL ADHESION MOLECULE; POSTN PROTEIN, HUMAN; SCLEROPROTEIN; SPARC PROTEIN, HUMAN; THROMBOSPONDIN;

EID: 84908281707     PISSN: 0945053X     EISSN: 15691802     Source Type: Journal    
DOI: 10.1016/j.matbio.2014.03.002     Document Type: Review
Times cited : (53)

References (125)
  • 2
    • 0036731861 scopus 로고    scopus 로고
    • The lack of thrombospondin-1 (TSP1) dictates the course of wound healing in double-TSP1/TSP2-null mice
    • Agah A., Kyriakides T.R., Lawler J., Bornstein P. The lack of thrombospondin-1 (TSP1) dictates the course of wound healing in double-TSP1/TSP2-null mice. Am. J. Pathol. 2002, 161:831-839.
    • (2002) Am. J. Pathol. , vol.161 , pp. 831-839
    • Agah, A.1    Kyriakides, T.R.2    Lawler, J.3    Bornstein, P.4
  • 3
    • 33745520093 scopus 로고    scopus 로고
    • Three-dimensional nanofibrillar surfaces covalently modified with tenascin-C-derived peptides enhance neuronal growth in vitro
    • Ahmed I., Liu H.-Y., Mamiya P.C., Ponery A.S., Babu A.N., Weik T., Schindler M., Meiners S. Three-dimensional nanofibrillar surfaces covalently modified with tenascin-C-derived peptides enhance neuronal growth in vitro. J. Biomed. Mater. Res. A 2005, 76:851-860.
    • (2005) J. Biomed. Mater. Res. A , vol.76 , pp. 851-860
    • Ahmed, I.1    Liu, H.-Y.2    Mamiya, P.C.3    Ponery, A.S.4    Babu, A.N.5    Weik, T.6    Schindler, M.7    Meiners, S.8
  • 4
    • 33746561028 scopus 로고    scopus 로고
    • Matricellular proteins: extracellular modulators of bone development, remodeling, and regeneration
    • Alford A.I., Hankenson K.D. Matricellular proteins: extracellular modulators of bone development, remodeling, and regeneration. Bone 2006, 38:749-757.
    • (2006) Bone , vol.38 , pp. 749-757
    • Alford, A.I.1    Hankenson, K.D.2
  • 6
    • 0037360164 scopus 로고    scopus 로고
    • Thrombospondins 1 and 2 function as inhibitors of angiogenesis
    • Armstrong L.C., Bornstein P. Thrombospondins 1 and 2 function as inhibitors of angiogenesis. Matrix Biol. 2003, 22:63-71.
    • (2003) Matrix Biol. , vol.22 , pp. 63-71
    • Armstrong, L.C.1    Bornstein, P.2
  • 7
    • 34249819953 scopus 로고    scopus 로고
    • The extracellular matrix as a biologic scaffold material
    • Badylak S.F. The extracellular matrix as a biologic scaffold material. Biomaterials 2007, 28:3587-3593.
    • (2007) Biomaterials , vol.28 , pp. 3587-3593
    • Badylak, S.F.1
  • 13
    • 72449177328 scopus 로고    scopus 로고
    • Matricellular proteins: an overview
    • Bornstein P. Matricellular proteins: an overview. J. Cell Commun. Signal. 2009, 3:163-165.
    • (2009) J. Cell Commun. Signal. , vol.3 , pp. 163-165
    • Bornstein, P.1
  • 14
    • 0036775425 scopus 로고    scopus 로고
    • Matricellular proteins: extracellular modulators of cell function
    • Bornstein P., Sage E.H. Matricellular proteins: extracellular modulators of cell function. Curr. Opin. Cell Biol. 2002, 14:608-616.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 608-616
    • Bornstein, P.1    Sage, E.H.2
  • 16
    • 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
  • 17
    • 33749454574 scopus 로고    scopus 로고
    • Electrospinning approaches toward scaffold engineering-a brief overview
    • Boudriot U., Dersch R., Greiner A., WendorffJ.H. Electrospinning approaches toward scaffold engineering-a brief overview. Artif. Organs 2006, 30:785-792.
    • (2006) Artif. Organs , vol.30 , pp. 785-792
    • Boudriot, U.1    Dersch, R.2    Greiner, A.3    Wendorff, J.H.4
  • 20
    • 72449202606 scopus 로고    scopus 로고
    • The role of SPARC in extracellular matrix assembly
    • Bradshaw A.D. The role of SPARC in extracellular matrix assembly. J. Cell Commun. Signal. 2009, 3:239-246.
    • (2009) J. Cell Commun. Signal. , vol.3 , pp. 239-246
    • Bradshaw, A.D.1
  • 21
    • 0037791886 scopus 로고    scopus 로고
    • SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength
    • Bradshaw A.D., Puolakkainen P., Dasgupta J., Davidson J.M., Wight T.N., Helene Sage E. SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength. J. Invest. Dermatol. 2003, 120:949-955.
    • (2003) J. Invest. Dermatol. , vol.120 , pp. 949-955
    • Bradshaw, A.D.1    Puolakkainen, P.2    Dasgupta, J.3    Davidson, J.M.4    Wight, T.N.5    Helene Sage, E.6
  • 22
    • 0035234139 scopus 로고    scopus 로고
    • SPARC, a matricellular protein: at the crossroads of cell-matrix communication
    • Brekken R.A., Sage E.H. SPARC, a matricellular protein: at the crossroads of cell-matrix communication. Matrix Biol. 2001, 19:816-827.
    • (2001) Matrix Biol. , vol.19 , pp. 816-827
    • Brekken, R.A.1    Sage, E.H.2
  • 24
    • 84862702111 scopus 로고    scopus 로고
    • Engineering biomaterials to integrate and heal: the biocompatibility paradigm shifts
    • Bryers J.D., Giachelli C.M., Ratner B.D. Engineering biomaterials to integrate and heal: the biocompatibility paradigm shifts. Biotechnol. Bioeng. 2012, 109:1898-1911.
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 1898-1911
    • Bryers, J.D.1    Giachelli, C.M.2    Ratner, B.D.3
  • 26
    • 0030421882 scopus 로고    scopus 로고
    • Bioactive materials
    • Cao W., Hench L.L. Bioactive materials. Ceram. Int. 1996, 8842:493-507.
    • (1996) Ceram. Int. , vol.8842 , pp. 493-507
    • Cao, W.1    Hench, L.L.2
  • 27
    • 34848914037 scopus 로고    scopus 로고
    • A multi-functional scaffold for tissue regeneration: the need to engineer a tissue analogue
    • Causa F., Netti P.A., Ambrosio L. A multi-functional scaffold for tissue regeneration: the need to engineer a tissue analogue. Biomaterials 2007, 28:5093-5099.
    • (2007) Biomaterials , vol.28 , pp. 5093-5099
    • Causa, F.1    Netti, P.A.2    Ambrosio, L.3
  • 28
    • 59649107705 scopus 로고    scopus 로고
    • Functions and mechanisms of action of CCN matricellular proteins
    • Chen C.-C., Lau L.F. Functions and mechanisms of action of CCN matricellular proteins. Int. J. Biochem. Cell Biol. 2009, 41:771-783.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 771-783
    • Chen, C.-C.1    Lau, L.F.2
  • 29
    • 0033734494 scopus 로고    scopus 로고
    • The cell biology of thrombospondin-1
    • Chen H., Herndon M.E., Lawler J. The cell biology of thrombospondin-1. Matrix Biol. 2000, 19:597-614.
    • (2000) Matrix Biol. , vol.19 , pp. 597-614
    • Chen, H.1    Herndon, M.E.2    Lawler, J.3
  • 30
    • 84896413871 scopus 로고    scopus 로고
    • Cell spreading and proliferation in response to the composition and mechanics of engineered fibrillar extracellular matrices
    • Chen A.K., Delrio F.W., Peterson A.W., Chung K.-H., Bhadiraju K., Plant A.L. Cell spreading and proliferation in response to the composition and mechanics of engineered fibrillar extracellular matrices. Biotechnol. Bioeng. 2013, 110:2731-2741.
    • (2013) Biotechnol. Bioeng. , vol.110 , pp. 2731-2741
    • Chen, A.K.1    Delrio, F.W.2    Peterson, A.W.3    Chung, K.-H.4    Bhadiraju, K.5    Plant, A.L.6
  • 32
    • 79951775415 scopus 로고    scopus 로고
    • An overview of tissue and whole organ decellularization processes
    • Crapo P.M., Gilbert T.W., Badylak S.F. An overview of tissue and whole organ decellularization processes. Biomaterials 2011, 32:3233-3243.
    • (2011) Biomaterials , vol.32 , pp. 3233-3243
    • Crapo, P.M.1    Gilbert, T.W.2    Badylak, S.F.3
  • 35
    • 58149105371 scopus 로고    scopus 로고
    • Slow release of growth factors and thrombospondin-1 in Choukroun's platelet-rich fibrin (PRF): a gold standard to achieve for all surgical platelet concentrates technologies
    • Dohan Ehrenfest D.M., de Peppo G.M., Doglioli P., Sammartino G. Slow release of growth factors and thrombospondin-1 in Choukroun's platelet-rich fibrin (PRF): a gold standard to achieve for all surgical platelet concentrates technologies. Growth Factors 2009, 27:63-69.
    • (2009) Growth Factors , vol.27 , pp. 63-69
    • Dohan Ehrenfest, D.M.1    de Peppo, G.M.2    Doglioli, P.3    Sammartino, G.4
  • 36
    • 0027685702 scopus 로고
    • Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions
    • Erickson H.P. Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions. Curr. Opin. Cell Biol. 1993, 5:869-876.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 869-876
    • Erickson, H.P.1
  • 37
    • 82355181433 scopus 로고    scopus 로고
    • Characterization of in vitro endothelial linings grown within microfluidic channels
    • Esch M.B., Post D.J., Shuler M.L., Stokol T. Characterization of in vitro endothelial linings grown within microfluidic channels. Tissue Eng. Part A 2011, 17:2965-2971.
    • (2011) Tissue Eng. Part A , vol.17 , pp. 2965-2971
    • Esch, M.B.1    Post, D.J.2    Shuler, M.L.3    Stokol, T.4
  • 38
    • 84860145209 scopus 로고    scopus 로고
    • Matricellular proteins in cardiac adaptation and disease
    • Frangogiannis N.G. Matricellular proteins in cardiac adaptation and disease. Physiol. Rev. 2012, 92:635-688.
    • (2012) Physiol. Rev. , vol.92 , pp. 635-688
    • Frangogiannis, N.G.1
  • 39
    • 84875686716 scopus 로고    scopus 로고
    • Ti based biomaterials, the ultimate choice for orthopaedic implants - a review
    • Geetha M., Singh A.K., Asokamani R., Gogia A.K. Ti based biomaterials, the ultimate choice for orthopaedic implants - a review. Prog. Mater. Sci. 2009, 54:397-425.
    • (2009) Prog. Mater. Sci. , vol.54 , pp. 397-425
    • Geetha, M.1    Singh, A.K.2    Asokamani, R.3    Gogia, A.K.4
  • 40
    • 0033731371 scopus 로고    scopus 로고
    • Osteopontin: a versatile regulator of inflammation and biomineralization
    • Giachelli C.M., Steitz S. Osteopontin: a versatile regulator of inflammation and biomineralization. Matrix Biol. 2000, 19:615-622.
    • (2000) Matrix Biol. , vol.19 , pp. 615-622
    • Giachelli, C.M.1    Steitz, S.2
  • 44
    • 67649184798 scopus 로고    scopus 로고
    • Dentin extracellular matrix molecules implanted into exposed pulps generate reparative dentin: a novel strategy in regenerative dentistry
    • Goldberg M., Six N., Chaussain C., DenBesten P., Veis A., Poliard A. Dentin extracellular matrix molecules implanted into exposed pulps generate reparative dentin: a novel strategy in regenerative dentistry. J. Dent. Res. 2009, 88:396-399.
    • (2009) J. Dent. Res. , vol.88 , pp. 396-399
    • Goldberg, M.1    Six, N.2    Chaussain, C.3    DenBesten, P.4    Veis, A.5    Poliard, A.6
  • 45
    • 0031225015 scopus 로고    scopus 로고
    • Connective tissue growth factor: a mediator of TGF-β action on fibroblasts
    • Grotendorst G.R. Connective tissue growth factor: a mediator of TGF-β action on fibroblasts. Cytokine Growth Factor Rev. 1997, 8(3):171-179.
    • (1997) Cytokine Growth Factor Rev. , vol.8 , Issue.3 , pp. 171-179
    • Grotendorst, G.R.1
  • 46
    • 54949146436 scopus 로고    scopus 로고
    • Functional role of periostin in development and wound repair: implications for connective tissue disease
    • Hamilton D.W. Functional role of periostin in development and wound repair: implications for connective tissue disease. J. Cell Commun. Signal. 2008, 2:9-17.
    • (2008) J. Cell Commun. Signal. , vol.2 , pp. 9-17
    • Hamilton, D.W.1
  • 48
    • 0030034590 scopus 로고    scopus 로고
    • Kinetics of bone cell organization and mineralization on materials with patterned surface chemistry
    • Healy K.E., Thomas C.H., Rezania A., Kim J.E., McKeown P.J., Lom B., Hockberger P.E. Kinetics of bone cell organization and mineralization on materials with patterned surface chemistry. Biomaterials 1996, 17:195-208.
    • (1996) Biomaterials , vol.17 , pp. 195-208
    • Healy, K.E.1    Thomas, C.H.2    Rezania, A.3    Kim, J.E.4    McKeown, P.J.5    Lom, B.6    Hockberger, P.E.7
  • 49
    • 0032143779 scopus 로고    scopus 로고
    • Biomaterials: a forecast for the future
    • Hench L.L. Biomaterials: a forecast for the future. Biomaterials 1998, 19:1419-1423.
    • (1998) Biomaterials , vol.19 , pp. 1419-1423
    • Hench, L.L.1
  • 50
  • 52
    • 22844451608 scopus 로고    scopus 로고
    • Meet the tenascins: multifunctional and mysterious
    • Hsia H.C., Schwarzbauer J.E. Meet the tenascins: multifunctional and mysterious. J. Biol. Chem. 2005, 280:26641-26644.
    • (2005) J. Biol. Chem. , vol.280 , pp. 26641-26644
    • Hsia, H.C.1    Schwarzbauer, J.E.2
  • 55
    • 34547583582 scopus 로고    scopus 로고
    • Periostin: novel diagnostic and therapeutic target for cancer
    • Kudo Y., Hatano H., Ogawa I., Takata T. Periostin: novel diagnostic and therapeutic target for cancer. Histol. Histopathol. 2007, 1:1167-1174.
    • (2007) Histol. Histopathol. , vol.1 , pp. 1167-1174
    • Kudo, Y.1    Hatano, H.2    Ogawa, I.3    Takata, T.4
  • 56
    • 34547691243 scopus 로고    scopus 로고
    • Periostin induces proliferation of differentiated cardiomyocytes and promotes cardiac repair
    • Kühn B., del Monte F., Hajjar R.J., Chang Y.-S., Lebeche D., Arab S., Keating M.T. Periostin induces proliferation of differentiated cardiomyocytes and promotes cardiac repair. Nat. Med. 2007, 13:962-969.
    • (2007) Nat. Med. , vol.13 , pp. 962-969
    • Kühn, B.1    del Monte, F.2    Hajjar, R.J.3    Chang, Y.-S.4    Lebeche, D.5    Arab, S.6    Keating, M.T.7
  • 57
    • 0347674325 scopus 로고    scopus 로고
    • Matricellular proteins as modulators of wound healing and the foreign body response
    • Kyriakides T.R., Bornstein P. Matricellular proteins as modulators of wound healing and the foreign body response. Thromb. Haemost. 2003, 90:986-992.
    • (2003) Thromb. Haemost. , vol.90 , pp. 986-992
    • Kyriakides, T.R.1    Bornstein, P.2
  • 58
    • 72449205070 scopus 로고    scopus 로고
    • The role of thrombospondins in wound healing, ischemia, and the foreign body reaction
    • Kyriakides T.R., Maclauchlan S. The role of thrombospondins in wound healing, ischemia, and the foreign body reaction. J. Cell Commun. Signal. 2009, 3:215-225.
    • (2009) J. Cell Commun. Signal. , vol.3 , pp. 215-225
    • Kyriakides, T.R.1    Maclauchlan, S.2
  • 59
    • 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
  • 60
    • 0033551072 scopus 로고    scopus 로고
    • Mice that lack the angiogenesis inhibitor, thrombospondin 2, mount an altered foreign body reaction characterized by increased vascularity
    • Kyriakides T.R., Leach K.J., Hoffman A.S., Ratner B.D., Bornstein P. Mice that lack the angiogenesis inhibitor, thrombospondin 2, mount an altered foreign body reaction characterized by increased vascularity. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:4449-4454.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4449-4454
    • Kyriakides, T.R.1    Leach, K.J.2    Hoffman, A.S.3    Ratner, B.D.4    Bornstein, P.5
  • 61
    • 0032707093 scopus 로고    scopus 로고
    • Accelerated wound healing in mice with a disruption of the thrombospondin 2 gene
    • Kyriakides T.R., Tam J.W.Y., Bornstein P. Accelerated wound healing in mice with a disruption of the thrombospondin 2 gene. J. Invest. Dermatol. 1999, 113:782-787.
    • (1999) J. Invest. Dermatol. , vol.113 , pp. 782-787
    • Kyriakides, T.R.1    Tam, J.W.Y.2    Bornstein, P.3
  • 62
    • 0034964005 scopus 로고    scopus 로고
    • Regulation of angiogenesis and matrix remodeling by localized, matrix-mediated antisense gene delivery
    • Kyriakides T.R., Hartzel T., Huynh G., Bornstein P. Regulation of angiogenesis and matrix remodeling by localized, matrix-mediated antisense gene delivery. Mol. Ther. 2001, 3:842-849.
    • (2001) Mol. Ther. , vol.3 , pp. 842-849
    • Kyriakides, T.R.1    Hartzel, T.2    Huynh, G.3    Bornstein, P.4
  • 65
    • 13944281786 scopus 로고    scopus 로고
    • Myoblast proliferation and differentiation on fibronectin-coated self assembled monolayers presenting different surface chemistries
    • Lan M.A., Gersbach C.A., Michael K.E., Keselowsky B.G., García A.J. Myoblast proliferation and differentiation on fibronectin-coated self assembled monolayers presenting different surface chemistries. Biomaterials 2005, 26:4523-4531.
    • (2005) Biomaterials , vol.26 , pp. 4523-4531
    • Lan, M.A.1    Gersbach, C.A.2    Michael, K.E.3    Keselowsky, B.G.4    García, A.J.5
  • 66
    • 0033818794 scopus 로고    scopus 로고
    • The functions of thrombospondin-1 and-2
    • Lawler J. The functions of thrombospondin-1 and-2. Curr. Opin. Cell Biol. 2000, 12:634-640.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 634-640
    • Lawler, J.1
  • 67
    • 0023035074 scopus 로고
    • The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins
    • Lawler J., Hynes R.O. The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins. J. Cell Biol. 1986, 103:1635-1648.
    • (1986) J. Cell Biol. , vol.103 , pp. 1635-1648
    • Lawler, J.1    Hynes, R.O.2
  • 68
    • 0026490256 scopus 로고
    • Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein
    • Leahy D.J., Hendrickson W.A., Aukhil I., Erickson H.P. Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 1992, 258:987-991.
    • (1992) Science , vol.258 , pp. 987-991
    • Leahy, D.J.1    Hendrickson, W.A.2    Aukhil, I.3    Erickson, H.P.4
  • 69
    • 0006932322 scopus 로고
    • Experiments on the use of metallic ligatures, as applied to arteries
    • Levert H.S. Experiments on the use of metallic ligatures, as applied to arteries. Am. J. Med. Sci. 1829, 7:17-23.
    • (1829) Am. J. Med. Sci. , vol.7 , pp. 17-23
    • Levert, H.S.1
  • 70
    • 68249155375 scopus 로고    scopus 로고
    • Fabrication of nano-hydroxyapatite/collagen/osteonectin composites for bone graft applications
    • Liao S., Ngiam M., Chan C.K., Ramakrishna S. Fabrication of nano-hydroxyapatite/collagen/osteonectin composites for bone graft applications. Biomed. Mater. 2009, 4:1-8.
    • (2009) Biomed. Mater. , vol.4 , pp. 1-8
    • Liao, S.1    Ngiam, M.2    Chan, C.K.3    Ramakrishna, S.4
  • 72
    • 44949128995 scopus 로고    scopus 로고
    • Reduced foreign body reaction to implanted biomaterials by surface treatment with oriented osteopontin
    • Liu L., Chen G., Chao T., Ratner B.D., Sage E.H., Jiang S. Reduced foreign body reaction to implanted biomaterials by surface treatment with oriented osteopontin. J. Biomater. Sci. Polym. Ed. 2008, 19:821-835.
    • (2008) J. Biomater. Sci. Polym. Ed. , vol.19 , pp. 821-835
    • Liu, L.1    Chen, G.2    Chao, T.3    Ratner, B.D.4    Sage, E.H.5    Jiang, S.6
  • 73
    • 84891815577 scopus 로고    scopus 로고
    • CCN2 expression by fibroblasts is not required for cutaneous tissue repair
    • Liu S., Thompson K., Leask A. CCN2 expression by fibroblasts is not required for cutaneous tissue repair. Wound Repair Regen. 2014, 22:119-124.
    • (2014) Wound Repair Regen. , vol.22 , pp. 119-124
    • Liu, S.1    Thompson, K.2    Leask, A.3
  • 74
    • 59649112680 scopus 로고    scopus 로고
    • Genetic manipulation of periostin expression in the heart does not affect myocyte content, cell cycle activity, or cardiac repair
    • Lorts A., Schwanekamp J.A., Elrod J.W., Sargent M.A., Molkentin J.D. Genetic manipulation of periostin expression in the heart does not affect myocyte content, cell cycle activity, or cardiac repair. Circ. Res. 2009, 104:e1-e7.
    • (2009) Circ. Res. , vol.104 , pp. e1-e7
    • Lorts, A.1    Schwanekamp, J.A.2    Elrod, J.W.3    Sargent, M.A.4    Molkentin, J.D.5
  • 75
    • 84879886808 scopus 로고    scopus 로고
    • Towards constructing extracellular matrix-mimetic hydrogels: an elastic hydrogel constructed from tandem modular proteins containing tenascin FnIII domains
    • Lv S., Bu T., Kayser J., Bausch A., Li H. Towards constructing extracellular matrix-mimetic hydrogels: an elastic hydrogel constructed from tandem modular proteins containing tenascin FnIII domains. Acta Biomater. 2013, 9:6481-6491.
    • (2013) Acta Biomater. , vol.9 , pp. 6481-6491
    • Lv, S.1    Bu, T.2    Kayser, J.3    Bausch, A.4    Li, H.5
  • 76
    • 80052709760 scopus 로고    scopus 로고
    • Role of matricellular proteins in cardiac tissue remodeling after myocardial infarction
    • Matsui Y., Morimoto J., Uede T. Role of matricellular proteins in cardiac tissue remodeling after myocardial infarction. World J. Biol. Chem. 2010, 1:69-80.
    • (2010) World J. Biol. Chem. , vol.1 , pp. 69-80
    • Matsui, Y.1    Morimoto, J.2    Uede, T.3
  • 77
    • 79953871659 scopus 로고    scopus 로고
    • Affinity peptides protect transforming growth factor beta during encapsulation in poly(ethylene glycol) hydrogels
    • McCall J.D., Lin C.-C., Anseth K.S. Affinity peptides protect transforming growth factor beta during encapsulation in poly(ethylene glycol) hydrogels. Biomacromolecules 2011, 12:1051-1057.
    • (2011) Biomacromolecules , vol.12 , pp. 1051-1057
    • McCall, J.D.1    Lin, C.-C.2    Anseth, K.S.3
  • 78
    • 77953356636 scopus 로고    scopus 로고
    • Smart biomaterials - regulating cell behavior through signaling molecules
    • Mieszawska A.J., Kaplan D.L. Smart biomaterials - regulating cell behavior through signaling molecules. BMC Biol. 2010, 8:59.
    • (2010) BMC Biol. , vol.8 , pp. 59
    • Mieszawska, A.J.1    Kaplan, D.L.2
  • 79
    • 77951954578 scopus 로고    scopus 로고
    • Controlled spatial and conformational display of immobilised bone morphogenetic protein-2 and osteopontin signalling motifs regulates osteoblast adhesion and differentiation in vitro
    • Mitchell E.A., Chaffey B.T., McCaskie A.W., Lakey J.H., Birch M.A. Controlled spatial and conformational display of immobilised bone morphogenetic protein-2 and osteopontin signalling motifs regulates osteoblast adhesion and differentiation in vitro. BMC Biol. 2010, 8:57.
    • (2010) BMC Biol. , vol.8 , pp. 57
    • Mitchell, E.A.1    Chaffey, B.T.2    McCaskie, A.W.3    Lakey, J.H.4    Birch, M.A.5
  • 80
    • 38749106966 scopus 로고    scopus 로고
    • Molecular mechanisms linking wound inflammation and fibrosis: knockdown of osteopontin leads to rapid repair and reduced scarring
    • Mori R., Shaw T.J., Martin P. Molecular mechanisms linking wound inflammation and fibrosis: knockdown of osteopontin leads to rapid repair and reduced scarring. J. Exp. Med. 2008, 205:43-51.
    • (2008) J. Exp. Med. , vol.205 , pp. 43-51
    • Mori, R.1    Shaw, T.J.2    Martin, P.3
  • 81
    • 0035058769 scopus 로고    scopus 로고
    • The de-adhesive activity of matricellular proteins: is intermediate cell adhesion an adaptive state?
    • Murphy-Ullrich J.E. The de-adhesive activity of matricellular proteins: is intermediate cell adhesion an adaptive state?. J. Clin. Invest. 2001, 107:785-790.
    • (2001) J. Clin. Invest. , vol.107 , pp. 785-790
    • Murphy-Ullrich, J.E.1
  • 83
    • 72449193549 scopus 로고    scopus 로고
    • The many facets of the matricellular protein periostin during cardiac development, remodeling, and pathophysiology
    • Norris R.A., Moreno-Rodriguez R., Hoffman S., Markwald R.R. The many facets of the matricellular protein periostin during cardiac development, remodeling, and pathophysiology. J. Cell Commun. Signal. 2009, 3:275-286.
    • (2009) J. Cell Commun. Signal. , vol.3 , pp. 275-286
    • Norris, R.A.1    Moreno-Rodriguez, R.2    Hoffman, S.3    Markwald, R.R.4
  • 86
    • 84856750390 scopus 로고    scopus 로고
    • Matricellular proteins: new molecular targets to prevent heart failure
    • Okamoto H., Imanaka-Yoshida K. Matricellular proteins: new molecular targets to prevent heart failure. Cardiovasc. Ther. 2012, 30:e198-e209.
    • (2012) Cardiovasc. Ther. , vol.30 , pp. e198-e209
    • Okamoto, H.1    Imanaka-Yoshida, K.2
  • 87
    • 72049096929 scopus 로고    scopus 로고
    • Stainless steel ions stimulate increased thrombospondin-1-dependent TGF-beta activation by vascular smooth muscle cells: implications for in-stent restenosis
    • Pallero M.A., Talbert Roden M., Chen Y.-F., Anderson P.G., Lemons J., Brott B.C., Murphy-Ullrich J.E. Stainless steel ions stimulate increased thrombospondin-1-dependent TGF-beta activation by vascular smooth muscle cells: implications for in-stent restenosis. J. Vasc. Res. 2010, 47:309-322.
    • (2010) J. Vasc. Res. , vol.47 , pp. 309-322
    • Pallero, M.A.1    Talbert Roden, M.2    Chen, Y.-F.3    Anderson, P.G.4    Lemons, J.5    Brott, B.C.6    Murphy-Ullrich, J.E.7
  • 88
    • 38749138841 scopus 로고    scopus 로고
    • The biodegradability of electrospun Dextran/PLGA scaffold in a fibroblast/macrophage co-culture
    • Pan H., Jiang H., Chen W. The biodegradability of electrospun Dextran/PLGA scaffold in a fibroblast/macrophage co-culture. Biomaterials 2008, 29:1583-1592.
    • (2008) Biomaterials , vol.29 , pp. 1583-1592
    • Pan, H.1    Jiang, H.2    Chen, W.3
  • 89
    • 78649721546 scopus 로고    scopus 로고
    • SPARC-derived protease substrates to enhance the plasmin sensitivity of molecularly engineered PEG hydrogels
    • Patterson J., Hubbell J.A. SPARC-derived protease substrates to enhance the plasmin sensitivity of molecularly engineered PEG hydrogels. Biomaterials 2011, 32:1301-1310.
    • (2011) Biomaterials , vol.32 , pp. 1301-1310
    • Patterson, J.1    Hubbell, J.A.2
  • 90
    • 0347915577 scopus 로고    scopus 로고
    • Rapid review CCN proteins: multifunctional signalling regulators
    • Perbal B. Rapid review CCN proteins: multifunctional signalling regulators. Lancet 2004, 363:62-64.
    • (2004) Lancet , vol.363 , pp. 62-64
    • Perbal, B.1
  • 92
    • 84860999041 scopus 로고    scopus 로고
    • Intrapericardial delivery of gelfoam enables the targeted delivery of Periostin peptide after myocardial infarction by inducing fibrin clot formation
    • Polizzotti B.D., Arab S., Kühn B. Intrapericardial delivery of gelfoam enables the targeted delivery of Periostin peptide after myocardial infarction by inducing fibrin clot formation. PLoS One 2012, 7:1-11.
    • (2012) PLoS One , vol.7 , pp. 1-11
    • Polizzotti, B.D.1    Arab, S.2    Kühn, B.3
  • 93
    • 0032745323 scopus 로고    scopus 로고
    • Understanding and controlling the bone-implant interface
    • Puleo D.A., Nanci A. Understanding and controlling the bone-implant interface. Biomaterials 1999, 20:2311-2321.
    • (1999) Biomaterials , vol.20 , pp. 2311-2321
    • Puleo, D.A.1    Nanci, A.2
  • 94
    • 0037331246 scopus 로고    scopus 로고
    • Compromised production of extracellular matrix in mice lacking secreted protein, acidic and rich in cysteine (SPARC) leads to a reduced foreign body reaction to implanted biomaterials
    • Puolakkainen P., Bradshaw A.D., Kyriakides T.R., Reed M., Brekken R., Wight T., Bornstein P., Ratner B., Sage E.H. Compromised production of extracellular matrix in mice lacking secreted protein, acidic and rich in cysteine (SPARC) leads to a reduced foreign body reaction to implanted biomaterials. Am. J. Pathol. 2003, 162:627-635.
    • (2003) Am. J. Pathol. , vol.162 , pp. 627-635
    • Puolakkainen, P.1    Bradshaw, A.D.2    Kyriakides, T.R.3    Reed, M.4    Brekken, R.5    Wight, T.6    Bornstein, P.7    Ratner, B.8    Sage, E.H.9
  • 96
    • 0035755650 scopus 로고    scopus 로고
    • Replacing and renewing: synthetic materials, biomimetics, and tissue engineering in implant dentistry
    • Ratner B.D. Replacing and renewing: synthetic materials, biomimetics, and tissue engineering in implant dentistry. J. Dent. Educ. 2001, 65:1340-1347.
    • (2001) J. Dent. Educ. , vol.65 , pp. 1340-1347
    • Ratner, B.D.1
  • 97
    • 0037122775 scopus 로고    scopus 로고
    • Reducing capsular thickness and enhancing angiogenesis around implant drug release systems
    • Ratner B.D. Reducing capsular thickness and enhancing angiogenesis around implant drug release systems. J. Control. Release 2002, 78:211-218.
    • (2002) J. Control. Release , vol.78 , pp. 211-218
    • Ratner, B.D.1
  • 98
    • 4444330267 scopus 로고    scopus 로고
    • Biomaterials: where we have been and where we are going
    • Ratner B.D., Bryant S.J. Biomaterials: where we have been and where we are going. Annu. Rev. Biomed. Eng. 2004, 6:41-75.
    • (2004) Annu. Rev. Biomed. Eng. , vol.6 , pp. 41-75
    • Ratner, B.D.1    Bryant, S.J.2
  • 99
    • 84855825434 scopus 로고    scopus 로고
    • Cell behavior on a CCN1 functionalized elastin-mimetic protein polymer
    • Ravi S., Haller C.A., Sallach R.E., Chaikof E.L. Cell behavior on a CCN1 functionalized elastin-mimetic protein polymer. Biomaterials 2012, 33:2431-2438.
    • (2012) Biomaterials , vol.33 , pp. 2431-2438
    • Ravi, S.1    Haller, C.A.2    Sallach, R.E.3    Chaikof, E.L.4
  • 101
    • 77957318714 scopus 로고    scopus 로고
    • The effects of processing methods upon mechanical and biologic properties of porcine dermal extracellular matrix scaffolds
    • Reing J.E., Brown B.N., Daly K.A., Hsiong S., Huber A., Kullas K.E., Tottey S., Badylak S.F. The effects of processing methods upon mechanical and biologic properties of porcine dermal extracellular matrix scaffolds. Biomaterials 2010, 31:8626-8633.
    • (2010) Biomaterials , vol.31 , pp. 8626-8633
    • Reing, J.E.1    Brown, B.N.2    Daly, K.A.3    Hsiong, S.4    Huber, A.5    Kullas, K.E.6    Tottey, S.7    Badylak, S.F.8
  • 102
    • 0031259844 scopus 로고    scopus 로고
    • The detachment strength and morphology of bone cells contacting materials modified with a peptide sequence found within bone sialoprotein
    • Rezania A., Thomas C.H., Branger A.B., Waters C.M., Healy K.E. The detachment strength and morphology of bone cells contacting materials modified with a peptide sequence found within bone sialoprotein. J. Biomed. Mater. Res. 1997, 37:9-19.
    • (1997) J. Biomed. Mater. Res. , vol.37 , pp. 9-19
    • Rezania, A.1    Thomas, C.H.2    Branger, A.B.3    Waters, C.M.4    Healy, K.E.5
  • 103
    • 34250897750 scopus 로고    scopus 로고
    • Modern biomaterials: a review - bulk properties and implications of surface modifications
    • Roach P., Eglin D., Rohde K., Perry C.C. Modern biomaterials: a review - bulk properties and implications of surface modifications. J. Mater. Sci. Mater. Med. 2007, 18:1263-1277.
    • (2007) J. Mater. Sci. Mater. Med. , vol.18 , pp. 1263-1277
    • Roach, P.1    Eglin, D.2    Rohde, K.3    Perry, C.C.4
  • 104
    • 84881174013 scopus 로고    scopus 로고
    • The matrikine tenascin-C protects multipotential stromal cells/mesenchymal stem cells from death cytokines such as FasL
    • Rodrigues M., Yates C.C., Nuschke A., Griffith L., Wells A. The matrikine tenascin-C protects multipotential stromal cells/mesenchymal stem cells from death cytokines such as FasL. Tissue Eng. Part A 2013, 19:1972-1983.
    • (2013) Tissue Eng. Part A , vol.19 , pp. 1972-1983
    • Rodrigues, M.1    Yates, C.C.2    Nuschke, A.3    Griffith, L.4    Wells, A.5
  • 105
    • 67650451085 scopus 로고    scopus 로고
    • The multifaceted role of periostin in tumorigenesis
    • Ruan K., Bao S., Ouyang G. The multifaceted role of periostin in tumorigenesis. Cell. Mol. Life Sci. 2009, 66:2219-2230.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2219-2230
    • Ruan, K.1    Bao, S.2    Ouyang, G.3
  • 106
    • 84859602944 scopus 로고    scopus 로고
    • Formulation and in vitro characterization of PEGylated chitosan and polyethylene imine polymers with thrombospondin-I gene bearing pDNA
    • Saka O.M., Bozkir A. Formulation and in vitro characterization of PEGylated chitosan and polyethylene imine polymers with thrombospondin-I gene bearing pDNA. J. Biomed. Mater. Res. B Appl. Biomater. 2012, 100:984-992.
    • (2012) J. Biomed. Mater. Res. B Appl. Biomater. , vol.100 , pp. 984-992
    • Saka, O.M.1    Bozkir, A.2
  • 107
    • 38149052983 scopus 로고    scopus 로고
    • Osteonectin-derived peptide increases the modulus of a bone-mimetic nanocomposite
    • Sarvestani A.S., He X., Jabbari E. Osteonectin-derived peptide increases the modulus of a bone-mimetic nanocomposite. Eur. Biophys. J. 2008, 37:229-234.
    • (2008) Eur. Biophys. J. , vol.37 , pp. 229-234
    • Sarvestani, A.S.1    He, X.2    Jabbari, E.3
  • 108
    • 62449175839 scopus 로고    scopus 로고
    • Interactions between extracellular matrix and growth factors in wound healing
    • Schultz G.S., Wysocki A. Interactions between extracellular matrix and growth factors in wound healing. Wound Repair Regen. 2009, 17:153-162.
    • (2009) Wound Repair Regen. , vol.17 , pp. 153-162
    • Schultz, G.S.1    Wysocki, A.2
  • 109
    • 0027305971 scopus 로고
    • Thrombospondin causes activation of latent transforming growth factor-beta secreted by endothelial cells by a novel mechanism
    • Schultz-Cherry S., Murphy-Ullrich J.E. Thrombospondin causes activation of latent transforming growth factor-beta secreted by endothelial cells by a novel mechanism. J. Cell Biol. 1993, 122:923-932.
    • (1993) J. Cell Biol. , vol.122 , pp. 923-932
    • Schultz-Cherry, S.1    Murphy-Ullrich, J.E.2
  • 110
    • 79953037494 scopus 로고    scopus 로고
    • Identifying sarcomere gene mutations in hypertrophic cardiomyopathy: a personal history
    • Seidman C.E., Seidman J.G. Identifying sarcomere gene mutations in hypertrophic cardiomyopathy: a personal history. Circ. Res. 2011, 108:743-750.
    • (2011) Circ. Res. , vol.108 , pp. 743-750
    • Seidman, C.E.1    Seidman, J.G.2
  • 111
    • 0042562089 scopus 로고    scopus 로고
    • Biomimetic materials for tissue engineering
    • Shin H., Jo S., Mikos A.G. Biomimetic materials for tissue engineering. Biomaterials 2003, 24:4353-4364.
    • (2003) Biomaterials , vol.24 , pp. 4353-4364
    • Shin, H.1    Jo, S.2    Mikos, A.G.3
  • 113
    • 79961088512 scopus 로고    scopus 로고
    • Organ engineering based on decellularized matrix scaffolds
    • Song J.J., Ott H.C. Organ engineering based on decellularized matrix scaffolds. Trends Mol. Med. 2011, 17:424-432.
    • (2011) Trends Mol. Med. , vol.17 , pp. 424-432
    • Song, J.J.1    Ott, H.C.2
  • 114
    • 27944466697 scopus 로고    scopus 로고
    • Exploring and engineering the cell surface interface
    • Stevens M.M., George J.H. Exploring and engineering the cell surface interface. Science 2005, 310:1135-1138.
    • (2005) Science , vol.310 , pp. 1135-1138
    • Stevens, M.M.1    George, J.H.2
  • 117
    • 14644445680 scopus 로고    scopus 로고
    • Hevin/SC1, a matricellular glycoprotein and potential tumor-suppressor of the SPARC/BM-40/Osteonectin family
    • Sullivan M.M., Sage E.H. Hevin/SC1, a matricellular glycoprotein and potential tumor-suppressor of the SPARC/BM-40/Osteonectin family. Int. J. Biochem. Cell Biol. 2004, 36:991-996.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 991-996
    • Sullivan, M.M.1    Sage, E.H.2
  • 118
    • 77957357565 scopus 로고    scopus 로고
    • The calreticulin-binding sequence of thrombospondin 1 regulates collagen expression and organization during tissue remodeling
    • Sweetwyne M.T., Pallero M.A., Lu A., Van Duyn Graham L., Murphy-Ullrich J.E. The calreticulin-binding sequence of thrombospondin 1 regulates collagen expression and organization during tissue remodeling. Am. J. Pathol. 2010, 177:1710-1724.
    • (2010) Am. J. Pathol. , vol.177 , pp. 1710-1724
    • Sweetwyne, M.T.1    Pallero, M.A.2    Lu, A.3    Van Duyn Graham, L.4    Murphy-Ullrich, J.E.5
  • 120
    • 38549097166 scopus 로고    scopus 로고
    • Osteopontin: regulation in tumor metastasis
    • Wai P.Y., Kuo P.C. Osteopontin: regulation in tumor metastasis. Cancer Metastasis Rev. 2008, 27:103-118.
    • (2008) Cancer Metastasis Rev. , vol.27 , pp. 103-118
    • Wai, P.Y.1    Kuo, P.C.2
  • 122
    • 33745714841 scopus 로고    scopus 로고
    • A review on macrophage responses to biomaterials
    • Xia Z., Triffitt J.T. A review on macrophage responses to biomaterials. Biomed. Mater. 2006, 1:R1-R9.
    • (2006) Biomed. Mater. , vol.1 , pp. R1-R9
    • Xia, Z.1    Triffitt, J.T.2
  • 123
    • 33750432152 scopus 로고    scopus 로고
    • Role of fibrillar structure of collagenous carrier in bone sialoprotein-mediated matrix mineralization and osteoblast differentiation
    • Xu L., Anderson A.L., Lu Q., Wang J. Role of fibrillar structure of collagenous carrier in bone sialoprotein-mediated matrix mineralization and osteoblast differentiation. Biomaterials 2007, 28:750-761.
    • (2007) Biomaterials , vol.28 , pp. 750-761
    • Xu, L.1    Anderson, A.L.2    Lu, Q.3    Wang, J.4
  • 124
    • 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
  • 125
    • 84880513736 scopus 로고    scopus 로고
    • Derivation of human peripheral blood derived endothelial progenitor cells and the role of osteopontin surface modification and eNOS transfection
    • Yuan Y., Altalhi W.A., Ng J.J., Courtman D.W. Derivation of human peripheral blood derived endothelial progenitor cells and the role of osteopontin surface modification and eNOS transfection. Biomaterials 2013, 34:7292-7301.
    • (2013) Biomaterials , vol.34 , pp. 7292-7301
    • Yuan, Y.1    Altalhi, W.A.2    Ng, J.J.3    Courtman, D.W.4


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