메뉴 건너뛰기




Volumn 5, Issue 6, 2010, Pages 961-970

Mining the extracellular matrix for tissue engineering applications

Author keywords

basement membrane protein; biomaterial; biomimetic scaffold; extracellular matrix derived peptide; tissue reconstruction

Indexed keywords

ARGINYLGLYCYLASPARTIC ACID; ASPARTYLGLYCYLGLUTAMYLALANINE; BIOMATERIAL; GLYCOCONJUGATE; GLYCYLPHENYLALANYLGLUTAMINYLGLYCYLGLUTAMYLARGININE; HEXAPEPTIDE; HYALURONIC ACID; ISOLEUCYLLYSYLVALYLALANYLVALINE; PENTAPEPTIDE; PERLECAN; TETRAPEPTIDE; TYROSYLISOLEUCYLGLYCYLSERYLARGININE; UNCLASSIFIED DRUG;

EID: 78649382350     PISSN: 17460751     EISSN: None     Source Type: Journal    
DOI: 10.2217/rme.10.61     Document Type: Review
Times cited : (51)

References (137)
  • 1
    • 0038236715 scopus 로고    scopus 로고
    • Integrins in regulation of tissue development and function
    • Danen EH, Sonnenberg A: Integrins in regulation of tissue development and function. J. Pathol. 200(4), 471-480 (2003).
    • (2003) J. Pathol. , vol.200 , Issue.4 , pp. 471-480
    • Danen, E.H.1    Sonnenberg, A.2
  • 5
    • 0028956747 scopus 로고
    • Local regulation of extracellular matrix structure
    • Weber KT, Sun Y, Katwa LC: Local regulation of extracellular matrix structure. Herz. 20(2), 81-88 (1995).
    • (1995) Herz. , vol.20 , Issue.2 , pp. 81-88
    • Weber, K.T.1    Sun, Y.2    Katwa, L.C.3
  • 6
    • 0033773107 scopus 로고    scopus 로고
    • Extracellular matrix and cytokines: A functional unit
    • Schonherr E, Hausser HJ: Extracellular matrix and cytokines: a functional unit. Dev. Immunol. 7(2-4), 89-101 (2000).
    • (2000) Dev. Immunol. , vol.7 , Issue.2-4 , pp. 89-101
    • Schonherr, E.1    Hausser, H.J.2
  • 7
    • 30744468824 scopus 로고    scopus 로고
    • Role of extracellular matrix and its regulators in human airway smooth muscle biology
    • Parameswaran K, Willems-Widyastuti A, Alagappan VK et al.: Role of extracellular matrix and its regulators in human airway smooth muscle biology. Cell Biochem. Biophys. 44(1), 139-146 (2006).
    • (2006) Cell Biochem. Biophys. , vol.44 , Issue.1 , pp. 139-146
    • Parameswaran, K.1    Willems-Widyastuti, A.2    Alagappan, V.K.3
  • 8
    • 17444412597 scopus 로고    scopus 로고
    • The role of matrix extracellular proteins and metalloproteinases in head and neck carcinomas: An updated review
    • Pereira AL, Veras SS, Silveira EJ et al.: The role of matrix extracellular proteins and metalloproteinases in head and neck carcinomas: an updated review. Braz. J. Otorhinolaryngol. 71(1), 81-86 (2005).
    • (2005) Braz. J. Otorhinolaryngol. , vol.71 , Issue.1 , pp. 81-86
    • Pereira, A.L.1    Veras, S.S.2    Silveira, E.J.3
  • 9
    • 67249144694 scopus 로고    scopus 로고
    • Basement membranes in skin: Unique matrix structures with diverse functions?
    • Breitkreutz D, Mirancea N, Nischt R: Basement membranes in skin: unique matrix structures with diverse functions? Histochem. Cell Biol. 132(1), 1-10 (2009).
    • (2009) Histochem Cell Biol. , vol.132 , Issue.1 , pp. 1-10
    • Breitkreutz, D.1    Mirancea, N.2    Nischt, R.3
  • 10
    • 0033808066 scopus 로고    scopus 로고
    • Still more complexity in mammalian basement membranes
    • Erickson AC, Couchman JR: Still more complexity in mammalian basement membranes. J. Histochem. Cytochem. 48(10), 1291-1306 (2000).
    • (2000) J. Histochem. Cytochem. , vol.48 , Issue.10 , pp. 1291-1306
    • Erickson, A.C.1    Couchman, J.R.2
  • 11
    • 54049137191 scopus 로고    scopus 로고
    • Breaching the basement membrane: Who, when and how?
    • Rowe RG, Weiss SJ: Breaching the basement membrane: who, when and how? Trends Cell Biol. 18(11), 560-574 (2008).
    • (2008) Trends Cell Biol. , vol.18 , Issue.11 , pp. 560-574
    • Rowe, R.G.1    Weiss, S.J.2
  • 13
    • 13544259736 scopus 로고    scopus 로고
    • Cellular and molecular facets of keratinocyte reepithelization during wound healing
    • Santoro MM, Gaudino G: Cellular and molecular facets of keratinocyte reepithelization during wound healing. Exp. Cell Res. 304(1), 274-286 (2005).
    • (2005) Exp. Cell Res. , vol.304 , Issue.1 , pp. 274-286
    • Santoro, M.M.1    Gaudino, G.2
  • 14
    • 0030087944 scopus 로고    scopus 로고
    • Supramolecular assembly of basement membranes
    • Timpl R, Brown JC: Supramolecular assembly of basement membranes. Bioessays 18(2), 123-132 (1996).
    • (1996) Bioessays , vol.18 , Issue.2 , pp. 123-132
    • Timpl, R.1    Brown, J.C.2
  • 16
    • 34547093441 scopus 로고    scopus 로고
    • Role of laminin terminal globular domains in basement membrane assembly
    • DOI 10.1074/jbc.M702963200
    • McKee KK, Harrison D, Capizzi S, Yurchenco PD: Role of laminin terminal globular domains in basement membrane assembly. J. Biol. Chem. 282(29), 21437-21447 (2007). (Pubitemid 47099937)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.29 , pp. 21437-21447
    • McKee, K.K.1    Harrison, D.2    Capizzi, S.3    Yurchenco, P.D.4
  • 18
    • 77951975118 scopus 로고    scopus 로고
    • Laminin chain assembly is regulated by specifc coiled-coil interactions
    • Macdonald PR, Lustig A, Steinmetz MO, Kammerer RA: Laminin chain assembly is regulated by specifc coiled-coil interactions. J. Struct. Biol. 170(2), 398-405 (2010).
    • (2010) J. Struct. Biol. , vol.170 , Issue.2 , pp. 398-405
    • MacDonald, P.R.1    Lustig, A.2    Steinmetz, M.O.3    Kammerer, R.A.4
  • 19
    • 67649768516 scopus 로고    scopus 로고
    • Scaffold-forming and adhesive contributions of synthetic laminin-binding proteins to basement membrane assembly
    • McKee KK, Capizzi S, Yurchenco PD: Scaffold-forming and adhesive contributions of synthetic laminin-binding proteins to basement membrane assembly. J. Biol. Chem. 284(13), 8984-8994 (2009).
    • (2009) J. Biol. Chem. , vol.284 , Issue.13 , pp. 8984-8994
    • McKee, K.K.1    Capizzi, S.2    Yurchenco, P.D.3
  • 20
    • 72449128021 scopus 로고    scopus 로고
    • Laminins
    • Durbeej M: Laminins. Cell Tissue Res. 339(1), 259-268 (2010).
    • (2010) Cell Tissue Res. , vol.339 , Issue.1 , pp. 259-268
    • Durbeej, M.1
  • 21
    • 36249022091 scopus 로고    scopus 로고
    • Bridging structure with function: Structural, regulatory, and developmental role of laminins
    • Tzu J, Marinkovich MP: Bridging structure with function: structural, regulatory, and developmental role of laminins. Int. J. Biochem. Cell Biol. 40(2), 199-214 (2008).
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , Issue.2 , pp. 199-214
    • Tzu, J.1    Marinkovich, M.P.2
  • 23
    • 17644375191 scopus 로고    scopus 로고
    • Laminin-sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fbroblasts
    • Li S, Liquari P, McKee KK et al.: Laminin-sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fbroblasts. J. Cell Biol. 1(1), 179-189 (2005).
    • (2005) J. Cell Biol. , vol.1 , Issue.1 , pp. 179-189
    • Li, S.1    Liquari, P.2    McKee, K.K.3
  • 24
    • 0035824882 scopus 로고    scopus 로고
    • Short arm region of laminin-5 g2 chain: Structure, mechanism of processing and binding to heparin and proteins
    • Sasaki T, Gohring W, Mann K et al.: Short arm region of laminin-5 g2 chain: structure, mechanism of processing and binding to heparin and proteins. J. Mol. Biol. 314(4), 751-763 (2001).
    • (2001) J. Mol. Biol. , vol.314 , Issue.4 , pp. 751-763
    • Sasaki, T.1    Gohring, W.2    Mann, K.3
  • 28
    • 0026703151 scopus 로고
    • Basement-membrane heparan sulfate proteoglycan binds to laminin by its heparan sulfate chains and to nidogen by sites in the protein core
    • Battaglia C, Mayer U, Aumailley M, Timpl R: Basement-membrane heparan sulfate proteoglycan binds to laminin by its heparan sulfate chains and to nidogen by sites in the protein core. Eur. J. Biochem. 208(2), 359-366 (1992).
    • (1992) Eur. J. Biochem. , vol.208 , Issue.2 , pp. 359-366
    • Battaglia, C.1    Mayer, U.2    Aumailley, M.3    Timpl, R.4
  • 29
    • 23144436642 scopus 로고    scopus 로고
    • Basement membrane proteoglycans: From cellar to ceiling
    • Iozzo RV: Basement membrane proteoglycans: from cellar to ceiling. Nat. Rev. Mol. Cell Biol. 6(8), 646-656 (2005).
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , Issue.8 , pp. 646-656
    • Iozzo, R.V.1
  • 30
    • 1442310569 scopus 로고    scopus 로고
    • Basement membrane assembly, stability and activities observed through a developmental lens
    • Yurchenco PD, Amenta PS, Patton BL: Basement membrane assembly, stability and activities observed through a developmental lens. Matrix Biol. 22(7), 521-538 (2004).
    • (2004) Matrix Biol. , vol.22 , Issue.7 , pp. 521-538
    • Yurchenco, P.D.1    Amenta, P.S.2    Patton, B.L.3
  • 31
    • 21244438355 scopus 로고    scopus 로고
    • Expression and function of laminins in the embryonic and mature vasculature
    • Hallmann R, Horn N, Selg M et al.: Expression and function of laminins in the embryonic and mature vasculature. Physiol. Rev. 85(3), 979-1000 (2005).
    • (2005) Physiol. Rev. , vol.85 , Issue.3 , pp. 979-1000
    • Hallmann, R.1    Horn, N.2    Selg, M.3
  • 32
    • 33644683263 scopus 로고    scopus 로고
    • Endothelial extracellular matrix: Biosynthesis, remodeling, and functions during vascular morphogenesis and neovessel stabilization
    • Davis GE, Senger DR: Endothelial extracellular matrix: biosynthesis, remodeling, and functions during vascular morphogenesis and neovessel stabilization. Circ. Res. 97(11), 1093-1107 (2005).
    • (2005) Circ. Res. , vol.97 , Issue.11 , pp. 1093-1107
    • Davis, G.E.1    Senger, D.R.2
  • 33
    • 0030919488 scopus 로고    scopus 로고
    • The laminin a-chains: Expression, developmental transitions, and chromosomal locations of a1-5, identifcation of heterotrimeric laminins 8-11, and cloning of a novel a3 isoform
    • Miner JH, Patton BL, Lentz SI et al.: The laminin a-chains: expression, developmental transitions, and chromosomal locations of a1-5, identifcation of heterotrimeric laminins 8-11, and cloning of a novel a3 isoform. J. Cell Biol. 137(3), 685-701 (1997).
    • (1997) J. Cell Biol. , vol.137 , Issue.3 , pp. 685-701
    • Miner, J.H.1    Patton, B.L.2    Lentz, S.I.3
  • 34
    • 0036007196 scopus 로고    scopus 로고
    • Deletion of the laminin a4 chain leads to impaired microvessel maturation
    • Thyboll J, Kortesmaa J, Cao R et al.: Deletion of the laminin a4 chain leads to impaired microvessel maturation. Mol. Cell Biol. 22(4), 1194-1202 (2002).
    • (2002) Mol. Cell Biol. , vol.22 , Issue.4 , pp. 1194-1202
    • Thyboll, J.1    Kortesmaa, J.2    Cao, R.3
  • 35
    • 0032517785 scopus 로고    scopus 로고
    • Roles for laminin in embryogenesis: Exencephaly, syndactyly, and placentopathy in mice lacking the laminin a5 chain
    • Miner JH, Cunningham J, Sanes JR: Roles for laminin in embryogenesis: exencephaly, syndactyly, and placentopathy in mice lacking the laminin a5 chain. J. Cell Biol. 143(6), 1713-1723 (1998).
    • (1998) J. Cell Biol. , vol.143 , Issue.6 , pp. 1713-1723
    • Miner, J.H.1    Cunningham, J.2    Sanes, J.R.3
  • 37
    • 0037805549 scopus 로고    scopus 로고
    • Basement membranes: Structure, assembly and role in tumour angiogenesis
    • Kalluri R: Basement membranes: structure, assembly and role in tumour angiogenesis. Nat. Rev. Cancer 3(6), 422-433 (2003).
    • (2003) Nat. Rev. Cancer , vol.3 , Issue.6 , pp. 422-433
    • Kalluri, R.1
  • 38
    • 0037309778 scopus 로고    scopus 로고
    • Distribution of the collagen IV isoforms in human Bruch's membrane
    • DOI 10.1136/bjo.87.2.212
    • Chen L, Miyamura N, Ninomiya Y, Handa JT: Distribution of the collagen IV isoforms in human Bruch's membrane. Br. J. Ophthalmol. 87(2), 212-215 (2003). (Pubitemid 36152750)
    • (2003) British Journal of Ophthalmology , vol.87 , Issue.2 , pp. 212-215
    • Chen, L.1    Miyamura, N.2    Ninomiya, Y.3    Handa, J.T.4
  • 39
    • 1842482987 scopus 로고    scopus 로고
    • Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development
    • Poschl E, Schlotzer-Schrehardt U, Brachvogel B et al.: Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development. Development 131(7), 1619-1628 (2004).
    • (2004) Development , vol.131 , Issue.7 , pp. 1619-1628
    • Poschl, E.1    Schlotzer-Schrehardt, U.2    Brachvogel, B.3
  • 40
    • 0033615959 scopus 로고    scopus 로고
    • Perlecan maintains the integrity of cartilage and some basement membranes
    • Costell M, Gustafsson E, Aszodi A et al.: Perlecan maintains the integrity of cartilage and some basement membranes. J. Cell Biol. 147(5), 1109-1122 (1999).
    • (1999) J. Cell Biol. , vol.147 , Issue.5 , pp. 1109-1122
    • Costell, M.1    Gustafsson, E.2    Aszodi, A.3
  • 41
    • 3142736457 scopus 로고    scopus 로고
    • Endorepellin causes endothelial cell disassembly of actin cytoskeleton and focal adhesions through a2b 1 integrin
    • Bix G, Fu J, Gonzalez EM et al.: Endorepellin causes endothelial cell disassembly of actin cytoskeleton and focal adhesions through a2b 1 integrin. J. Cell Biol. 166(1), 97-109 (2004).
    • (2004) J. Cell Biol. , vol.166 , Issue.1 , pp. 97-109
    • Bix, G.1    Fu, J.2    Gonzalez, E.M.3
  • 42
    • 33745120853 scopus 로고    scopus 로고
    • Antiangiogenic peptides and proteins: From experimental tools to clinical drugs
    • Ruegg C, Hasmim M, Lejeune FJ, Alghisi GC: Antiangiogenic peptides and proteins: from experimental tools to clinical drugs. Biochim. Biophys. Acta 1765(2), 155-177 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1765 , Issue.2 , pp. 155-177
    • Ruegg, C.1    Hasmim, M.2    Lejeune, F.J.3    Alghisi, G.C.4
  • 43
    • 34247330149 scopus 로고    scopus 로고
    • Endorepellin, the C-terminal angiostatic module of perlecan, enhances collagen-platelet responses via the a2b 1-integrin receptor
    • Bix G, Iozzo RA, Woodall B et al.: Endorepellin, the C-terminal angiostatic module of perlecan, enhances collagen-platelet responses via the a2b 1-integrin receptor. Blood 109(9), 3745-3748 (2007).
    • (2007) Blood , vol.109 , Issue.9 , pp. 3745-3748
    • Bix, G.1    Iozzo, R.A.2    Woodall, B.3
  • 44
    • 0037423391 scopus 로고    scopus 로고
    • Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan
    • Mongiat M, Sweeney SM, San Antonio JD, Fu J, Iozzo RV: Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan. J. Biol. Chem. 278(6), 4238-4249 (2003).
    • (2003) J. Biol. Chem. , vol.278 , Issue.6 , pp. 4238-4249
    • Mongiat, M.1    Sweeney, S.M.2    San Antonio, J.D.3    Fu, J.4    Iozzo, R.V.5
  • 45
    • 33751354608 scopus 로고    scopus 로고
    • Endorepellin in vivo: Targeting the tumor vasculature and retarding cancer growth and metabolism
    • Bix G, Castello R, Burrows M et al.: Endorepellin in vivo: targeting the tumor vasculature and retarding cancer growth and metabolism. J. Natl Cancer Inst. 98(22), 1634-1646 (2006).
    • (2006) J. Natl Cancer Inst. , vol.98 , Issue.22 , pp. 1634-1646
    • Bix, G.1    Castello, R.2    Burrows, M.3
  • 46
    • 0029944122 scopus 로고    scopus 로고
    • Angiostatin induces and sustains dormancy of human primary tumors in mice
    • O'Reilly MS, Holmgren L, Chen C, Folkman J: Angiostatin induces and sustains dormancy of human primary tumors in mice. Nat. Med. 2(6), 689-692 (1996).
    • (1996) Nat. Med. , vol.2 , Issue.6 , pp. 689-692
    • O'Reilly, M.S.1    Holmgren, L.2    Chen, C.3    Folkman, J.4
  • 47
    • 0028176183 scopus 로고
    • A1(XVIII), a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution, and homology with type XV collagen
    • Rehn M, Pihlajaniemi T: a1(XVIII), a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution, and homology with type XV collagen. Proc. Natl Acad. Sci. USA 91(10), 4234-4238 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , Issue.10 , pp. 4234-4238
    • Rehn, M.1    Pihlajaniemi, T.2
  • 48
    • 33750494958 scopus 로고    scopus 로고
    • Regulation of corneal angiogenesis in limbal stem cell defciency
    • Ma DH, Chen JK, Zhang F et al.: Regulation of corneal angiogenesis in limbal stem cell defciency Prog. Retin. Eye Res. 25(6), 563-590 (2006).
    • (2006) Prog. Retin. Eye Res. , vol.25 , Issue.6 , pp. 563-590
    • Ma, D.H.1    Chen, J.K.2    Zhang, F.3
  • 49
    • 0026003126 scopus 로고
    • Immunochemical localization of extracellular materials in bone marrow of rats
    • Hamilton R, Campbell FR: Immunochemical localization of extracellular materials in bone marrow of rats. Anat. Rec. 231(2), 218-224 (1991).
    • (1991) Anat. Rec. , vol.231 , Issue.2 , pp. 218-224
    • Hamilton, R.1    Campbell, F.R.2
  • 50
    • 0023811128 scopus 로고
    • Extracellular matrix of the marrow microenvironment
    • Gordon MY: Extracellular matrix of the marrow microenvironment. Br. J. Haematol. 70(1), 1-4 (1988).
    • (1988) Br. J. Haematol. , vol.70 , Issue.1 , pp. 1-4
    • Gordon, M.Y.1
  • 51
    • 70349580508 scopus 로고    scopus 로고
    • Mesenchymal stem cells: Innovative therapeutic tools for rheumatic diseases
    • Djouad F, Bouff C, Ghannam S, Noel D, Jorgensen C: Mesenchymal stem cells: innovative therapeutic tools for rheumatic diseases. Nat. Rev. Rheumatol. 5(7), 392-399 (2009).
    • (2009) Nat. Rev. Rheumatol. , vol.5 , Issue.7 , pp. 392-399
    • Djouad, F.1    Bouff, C.2    Ghannam, S.3    Noel, D.4    Jorgensen, C.5
  • 52
    • 0142026448 scopus 로고    scopus 로고
    • Controlling mesenchymal stem cell differentiation by TGF-b family members
    • Roelen BA, Dijke P: Controlling mesenchymal stem cell differentiation by TGF-b family members. J. Orthop. Sci. 8(5), 740-748 (2003).
    • (2003) J. Orthop. Sci. , vol.8 , Issue.5 , pp. 740-748
    • Roelen, B.A.1    Dijke, P.2
  • 53
    • 42449096890 scopus 로고    scopus 로고
    • Polymeric biomaterials in tissue engineering
    • Kohane DS, Langer R: Polymeric biomaterials in tissue engineering. Pediatr. Res. 63(5), 487-491 (2008).
    • (2008) Pediatr. Res. , vol.63 , Issue.5 , pp. 487-491
    • Kohane, D.S.1    Langer, R.2
  • 54
    • 34748872232 scopus 로고    scopus 로고
    • Hydrogels for tissue engineering and delivery of tissue-inducing substances
    • Baroli B: Hydrogels for tissue engineering and delivery of tissue-inducing substances. J. Pharm. Sci. 96(9), 2197-2223 (2007).
    • (2007) J. Pharm. Sci. , vol.96 , Issue.9 , pp. 2197-2223
    • Baroli, B.1
  • 55
    • 34249935409 scopus 로고    scopus 로고
    • Injectable matrices and scaffolds for drug delivery in tissue engineering
    • Kretlow JD, Klouda L, Mikos AG: Injectable matrices and scaffolds for drug delivery in tissue engineering. Adv. Drug Deliv. Rev. 59(4-5), 263-273 (2007).
    • (2007) Adv. Drug Deliv. Rev. , vol.59 , Issue.4-5 , pp. 263-273
    • Kretlow, J.D.1    Klouda, L.2    Mikos, A.G.3
  • 56
    • 34249931102 scopus 로고    scopus 로고
    • Surface engineered and drug releasing pre-fabricated scaffolds for tissue engineering
    • Chung HJ, Park TG: Surface engineered and drug releasing pre-fabricated scaffolds for tissue engineering. Adv. Drug Deliv. Rev. 59(4-5), 249-262 (2007).
    • (2007) Adv. Drug Deliv. Rev. , vol.59 , Issue.4-5 , pp. 249-262
    • Chung, H.J.1    Park, T.G.2
  • 57
    • 33745042944 scopus 로고    scopus 로고
    • Biodegradable polymeric microspheres and nanospheres for drug delivery in the peritoneum
    • Kohane DS, Tse JY, Yeo Y et al.: Biodegradable polymeric microspheres and nanospheres for drug delivery in the peritoneum. J. Biomed. Mater. Res. A 77(2), 351-361 (2006).
    • (2006) J. Biomed. Mater. Res. A , vol.77 , Issue.2 , pp. 351-361
    • Kohane, D.S.1    Tse, J.Y.2    Yeo, Y.3
  • 58
    • 67650479738 scopus 로고    scopus 로고
    • Evaluation of cross-linking methods for electrospun gelatin on cell growth and viability
    • Epub ahead of print
    • Sisson K, Zhang C, Farach-Carson MC, Chase DB, Rabolt JF: Evaluation of cross-linking methods for electrospun gelatin on cell growth and viability Biomacromolecules (2009) (Epub ahead of print).
    • (2009) Biomacromolecules
    • Sisson, K.1    Zhang, C.2    Farach-Carson, M.C.3    Chase, D.B.4    Rabolt, J.F.5
  • 59
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoslahti E, Pierschbacher MD: New perspectives in cell adhesion: RGD and integrins. Science 238(4826), 491-497 (1987).
    • (1987) Science , vol.238 , Issue.4826 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 60
    • 0021267179 scopus 로고
    • Dualistic nature of adhesive protein function: Fbronectin and its biologically active peptide fragments can autoinhibit fbronectin function
    • Yamada KM, Kennedy DW: Dualistic nature of adhesive protein function: fbronectin and its biologically active peptide fragments can autoinhibit fbronectin function. J. Cell Biol. 99(1 Pt 1), 29-36 (1984).
    • (1984) J. Cell Biol. , vol.99 , Issue.1 PART 1 , pp. 29-36
    • Yamada, K.M.1    Kennedy, D.W.2
  • 61
    • 0022385454 scopus 로고
    • The tetrapeptide analogue of the cell attachment site of fbronectin inhibits platelet aggregation and fbrinogen binding to activated platelets
    • Gartner TK, Bennett JS: The tetrapeptide analogue of the cell attachment site of fbronectin inhibits platelet aggregation and fbrinogen binding to activated platelets. J. Biol. Chem. 260(22), 11891-11894 (1985).
    • (1985) J. Biol. Chem. , vol.260 , Issue.22 , pp. 11891-11894
    • Gartner, T.K.1    Bennett, J.S.2
  • 62
    • 0021972086 scopus 로고
    • Inhibition of fbronectin binding to platelets by proteolytic fragments and synthetic peptides which support fbroblast adhesion
    • Ginsberg M, Pierschbacher MD, Ruoslahti E, Marguerie G, Plow E: Inhibition of fbronectin binding to platelets by proteolytic fragments and synthetic peptides which support fbroblast adhesion. J. Biol. Chem. 260(7), 3931-3936 (1985).
    • (1985) J. Biol. Chem. , vol.260 , Issue.7 , pp. 3931-3936
    • Ginsberg, M.1    Pierschbacher, M.D.2    Ruoslahti, E.3    Marguerie, G.4    Plow, E.5
  • 63
    • 0345518379 scopus 로고
    • The effect of Arg-Gly-Asp-containing peptides on fbrinogen and von Willebrand factor binding to platelets
    • Plow EF, Pierschbacher MD, Ruoslahti E, Marguerie GA, Ginsberg MH: The effect of Arg-Gly-Asp-containing peptides on fbrinogen and von Willebrand factor binding to platelets. Proc. Natl Acad. Sci. USA 82(23), 8057-8061 (1985).
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , Issue.23 , pp. 8057-8061
    • Plow, E.F.1    Pierschbacher, M.D.2    Ruoslahti, E.3    Marguerie, G.A.4    Ginsberg, M.H.5
  • 64
    • 0022000999 scopus 로고
    • Related binding mechanisms for fbrinogen fbronectin von Willebrand factor and thrombospondin on thrombin-stimulated human platelets
    • Plow EF, McEver R P, Coller BS et al.: Related binding mechanisms for fbrinogen, fbronectin, von Willebrand factor, and thrombospondin on thrombin-stimulated human platelets. Blood 66(3), 724-727 (1985).
    • (1985) Blood , vol.66 , Issue.3 , pp. 724-727
    • Plow, E.F.1    McEver, R.P.2    Coller, B.S.3
  • 65
    • 0022200025 scopus 로고
    • Vitronectin-a major cell attachment-promoting protein in fetal bovine serum
    • Hayman EG, Pierschbacher MD, Suzuki S, Ruoslahti E: Vitronectin-a major cell attachment-promoting protein in fetal bovine serum. Exp. Cell Res. 160(2), 245-258 (1985).
    • (1985) Exp. Cell Res. , vol.160 , Issue.2 , pp. 245-258
    • Hayman, E.G.1    Pierschbacher, M.D.2    Suzuki, S.3    Ruoslahti, E.4
  • 66
    • 0022273672 scopus 로고
    • Interaction of fbronectin with its receptor on platelets
    • Gardner JM, Hynes RO: Interaction of fbronectin with its receptor on platelets. Cell 42(2), 439-448 (1985).
    • (1985) Cell , vol.42 , Issue.2 , pp. 439-448
    • Gardner, J.M.1    Hynes, R.O.2
  • 68
    • 0028962092 scopus 로고
    • Polymerase chain reaction cloning with degenerate primers: Homology-based identifcation of adhesion molecules
    • Pytela R, Suzuki S, Breuss J, Erle DJ, Sheppard D: Polymerase chain reaction cloning with degenerate primers: homology-based identifcation of adhesion molecules. Methods Enzymol. 245, 420-451 (1994).
    • (1994) Methods Enzymol. , vol.245 , pp. 420-451
    • Pytela, R.1    Suzuki, S.2    Breuss, J.3    Erle, D.J.4    Sheppard, D.5
  • 69
    • 0001023374 scopus 로고
    • A 125/115-kDa cell surface receptor specifc for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence derived from fbronectin
    • Pytela R, Pierschbacher MD, Ruoslahti E: A 125/115-kDa cell surface receptor specifc for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence derived from fbronectin. Proc. Natl Acad. Sci. USA 82(17), 5766-5770 (1985).
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , Issue.17 , pp. 5766-5770
    • Pytela, R.1    Pierschbacher, M.D.2    Ruoslahti, E.3
  • 70
    • 0022000778 scopus 로고
    • Identifcation and isolation of a 140 kd cell surface glycoprotein with properties expected of a fbronectin receptor
    • Pytela R, Pierschbacher MD, Ruoslahti E: Identifcation and isolation of a 140 kd cell surface glycoprotein with properties expected of a fbronectin receptor. Cell 40(1), 191-198 (1985).
    • (1985) Cell , vol.40 , Issue.1 , pp. 191-198
    • Pytela, R.1    Pierschbacher, M.D.2    Ruoslahti, E.3
  • 71
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti E: RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol. 12, 697-715 (1996).
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 72
    • 0026761286 scopus 로고
    • A spontaneous mutation of integrin aIIb b3 (platelet glycoprotein IIb-IIIa) helps defne a ligand binding site
    • Bajt ML, Ginsberg MH, Frelinger AL 3rd, Berndt MC, Loftus JC: A spontaneous mutation of integrin aIIb b3 (platelet glycoprotein IIb-IIIa) helps defne a ligand binding site. J. Biol. Chem. 267(6), 3789-3794 (1992).
    • (1992) J. Biol. Chem. , vol.267 , Issue.6 , pp. 3789-3794
    • Bajt, M.L.1    Ginsberg, M.H.2    Frelinger III, A.L.3    Berndt, M.C.4    Loftus, J.C.5
  • 73
    • 0027990819 scopus 로고
    • Mutation of a ligand binding domain of b3 integrin. Integral role of oxygenated residues in aIIb b3 (GPIIb-IIIa) receptor function
    • Bajt ML, Loftus JC: Mutation of a ligand binding domain of b3 integrin. Integral role of oxygenated residues in aIIb b3 (GPIIb-IIIa) receptor function. J. Biol. Chem. 2(33), 20913-20919 (1994).
    • (1994) J. Biol. Chem. , vol.2 , Issue.33 , pp. 20913-20919
    • Bajt, M.L.1    Loftus, J.C.2
  • 74
    • 0024230916 scopus 로고
    • The Arg-Gly-Asp binding domain of the vitronectin receptor. Photoaffnity cross-linking implicates amino acid residues 61-203 of the b subunit
    • Smith JW, Cheresh DA: The Arg-Gly-Asp binding domain of the vitronectin receptor. Photoaffnity cross-linking implicates amino acid residues 61-203 of the b subunit. J. Biol. Chem. 263(35), 18726-18731 (1988).
    • (1988) J. Biol. Chem. , vol.263 , Issue.35 , pp. 18726-18731
    • Smith, J.W.1    Cheresh, D.A.2
  • 75
    • 0033847622 scopus 로고    scopus 로고
    • Regulation of tissue injury responses by the exposure of matricryptic sites within extracellular matrix molecules
    • Davis GE, Bayless KJ, Davis MJ, Meininger GA: Regulation of tissue injury responses by the exposure of matricryptic sites within extracellular matrix molecules. Am. J. Pathol. 156(5), 1489-1498 (2000).
    • (2000) Am. J. Pathol. , vol.156 , Issue.5 , pp. 1489-1498
    • Davis, G.E.1    Bayless, K.J.2    Davis, M.J.3    Meininger, G.A.4
  • 76
    • 50249117119 scopus 로고    scopus 로고
    • Binding of soluble fbronectin to integrin a5b1-link to focal adhesion redistribution and contractile shape
    • Huveneers S, Truong H, Fassler R, Sonnenberg A, Danen EH: Binding of soluble fbronectin to integrin a5b1-link to focal adhesion redistribution and contractile shape. J. Cell Sci. 121(Pt 15), 2452-2462 (2008).
    • (2008) J. Cell Sci. , vol.121 , Issue.PART 15 , pp. 2452-2462
    • Huveneers, S.1    Truong, H.2    Fassler, R.3    Sonnenberg, A.4    Danen, E.H.5
  • 77
    • 0027326861 scopus 로고
    • Purifcation and fragmentation of nondenatured bone sialoprotein: Evidence for a cryptic RGD-resistant cell attachment domain
    • Mintz KP, Grzesik WJ, Midura RJ et al.: Purifcation and fragmentation of nondenatured bone sialoprotein: evidence for a cryptic, RGD-resistant cell attachment domain. J. Bone Miner. Res. 8(8), 985-995 (1993).
    • (1993) J. Bone Miner. Res. , vol.8 , Issue.8 , pp. 985-995
    • Mintz, K.P.1    Grzesik, W.J.2    Midura, R.J.3
  • 78
    • 77649274233 scopus 로고    scopus 로고
    • Matricryptic sites control tissue injury responses in the cardiovascular system: Relationships to pattern recognition receptor regulated events
    • Davis GE: Matricryptic sites control tissue injury responses in the cardiovascular system: relationships to pattern recognition receptor regulated events. J. Mol. Cell Cardiol. 48(3), 454-460 (2010).
    • (2010) J. Mol. Cell Cardiol. , vol.48 , Issue.3 , pp. 454-460
    • Davis, G.E.1
  • 79
    • 0024461009 scopus 로고
    • Cell adhesion to fbronectin and tenascin: Quantitative measurements of initial binding and subsequent strengthening response
    • Lotz MM, Burdsal CA, Erickson HP, McClay DR: Cell adhesion to fbronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response. J. Cell Biol. 109(4 Pt 1), 1795-1805 (1989).
    • (1989) J. Cell Biol. , vol.109 , Issue.4 PART 1 , pp. 1795-1805
    • Lotz, M.M.1    Burdsal, C.A.2    Erickson, H.P.3    McClay, D.R.4
  • 80
    • 11144327011 scopus 로고    scopus 로고
    • Osteogenic differentiation of rat bone marrow stromal cells cultured on Arg-Gly-Asp modifed hydrogels without dexamethasone and b-glycerol phosphate
    • Shin H, Temenoff JS, Bowden GC et al.: Osteogenic differentiation of rat bone marrow stromal cells cultured on Arg-Gly-Asp modifed hydrogels without dexamethasone and b-glycerol phosphate. Biomaterials 26(17), 3645-3654 (2005).
    • (2005) Biomaterials , vol.26 , Issue.17 , pp. 3645-3654
    • Shin, H.1    Temenoff, J.S.2    Bowden, G.C.3
  • 81
    • 2442712725 scopus 로고    scopus 로고
    • Modulation of differentiation and mineralization of marrow stromal cells cultured on biomimetic hydrogels modifed with Arg-Gly-Asp containing peptides
    • Shin H, Zygourakis K, Farach-Carson MC, Yaszemski MJ, Mikos AG: Modulation of differentiation and mineralization of marrow stromal cells cultured on biomimetic hydrogels modifed with Arg-Gly-Asp containing peptides. J. Biomed. Mater. Res. A (3), 535-543 (2004).
    • (2004) J. Biomed. Mater. Res. A , vol.3 , pp. 535-543
    • Shin, H.1    Zygourakis, K.2    Farach-Carson, M.C.3    Yaszemski, M.J.4    Mikos, A.G.5
  • 82
    • 0242438787 scopus 로고    scopus 로고
    • Attachment, proliferation, and migration of marrow stromal osteoblasts cultured on biomimetic hydrogels modifed with an osteopontin-derived peptide
    • Shin H, Zygourakis K, Farach-Carson MC, Yaszemski MJ, Mikos AG: Attachment, proliferation, and migration of marrow stromal osteoblasts cultured on biomimetic hydrogels modifed with an osteopontin-derived peptide. Biomaterials 25(5), 895-906 (2004).
    • (2004) Biomaterials , vol.25 , Issue.5 , pp. 895-906
    • Shin, H.1    Zygourakis, K.2    Farach-Carson, M.C.3    Yaszemski, M.J.4    Mikos, A.G.5
  • 83
    • 0023492076 scopus 로고
    • YIGSR, a synthetic laminin pentapeptide, inhibits experimental metastasis formation
    • Iwamoto Y, Robey FA, Graf J et al.: YIGSR, a synthetic laminin pentapeptide, inhibits experimental metastasis formation. Science 238(4830), 1132-1134 (1987).
    • (1987) Science , vol.238 , Issue.4830 , pp. 1132-1134
    • Iwamoto, Y.1    Robey, F.A.2    Graf, J.3
  • 84
    • 0032513044 scopus 로고    scopus 로고
    • Involvement of the YIGSR sequence of laminin in protein tyrosine phosphorylation
    • Bushkin-Harav I, Littauer UZ: Involvement of the YIGSR sequence of laminin in protein tyrosine phosphorylation. FEBS Lett. 424(3), 243-247 (1998).
    • (1998) FEBS Lett. , vol.424 , Issue.3 , pp. 243-247
    • Bushkin-Harav, I.1    Littauer, U.Z.2
  • 85
    • 0023878482 scopus 로고
    • Neural crest migration in 3D extracellular matrix utilizes laminin, fbronectin, or collagen
    • Bilozur ME, Hay ED: Neural crest migration in 3D extracellular matrix utilizes laminin, fbronectin, or collagen. Dev. Biol. 125(1), 19-33 (1988).
    • (1988) Dev. Biol. , vol.125 , Issue.1 , pp. 19-33
    • Bilozur, M.E.1    Hay, E.D.2
  • 86
    • 0002766824 scopus 로고
    • Endothelial cell-selective materials for tissue engineering in the vascular graft via a new receptor
    • Hubbell JA, Massia SP, Desai NP, Drumheller PD: Endothelial cell-selective materials for tissue engineering in the vascular graft via a new receptor. Biotechnology (NY) 9(6), 568-572 (1991).
    • (1991) Biotechnology (NY) , vol.9 , Issue.6 , pp. 568-572
    • Hubbell, J.A.1    Massia, S.P.2    Desai, N.P.3    Drumheller, P.D.4
  • 87
    • 24944468716 scopus 로고    scopus 로고
    • Endothelialization of microporous YIGSR/PEG-modifed polyurethaneurea
    • Jun HW, West JL: Endothelialization of microporous YIGSR/PEG-modifed polyurethaneurea. Tissue Eng. 11(7-8), 1133-1140 (2005).
    • (2005) Tissue Eng. , vol.11 , Issue.7-8 , pp. 1133-1140
    • Jun, H.W.1    West, J.L.2
  • 88
    • 0023518505 scopus 로고
    • A pentapeptide from the laminin B1 chain mediates cell adhesion and binds the 67,000 laminin receptor
    • Graf J, Ogle RC, Robey FA et al.: A pentapeptide from the laminin B1 chain mediates cell adhesion and binds the 67,000 laminin receptor. Biochemistry 26(22), 6896-6900 (1987).
    • (1987) Biochemistry , vol.26 , Issue.22 , pp. 6896-6900
    • Graf, J.1    Ogle, R.C.2    Robey, F.A.3
  • 89
    • 0027279623 scopus 로고
    • Laminin receptors and laminin-binding proteins during tumor invasion and metastasis
    • Castronovo V: Laminin receptors and laminin-binding proteins during tumor invasion and metastasis. Invasion Metastasis 13(1), 1-30 (1993).
    • (1993) Invasion Metastasis , vol.13 , Issue.1 , pp. 1-30
    • Castronovo, V.1
  • 90
    • 0024443667 scopus 로고
    • A synthetic peptide containing the IKVAV sequence from the A chain of laminin mediates cell attachment, migration, and neurite outgrowth
    • Tashiro K, Sephel GC, Weeks B et al.: A synthetic peptide containing the IKVAV sequence from the A chain of laminin mediates cell attachment, migration, and neurite outgrowth. J. Biol. Chem. 264(27), 16174-16182 (1989).
    • (1989) J. Biol. Chem. , vol.264 , Issue.27 , pp. 16174-16182
    • Tashiro, K.1    Sephel, G.C.2    Weeks, B.3
  • 91
    • 0024350025 scopus 로고
    • A laminin-pepsin fragment with cell attachment and neurite outgrowth activity at distinct sites
    • Sephel GC, Tashiro K, Sasaki M et al.: A laminin-pepsin fragment with cell attachment and neurite outgrowth activity at distinct sites. Dev. Biol. 135(1), 172-181 (1989).
    • (1989) Dev. Biol. , vol.135 , Issue.1 , pp. 172-181
    • Sephel, G.C.1    Tashiro, K.2    Sasaki, M.3
  • 92
    • 0024406487 scopus 로고
    • Laminin A chain synthetic peptide which supports neurite outgrowth
    • Sephel GC, Tashiro KI, Sasaki M et al.: Laminin A chain synthetic peptide which supports neurite outgrowth. Biochem. Biophys. Res. Commun. 162(2), 821-829 (1989).
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , Issue.2 , pp. 821-829
    • Sephel, G.C.1    Tashiro, K.I.2    Sasaki, M.3
  • 93
    • 0029030898 scopus 로고
    • Structure-activity study of a laminin a-1 chain active peptide segment Ile-Lys-Val-Ala-Val (IKVAV)
    • Nomizu M, Weeks BS, Weston CA et al.: Structure-activity study of a laminin a-1 chain active peptide segment Ile-Lys-Val-Ala-Val (IKVAV). FEBS Lett. 365(2-3), 227-231 (1995).
    • (1995) FEBS Lett. , vol.365 , Issue.2-3 , pp. 227-231
    • Nomizu, M.1    Weeks, B.S.2    Weston, C.A.3
  • 94
    • 0024434199 scopus 로고
    • Two different laminin domains mediate the differentiation of human endothelial cells into capillary-like structures in vitro
    • Grant DS, Tashiro K, Segui-Real B et al.: Two different laminin domains mediate the differentiation of human endothelial cells into capillary-like structures in vitro. Cell 58(5), 933-943 (1989).
    • (1989) Cell , vol.58 , Issue.5 , pp. 933-943
    • Grant, D.S.1    Tashiro, K.2    Segui-Real, B.3
  • 95
    • 0033517355 scopus 로고    scopus 로고
    • Growth-cone attraction to netrin-1 is converted to repulsion by laminin-1
    • Hopker VH, Shewan D, Tessier-Lavigne M, Poo M, Holt C: Growth-cone attraction to netrin-1 is converted to repulsion by laminin-1. Nature 401(6748), 69-73 (1999).
    • (1999) Nature , vol.401 , Issue.6748 , pp. 69-73
    • Hopker, V.H.1    Shewan, D.2    Tessier-Lavigne, M.3    Poo, M.4    Holt, C.5
  • 96
    • 44849132167 scopus 로고    scopus 로고
    • Laminin terminates the Netrin/DCC mediated attraction of vagal sensory axons
    • Ratcliffe EM, D'Autreaux F, Gershon MD: Laminin terminates the Netrin/DCC mediated attraction of vagal sensory axons. Dev. Neurobiol. 68(7), 960-971 (2008).
    • (2008) Dev. Neurobiol. , vol.68 , Issue.7 , pp. 960-971
    • Ratcliffe, E.M.1    D'Autreaux, F.2    Gershon, M.D.3
  • 97
    • 0042970739 scopus 로고    scopus 로고
    • Engineering integrin-specifc surfaces with a triple-helical collagen-mimetic peptide
    • Reyes CD, Garcia AJ: Engineering integrin-specifc surfaces with a triple-helical collagen-mimetic peptide. J. Biomed. Mater. Res. A 65(4), 511-523 (2003).
    • (2003) J. Biomed. Mater. Res. A , vol.65 , Issue.4 , pp. 511-523
    • Reyes, C.D.1    Garcia, A.J.2
  • 98
    • 2942536146 scopus 로고    scopus 로고
    • A2b1 integrin-specifc collagen-mimetic surfaces supporting osteoblastic differentiation
    • Reyes CD, Garcia AJ: a2b1 integrin-specifc collagen-mimetic surfaces supporting osteoblastic differentiation. J. Biomed. Mater. Res. A (4), 591-600 (2004).
    • (2004) J. Biomed. Mater. Res. A , vol.4 , pp. 591-600
    • Reyes, C.D.1    Garcia, A.J.2
  • 99
    • 74449086731 scopus 로고    scopus 로고
    • Coating of biomaterial scaffolds with the collagen-mimetic peptide GFOGER for bone defect repair
    • Wojtowicz AM, Shekaran A, Oest ME et al.: Coating of biomaterial scaffolds with the collagen-mimetic peptide GFOGER for bone defect repair. Biomaterials 31(9), 2574-2582 (2010).
    • (2010) Biomaterials , vol.31 , Issue.9 , pp. 2574-2582
    • Wojtowicz, A.M.1    Shekaran, A.2    Oest, M.E.3
  • 100
    • 0033919703 scopus 로고    scopus 로고
    • Type i collagen-induced osteoblastic differentiation of bone-marrow cells mediated by collagen-a2b1 integrin interaction
    • Mizuno M, Fujisawa R, Kuboki Y: Type I collagen-induced osteoblastic differentiation of bone-marrow cells mediated by collagen-a2b1 integrin interaction. J. Cell Physiol. 184(2), 207-213 (2000).
    • (2000) J. Cell Physiol. , vol.184 , Issue.2 , pp. 207-213
    • Mizuno, M.1    Fujisawa, R.2    Kuboki, Y.3
  • 101
    • 0033008113 scopus 로고    scopus 로고
    • Collagen integrin receptors regulate early osteoblast differentiation induced by BMP-2
    • Jikko A, Harris SE, Chen D, Mendrick DL, Damsky CH: Collagen integrin receptors regulate early osteoblast differentiation induced by BMP-2. J. Bone Miner. Res. 14(7), 1075-1083 (1999).
    • (1999) J. Bone Miner. Res. , vol.14 , Issue.7 , pp. 1075-1083
    • Jikko, A.1    Harris, S.E.2    Chen, D.3    Mendrick, D.L.4    Damsky, C.H.5
  • 103
    • 0034069043 scopus 로고    scopus 로고
    • Establishment and characterization of a human gastric carcinoma cell line that is highly metastatic to lymph nodes
    • Yamaguchi K, Ura H, Yasoshima T et al.: Establishment and characterization of a human gastric carcinoma cell line that is highly metastatic to lymph nodes. J. Exp. Clin. Cancer Res. 19(1), 113-120 (2000).
    • (2000) J. Exp. Clin. Cancer Res. , vol.19 , Issue.1 , pp. 113-120
    • Yamaguchi, K.1    Ura, H.2    Yasoshima, T.3
  • 104
    • 0035122328 scopus 로고    scopus 로고
    • Osteoblast-related gene expression of bone marrow cells during the osteoblastic differentiation induced by type i collagen
    • Mizuno M, Kuboki Y: Osteoblast-related gene expression of bone marrow cells during the osteoblastic differentiation induced by type I collagen. J. Biochem. 129(1), 133-138 (2001).
    • (2001) J. Biochem. , vol.129 , Issue.1 , pp. 133-138
    • Mizuno, M.1    Kuboki, Y.2
  • 105
    • 0031282464 scopus 로고    scopus 로고
    • A collagen peptide motif activates tyrosine kinase-dependent calcium signalling pathways in human osteoblast-like cells
    • McCann TJ, Mason WT, Meikle MC, McDonald F: A collagen peptide motif activates tyrosine kinase-dependent calcium signalling pathways in human osteoblast-like cells. Matrix Biol. 16(5), 273-283 (1997).
    • (1997) Matrix Biol. , vol.16 , Issue.5 , pp. 273-283
    • McCann, T.J.1    Mason, W.T.2    Meikle, M.C.3    McDonald, F.4
  • 107
    • 0033229852 scopus 로고    scopus 로고
    • Expression of proteoglycan core proteins in human bone marrow stroma
    • Schofeld KP, Gallagher JT, David G: Expression of proteoglycan core proteins in human bone marrow stroma. Biochem. J. 343 (Pt 3), 663-668 (1999).
    • (1999) Biochem. J. , vol.343 , Issue.PART 3 , pp. 663-668
    • Schofeld, K.P.1    Gallagher, J.T.2    David, G.3
  • 108
    • 38949207947 scopus 로고    scopus 로고
    • A novel peptide sequence in perlecan domain IV supports cell adhesion, spreading and FAK activation
    • Farach-Carson MC, Brown AJ, Lynam M, Safran JB, Carson DD: A novel peptide sequence in perlecan domain IV supports cell adhesion, spreading and FAK activation. Matrix Biol. 27(2), 150-160 (2008).
    • (2008) Matrix Biol. , vol.27 , Issue.2 , pp. 150-160
    • Farach-Carson, M.C.1    Brown, A.J.2    Lynam, M.3    Safran, J.B.4    Carson, D.D.5
  • 109
    • 72649088995 scopus 로고    scopus 로고
    • Perlecan domain IV peptide stimulates salivary gland cell assembly in vitro
    • Pradhan S, Zhang C, Jia X et al.: Perlecan domain IV peptide stimulates salivary gland cell assembly in vitro. Tissue Eng. Part A. 15(11), 3309-3320 (2009).
    • (2009) Tissue Eng. Part A. , vol.15 , Issue.11 , pp. 3309-3320
    • Pradhan, S.1    Zhang, C.2    Jia, X.3
  • 110
    • 77953024277 scopus 로고    scopus 로고
    • Biofunctionalization of electrospun PCL-based scaffolds with perlecan domain IV peptide to create a 3-D pharmacokinetic cancer model
    • Hartman O, Zhang C, Adams EL et al.: Biofunctionalization of electrospun PCL-based scaffolds with perlecan domain IV peptide to create a 3-D pharmacokinetic cancer model. Biomaterials 31(21), 5700-5718 (2010).
    • (2010) Biomaterials , vol.31 , Issue.21 , pp. 5700-5718
    • Hartman, O.1    Zhang, C.2    Adams, E.L.3
  • 111
    • 0026446637 scopus 로고
    • CD44: The hyaluronan receptor
    • Underhill C: CD44: the hyaluronan receptor. J. Cell Sci. 103(Pt 2), 293-298 (1992).
    • (1992) J. Cell Sci. , vol.103 , Issue.PART 2 , pp. 293-298
    • Underhill, C.1
  • 112
    • 0027513932 scopus 로고
    • Identifcation of two hyaluronan-binding domains in the hyaluronan receptor RHAMM
    • Yang B, Zhang L, Turley EA: Identifcation of two hyaluronan-binding domains in the hyaluronan receptor RHAMM. J. Biol. Chem. 268(12), 8617-8623 (1993).
    • (1993) J. Biol. Chem. , vol.268 , Issue.12 , pp. 8617-8623
    • Yang, B.1    Zhang, L.2    Turley, E.A.3
  • 113
    • 0027284796 scopus 로고
    • The link proteins
    • Neame PJ, Barry FP: The link proteins. Experientia 49(5), 393-402 (1993).
    • (1993) Experientia , vol.49 , Issue.5 , pp. 393-402
    • Neame, P.J.1    Barry, F.P.2
  • 114
    • 0030788807 scopus 로고    scopus 로고
    • Identifcation of hyaluronan-binding domains of aggrecan
    • Watanabe H, Cheung SC, Itano N, Kimata K, Yamada Y: Identifcation of hyaluronan-binding domains of aggrecan. J. Biol. Chem. 272(44), 28057-28065 (1997).
    • (1997) J. Biol. Chem. , vol.272 , Issue.44 , pp. 28057-28065
    • Watanabe, H.1    Cheung, S.C.2    Itano, N.3    Kimata, K.4    Yamada, Y.5
  • 115
    • 0024397823 scopus 로고
    • Multiple domains of the large fbroblast proteoglycan, versican
    • Zimmermann DR, Ruoslahti E: Multiple domains of the large fbroblast proteoglycan, versican. EMBO J. 8(10), 2975-2981 (1989).
    • (1989) EMBO J. , vol.8 , Issue.10 , pp. 2975-2981
    • Zimmermann, D.R.1    Ruoslahti, E.2
  • 116
    • 0031819039 scopus 로고    scopus 로고
    • Identifcation of IHABP, a 95 kDa intracellular hyaluronate binding protein
    • Hofmann M, Fieber C, Assmann V et al.: Identifcation of IHABP, a 95 kDa intracellular hyaluronate binding protein. J. Cell Sci. 111(Pt 12), 1673-1684 (1998).
    • (1998) J. Cell Sci. , vol.111 , Issue.PART 12 , pp. 1673-1684
    • Hofmann, M.1    Fieber, C.2    Assmann, V.3
  • 117
    • 0032553328 scopus 로고    scopus 로고
    • SPACR, a novel interphotoreceptor matrix glycoprotein in human retina that interacts with hyaluronan
    • Acharya S, Rodriguez IR, Moreira EF et al.: SPACR, a novel interphotoreceptor matrix glycoprotein in human retina that interacts with hyaluronan. J. Biol. Chem. 273(47), 31599-31606 (1998).
    • (1998) J. Biol. Chem. , vol.273 , Issue.47 , pp. 31599-31606
    • Acharya, S.1    Rodriguez, I.R.2    Moreira, E.F.3
  • 118
    • 0029057403 scopus 로고
    • A novel glycosaminoglycan-binding protein is the vertebrate homologue of the cell cycle control protein
    • Grammatikakis N, Grammatikakis A, Yoneda M et al.: A novel glycosaminoglycan-binding protein is the vertebrate homologue of the cell cycle control protein, Cdc37. J. Biol. Chem. 270(27), 16198-16205 (1995).
    • (1995) Cdc37. J. Biol. Chem. , vol.270 , Issue.27 , pp. 16198-16205
    • Grammatikakis, N.1    Grammatikakis, A.2    Yoneda, M.3
  • 119
    • 0030985899 scopus 로고    scopus 로고
    • Multifunctional activities of human fbroblast 34-kDa hyaluronic acid-binding protein
    • Das S, Deb TB, Kumar R, Datta K: Multifunctional activities of human fbroblast 34-kDa hyaluronic acid-binding protein. Gene 190(1), 223-225 (1997).
    • (1997) Gene , vol.190 , Issue.1 , pp. 223-225
    • Das, S.1    Deb, T.B.2    Kumar, R.3    Datta, K.4
  • 120
    • 0034629563 scopus 로고    scopus 로고
    • SPACRCAN, a novel human interphotoreceptor matrix hyaluronan-binding proteoglycan synthesized by photoreceptors and pinealocytes
    • Acharya S, Foletta VC, Lee JW et al.: SPACRCAN, a novel human interphotoreceptor matrix hyaluronan-binding proteoglycan synthesized by photoreceptors and pinealocytes. J. Biol. Chem. 275(10), 45-55 (2000).
    • (2000) J. Biol. Chem. , vol.275 , Issue.10 , pp. 45-55
    • Acharya, S.1    Foletta, V.C.2    Lee, J.W.3
  • 121
    • 20444405700 scopus 로고    scopus 로고
    • Hyaluronan-binding motif identifed by panning arandom peptide display library
    • Amemiya K, Nakatani T, Saito A, Suzuki A, Munakata H: Hyaluronan-binding motif identifed by panning a random peptide display library. Biochim. Biophys. Acta 1724(1-2), 94-99 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1724 , Issue.1-2 , pp. 94-99
    • Amemiya, K.1    Nakatani, T.2    Saito, A.3    Suzuki, A.4    Munakata, H.5
  • 122
    • 17144362145 scopus 로고    scopus 로고
    • Perlecan domain i promotes fbroblast growth factor 2 delivery in collagen i fbril scaffolds
    • Yang WD, Gomes RR Jr, Alicknavitch M, Farach-Carson MC, Carson DD: Perlecan domain I promotes fbroblast growth factor 2 delivery in collagen I fbril scaffolds. Tissue Eng. 11(1-2), 76-89 (2005).
    • (2005) Tissue Eng. , vol.11 , Issue.1-2 , pp. 76-89
    • Yang, W.D.1    Gomes Jr., R.R.2    Alicknavitch, M.3    Farach-Carson, M.C.4    Carson, D.D.5
  • 123
    • 1842527113 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans: Coordinators of multiple signaling pathways during chondrogenesis
    • Kirn-Safran CB, Gomes RR, Brown AJ, Carson DD: Heparan sulfate proteoglycans: coordinators of multiple signaling pathways during chondrogenesis. Birth Defects Res. C Embryo Today 72(1), 69-88 (2004).
    • (2004) Birth Defects Res. C Embryo Today , vol.72 , Issue.1 , pp. 69-88
    • Kirn-Safran, C.B.1    Gomes, R.R.2    Brown, A.J.3    Carson, D.D.4
  • 124
    • 0037177869 scopus 로고    scopus 로고
    • Not all perlecans are created equal: Interactions with fbroblast growth factor (FGF) 2 and FGF receptors
    • Knox S, Merry C, Stringer S, Melrose J, Whitelock J: Not all perlecans are created equal: interactions with fbroblast growth factor (FGF) 2 and FGF receptors. J. Biol. Chem. 277(17), 14657-14665 (2002).
    • (2002) J. Biol. Chem. , vol.277 , Issue.17 , pp. 14657-14665
    • Knox, S.1    Merry, C.2    Stringer, S.3    Melrose, J.4    Whitelock, J.5
  • 125
    • 0344393418 scopus 로고    scopus 로고
    • Perlecan and tumor angiogenesis
    • Jiang X, Couchman JR: Perlecan and tumor angiogenesis. J. Histochem. Cytochem. 51(11), 1393-1410 (2003).
    • (2003) J. Histochem. Cytochem. , vol.51 , Issue.11 , pp. 1393-1410
    • Jiang, X.1    Couchman, J.R.2
  • 126
    • 0029985256 scopus 로고    scopus 로고
    • Human bone morphogenetic protein 2 contains a heparin-binding site which modifes its biological activity
    • Ruppert R, Hoffmann E, Sebald W: Human bone morphogenetic protein 2 contains a heparin-binding site which modifes its biological activity. Eur. J. Biochem. 237(1), 295-302 (1996).
    • (1996) Eur. J. Biochem. , vol.237 , Issue.1 , pp. 295-302
    • Ruppert, R.1    Hoffmann, E.2    Sebald, W.3
  • 127
    • 1042289596 scopus 로고    scopus 로고
    • Perlecan functions in chondrogenesis: Insights from in vitro and in vivo models
    • Gomes RR Jr, Farach-Carson MC, Carson DD: Perlecan functions in chondrogenesis: insights from in vitro and in vivo models. Cells Tissues Organs 176(1-3), 79-86 (2004).
    • (2004) Cells Tissues Organs , vol.176 , Issue.1-3 , pp. 79-86
    • Gomes Jr., R.R.1    Farach-Carson, M.C.2    Carson, D.D.3
  • 128
    • 0038129555 scopus 로고    scopus 로고
    • Role of collagen type II and perlecan in skeletal development
    • Gustafsson E, Aszodi A, Ortega N et al.: Role of collagen type II and perlecan in skeletal development. Ann. NY Acad. Sci. 995, 140-150 (2003).
    • (2003) Ann. NY Acad. Sci. , vol.995 , pp. 140-150
    • Gustafsson, E.1    Aszodi, A.2    Ortega, N.3
  • 130
    • 33746691230 scopus 로고    scopus 로고
    • Chondrogenic differentiation on perlecan domain I, collagen II, and bone morphogenetic protein-2-based matrices
    • Yang W, Gomes RR, Brown AJ et al.: Chondrogenic differentiation on perlecan domain I, collagen II, and bone morphogenetic protein-2-based matrices. Tissue Eng. 12(7), 2009-2024 (2006).
    • (2006) Tissue Eng. , vol.12 , Issue.7 , pp. 2009-2024
    • Yang, W.1    Gomes, R.R.2    Brown, A.J.3
  • 131
    • 0242694892 scopus 로고    scopus 로고
    • Preparation of lactose-silk fbroin conjugates and their application as a scaffold for hepatocyte attachment
    • Gotoh Y, Niimi S, Hayakawa T, Miyashita T: Preparation of lactose-silk fbroin conjugates and their application as a scaffold for hepatocyte attachment. Biomaterials 25(6), 1131-1140 (2004).
    • (2004) Biomaterials , vol.25 , Issue.6 , pp. 1131-1140
    • Gotoh, Y.1    Niimi, S.2    Hayakawa, T.3    Miyashita, T.4
  • 132
    • 0036582709 scopus 로고    scopus 로고
    • Cell migration through defned, synthetic ECM analogs
    • Gobin AS, West JL: Cell migration through defned, synthetic ECM analogs. FASEB J. 16(7), 751-753 (2002).
    • (2002) FASEB J. , vol.16 , Issue.7 , pp. 751-753
    • Gobin, A.S.1    West, J.L.2
  • 133
    • 19644367664 scopus 로고    scopus 로고
    • Synthetic biomaterials as instructive extracellular microenvironments for morphogenesis in tissue engineering
    • Lutolf MP, Hubbell JA: Synthetic biomaterials as instructive extracellular microenvironments for morphogenesis in tissue engineering. Nat. Biotechnol. 23(1), 47-55 (2005).
    • (2005) Nat. Biotechnol. , vol.23 , Issue.1 , pp. 47-55
    • Lutolf, M.P.1    Hubbell, J.A.2
  • 134
    • 0037965624 scopus 로고    scopus 로고
    • Synthetic matrix metalloproteinase-sensitive hydrogels for the conduction of tissue regeneration: Engineering cell-invasion characteristics
    • Lutolf MP, Lauer-Fields JL, Schmoekel HG et al.: Synthetic matrix metalloproteinase-sensitive hydrogels for the conduction of tissue regeneration: engineering cell-invasion characteristics. Proc. Natl Acad. Sci. USA 100(9), 5413-5418 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , Issue.9 , pp. 5413-5418
    • Lutolf, M.P.1    Lauer-Fields, J.L.2    Schmoekel, H.G.3
  • 135
    • 33846678968 scopus 로고    scopus 로고
    • Polymers for pro-and anti-angiogenic therapy
    • Fischbach C, Mooney DJ: Polymers for pro-and anti-angiogenic therapy. Biomaterials 28(12), 20-76 (2007).
    • (2007) Biomaterials , vol.28 , Issue.12 , pp. 20-76
    • Fischbach, C.1    Mooney, D.J.2
  • 136
    • 33947150969 scopus 로고    scopus 로고
    • Nanostructured materials for applications in drug delivery and tissue engineering
    • Goldberg M, Langer R, Jia X: Nanostructured materials for applications in drug delivery and tissue engineering. J. Biomater. Sci. Polym. Ed. 18(3), 241-268 (2007).
    • (2007) J. Biomater. Sci. Polym. Ed. , vol.18 , Issue.3 , pp. 241-268
    • Goldberg, M.1    Langer, R.2    Jia, X.3
  • 137
    • 33748922791 scopus 로고    scopus 로고
    • Cell adhesion molecules for targeted drug delivery
    • Dunehoo AL, Anderson M, Majumdar S et al.: Cell adhesion molecules for targeted drug delivery J. Pharm. Sci. 95(9), 1856-1872 (2006).
    • (2006) J. Pharm. Sci. , vol.95 , Issue.9 , pp. 1856-1872
    • Dunehoo, A.L.1    Anderson, M.2    Majumdar, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.