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Volumn 124, Issue 2, 1988, Pages 201-206

Potential Roles of Fibronectin in Cutaneous Wound Repair

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; GROWTH FACTOR; OPSONIN;

EID: 0023851909     PISSN: 0003987X     EISSN: 15383652     Source Type: Journal    
DOI: 10.1001/archderm.1988.01670020019010     Document Type: Article
Times cited : (89)

References (91)
  • 1
    • 0023854271 scopus 로고
    • Tissue debris at the injury site is coated by plasma fibronectin and subsequently removed by tissue macrophages
    • Martin DE, Reese MC, Maher JE, et al: Tissue debris at the injury site is coated by plasma fibronectin and subsequently removed by tissue macrophages. Arch Dermatol 1988;124:226–229.
    • (1988) Arch Dermatol , vol.124 , pp. 226-229
    • Martin, D.E.1    Reese, M.C.2    Maher, J.E.3
  • 2
    • 0023835502 scopus 로고
    • Fibronectin enhances healing of excised wounds in rats
    • Cheng CY, Martin DE, Leggett CG, et al: Fibronectin enhances healing of excised wounds in rats. Arch Dermatol 1988;124:221–225.
    • (1988) Arch Dermatol , vol.124 , pp. 221-225
    • Cheng, C.Y.1    Martin, D.E.2    Leggett, C.G.3
  • 3
    • 0022168434 scopus 로고
    • Molecular biology of fibronectin
    • Hynes R: Molecular biology of fibronectin. Annu Rev Cell Biol 1985;1:67–90.
    • (1985) Annu Rev Cell Biol , vol.1 , pp. 67-90
    • Hynes, R.1
  • 4
    • 0021099233 scopus 로고
    • Domain structure of the carboxylterminal half of human plasma fibronectin
    • Hayashi M, Yamada KM: Domain structure of the carboxylterminal half of human plasma fibronectin. J Biol Chem 1983; 258:3332–3340.
    • (1983) J Biol Chem , vol.258 , pp. 3332-3340
    • Hayashi, M.1    Yamada, K.M.2
  • 5
    • 0020553956 scopus 로고
    • Domain structure of plasma fibronectin
    • Sekiguchi K, Hakomori SI: Domain structure of plasma fibronectin. J Biol Chem 1983;258:3967–3973.
    • (1983) J Biol Chem , vol.258 , pp. 3967-3973
    • Sekiguchi, K.1    Hakomori, S.I.2
  • 6
    • 0023058313 scopus 로고
    • Arg-Gly-Asp: A versatile cell recognition signal
    • Ruoslahti E, Pierschbacher MD: Arg-Gly-Asp: A versatile cell recognition signal. Cell 1986;44:517–518.
    • (1986) Cell , vol.44 , pp. 517-518
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 7
    • 0022820769 scopus 로고
    • Mapping the collagen-binding site of human fibronectin by expression in Escherichia coli
    • Owens JO, Baralle FE: Mapping the collagen-binding site of human fibronectin by expression in Escherichia coli. EMBO J 1986;5:2825–2830.
    • (1986) EMBO J , vol.5 , pp. 2825-2830
    • Owens, J.O.1    Baralle, F.E.2
  • 8
    • 0023666065 scopus 로고    scopus 로고
    • Integrins: A family of cell receptors
    • Hynes R: Integrins: A family of cell receptors. Cell 197;48:549–554.
    • Cell 197 , vol.48 , pp. 549-554
    • Hynes, R.1
  • 9
    • 0023236022 scopus 로고
    • Immunochemical and aminoterminal sequence comparison of two cytoadhesins indicates they contain similar or identical β-subunits and distinct α-subunits
    • Ginsberg MH, Loftus J, Ryckwaert J, et al: Immunochemical and aminoterminal sequence comparison of two cytoadhesins indicates they contain similar or identical β-subunits and distinct α-subunits. J Biol Chem 1987;262:5437–5440.
    • (1987) J Biol Chem , vol.262 , pp. 5437-5440
    • Ginsberg, M.H.1    Loftus, J.2    Ryckwaert, J.3
  • 10
    • 0019964755 scopus 로고
    • Fibronectin fragment(s) are chemotactic for human peripheral blood monocytes
    • Norris DA, Clark RAF, Swigart LM, et al: Fibronectin fragment(s) are chemotactic for human peripheral blood monocytes. J Immunol 1982;129:1612–1618.
    • (1982) J Immunol , vol.129 , pp. 1612-1618
    • Norris, D.A.1    Clark, R.A.F.2    Swigart, L.M.3
  • 11
    • 84943446382 scopus 로고
    • Cryptic chemotactic activity for human monocytes resides in the cell-binding domain of fibronectin
    • Clark RAF, Wikner NE, Norris DA, et al: Cryptic chemotactic activity for human monocytes resides in the cell-binding domain of fibronectin. J Cell Biol 1985;101:217a.
    • (1985) J Cell Biol , vol.101 , pp. 217a
    • Clark, R.A.F.1    Wikner, N.E.2    Norris, D.A.3
  • 12
    • 85012405294 scopus 로고
    • Collagen and collagen peptideinduced chemotaxis of human blood monocytes
    • Postlethwaite AE, Kang AH: Collagen and collagen peptideinduced chemotaxis of human blood monocytes. J Exp Med 1976;143:1299–1307.
    • (1976) J Exp Med , vol.143 , pp. 1299-1307
    • Postlethwaite, A.E.1    Kang, A.H.2
  • 13
    • 0018893350 scopus 로고
    • Chemotactic activity of elastin-derived peptides
    • Senoir RM, Griffin GL, Mecham RP: Chemotactic activity of elastin-derived peptides. J Clin Invest 1980;66:859–862.
    • (1980) J Clin Invest , vol.66 , pp. 859-862
    • Senoir, R.M.1    Griffin, G.L.2    Mecham, R.P.3
  • 14
    • 0017826139 scopus 로고
    • Effect of LETS glycoprotein on cell motility
    • Ali U, Hynes RO: Effect of LETS glycoprotein on cell motility. Cell 1978;14:439–446.
    • (1978) Cell , vol.14 , pp. 439-446
    • Ali, U.1    Hynes, R.O.2
  • 15
    • 0019423313 scopus 로고
    • Induction of fibroblast chemotaxis by fibronectin: Localization of the chemotactic region to a 140 000 molecular weight non-gelatin-binding fragment
    • Postlethwaite AE, Keski-Oja J, Balian G, et al: Induction of fibroblast chemotaxis by fibronectin: Localization of the chemotactic region to a 140 000 molecular weight non-gelatin-binding fragment. J Exp Med 1981;15:494–499.
    • (1981) J Exp Med , vol.15 , pp. 494-499
    • Postlethwaite, A.E.1    Keski-Oja, J.2    Balian, G.3
  • 16
    • 0019507134 scopus 로고
    • The cell binding fragment of fibronectin is chemotactic for fibroblasts
    • Seppa HEJ, Yamada KM, Seppa ST, et al: The cell binding fragment of fibronectin is chemotactic for fibroblasts. Cell Biol Int Rep 1981;5:813–819.
    • (1981) Cell Biol Int Rep , vol.5 , pp. 813-819
    • Seppa, H.E.J.1    Yamada, K.M.2    Seppa, S.T.3
  • 17
    • 0019993889 scopus 로고
    • Chemotaxis of aortic endothelial cells in response to fibronectin
    • Bowersox JC, Sorgente N: Chemotaxis of aortic endothelial cells in response to fibronectin. Cancer Res 1982;42:2547–2551.
    • (1982) Cancer Res , vol.42 , pp. 2547-2551
    • Bowersox, J.C.1    Sorgente, N.2
  • 18
    • 0014940727 scopus 로고
    • The cold-insoluble globulin of human plasma: I. Purification, primary characterization, and relationship to fibrinogen and other cold-insoluble fraction components
    • Mosesson MW, Umfleet RA: The cold-insoluble globulin of human plasma: I. Purification, primary characterization, and relationship to fibrinogen and other cold-insoluble fraction components. J Biol Chem 1970;245:5728–5736.
    • (1970) J Biol Chem , vol.245 , pp. 5728-5736
    • Mosesson, M.W.1    Umfleet, R.A.2
  • 19
    • 0018601597 scopus 로고
    • The detection, immunofluorescent localization, and thrombin induced release of human platelet-associated fibronectin antigen
    • Ginsberg MH, Painter RG, Birdwell C, et al: The detection, immunofluorescent localization, and thrombin induced release of human platelet-associated fibronectin antigen. J Supramol Struct 1979;11:167–173.
    • (1979) J Supramol Struct , vol.11 , pp. 167-173
    • Ginsberg, M.H.1    Painter, R.G.2    Birdwell, C.3
  • 20
    • 0017045285 scopus 로고
    • Comparative disappearance and localization of isotopically labelled opsonic protein and soluble albumin following surgical trauma
    • Kaplan JE, Molnar J, Saba TM, et al: Comparative disappearance and localization of isotopically labelled opsonic protein and soluble albumin following surgical trauma. J Reticuloendothel Soc 1976;20:375–384.
    • (1976) J Reticuloendothel Soc , vol.20 , pp. 375-384
    • Kaplan, J.E.1    Molnar, J.2    Saba, T.M.3
  • 21
    • 0019462552 scopus 로고
    • Distribution of fibronectin during wound healing in vivo
    • Grinnell F, Billingham RE, Burgess L: Distribution of fibronectin during wound healing in vivo. J Invest Dermatol 1981;76:181–189.
    • (1981) J Invest Dermatol , vol.76 , pp. 181-189
    • Grinnell, F.1    Billingham, R.E.2    Burgess, L.3
  • 22
    • 0019273980 scopus 로고
    • Cold-insoluble globulin levels in operative trauma: Serum depletion, wound sequestration, and biological activity: An experimental and clinical study
    • Robbins AB, Doran JE, Reese AC, et al: Cold-insoluble globulin levels in operative trauma: Serum depletion, wound sequestration, and biological activity: An experimental and clinical study. Ann Surg 1980;46:663–672.
    • (1980) Ann Surg , vol.46 , pp. 663-672
    • Robbins, A.B.1    Doran, J.E.2    Reese, A.C.3
  • 23
    • 0019464254 scopus 로고
    • Fibronectin in delayedtype hypersensitivity skin reactions: Associations with vessel permeability and endothelial cell activation
    • Clark RAF, Dvorak HF, Colvin RB: Fibronectin in delayedtype hypersensitivity skin reactions: Associations with vessel permeability and endothelial cell activation. J Immunol 1981; 126:787–793.
    • (1981) J Immunol , vol.126 , pp. 787-793
    • Clark, R.A.F.1    Dvorak, H.F.2    Colvin, R.B.3
  • 24
    • 0021147341 scopus 로고
    • Fibronectin deposition in delayed-type hypersensitivity reactions of normals and a patient with afibrinogenemia
    • Clark RAF, Horsburgh RA, Hoffman A, et al: Fibronectin deposition in delayed-type hypersensitivity reactions of normals and a patient with afibrinogenemia. J Clin Invest 1984;74:1011–1016.
    • (1984) J Clin Invest , vol.74 , pp. 1011-1016
    • Clark, R.A.F.1    Horsburgh, R.A.2    Hoffman, A.3
  • 25
    • 0343878382 scopus 로고
    • Partial primary structure of bovine plasma fibronectin: Three types of internal homology
    • Petersen TE, Thøgersen HC, Skorsjengaard K, et al: Partial primary structure of bovine plasma fibronectin: Three types of internal homology. Proc Natl Acad Sci USA 1983;80:137–141.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 137-141
    • Petersen, T.E.1    Thøgersen, H.C.2    Skorsjengaard, K.3
  • 26
    • 0038493745 scopus 로고
    • Transformationenhancing activity of gelatin-binding fragments of fibronectin
    • DePetro G, Barlati S, Vartio T, et al: Transformationenhancing activity of gelatin-binding fragments of fibronectin. Proc Natl Acad Sci USA 1981;78:4965–4969.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 4965-4969
    • DePetro, G.1    Barlati, S.2    Vartio, T.3
  • 27
    • 0019200629 scopus 로고
    • Degradation of fibronectin by human leukocyte elastase: Release of biologically active fragments
    • McDonald JA, Kelley DG: Degradation of fibronectin by human leukocyte elastase: Release of biologically active fragments. J Biol Chem 1980;255:8848–8858.
    • (1980) J Biol Chem , vol.255 , pp. 8848-8858
    • McDonald, J.A.1    Kelley, D.G.2
  • 28
    • 0021323319 scopus 로고
    • Effect of fibronectin fragments on macrophage phagocytosis of gelatinized particles
    • Rourke FJ, Blumenstock FA, Kaplan JE: Effect of fibronectin fragments on macrophage phagocytosis of gelatinized particles. J Immunol 1984;132:1931–1936.
    • (1984) J Immunol , vol.132 , pp. 1931-1936
    • Rourke, F.J.1    Blumenstock, F.A.2    Kaplan, J.E.3
  • 29
    • 0019207585 scopus 로고
    • Fibronectinmediated uptake of gelatin-coated latex particles by peritoneal macrophages
    • Gudewicz PW, Molnar J, Lai MZ, et al: Fibronectinmediated uptake of gelatin-coated latex particles by peritoneal macrophages. J Cell Biol 1980;87:427–433.
    • (1980) J Cell Biol , vol.87 , pp. 427-433
    • Gudewicz, P.W.1    Molnar, J.2    Lai, M.Z.3
  • 30
    • 0019724810 scopus 로고
    • Phagocytosis of gelatin-latex particles by a murine macrophage line is dependent on fibronectin and heparin
    • Van de Water L, Schoeder S, Crenshaw EB, et al: Phagocytosis of gelatin-latex particles by a murine macrophage line is dependent on fibronectin and heparin. J Cell Biol 1981;90:32–39.
    • (1981) J Cell Biol , vol.90 , pp. 32-39
    • Van de Water, L.1    Schoeder, S.2    Crenshaw, E.B.3
  • 31
    • 0019523050 scopus 로고
    • Cold insoluble globin and heparin interactions in phagocytosis by macrophage monolayers: Lack of heparin requirement
    • Doran JE, Mansberger AR, Edmondson HT, et al: Cold insoluble globin and heparin interactions in phagocytosis by macrophage monolayers: Lack of heparin requirement. J Reticuloendothel Soc 1981;29:275–283.
    • (1981) J Reticuloendothel Soc , vol.29 , pp. 275-283
    • Doran, J.E.1    Mansberger, A.R.2    Edmondson, H.T.3
  • 32
    • 0019729248 scopus 로고
    • Fibroblast adhesion on collagen substrata in the presence and absence of plasma fibronectin
    • Grinnell F, Bennett MH: Fibroblast adhesion on collagen substrata in the presence and absence of plasma fibronectin. J Cell Sci 1981;48:19–34.
    • (1981) J Cell Sci , vol.48 , pp. 19-34
    • Grinnell, F.1    Bennett, M.H.2
  • 33
    • 0021817509 scopus 로고
    • Fibronectin-mediated keratinocyte migration and initiation of fibronectin receptor function in vitro
    • Takashima A, Grinnell F: Fibronectin-mediated keratinocyte migration and initiation of fibronectin receptor function in vitro. J Invest Dermatol 1985;85:304–308.
    • (1985) J Invest Dermatol , vol.85 , pp. 304-308
    • Takashima, A.1    Grinnell, F.2
  • 34
    • 0022451954 scopus 로고
    • Activation of rabbit keratinocyte fibronectin receptor function in vivo during wound healing
    • Takashima A, Billingham RE, Grinnell F: Activation of rabbit keratinocyte fibronectin receptor function in vivo during wound healing. J Invest Dermatol 1986;86:585–590.
    • (1986) J Invest Dermatol , vol.86 , pp. 585-590
    • Takashima, A.1    Billingham, R.E.2    Grinnell, F.3
  • 35
    • 0019417453 scopus 로고
    • Fibronectin binding to protein A-containing staphylococci
    • Doran JE, Raynor RH: Fibronectin binding to protein A-containing staphylococci. Infect Immun 1981;33:683–689.
    • (1981) Infect Immun , vol.33 , pp. 683-689
    • Doran, J.E.1    Raynor, R.H.2
  • 36
    • 0019410673 scopus 로고
    • Human fibronectin binding to staphylococcal surface protein and its relative inefficiency in promoting phagocytosis by human polymorphonuclear leukocytes, monocytes and alveolar macrophages
    • Verbrugh HA, Peterson PK, Smith DF, et al: Human fibronectin binding to staphylococcal surface protein and its relative inefficiency in promoting phagocytosis by human polymorphonuclear leukocytes, monocytes and alveolar macrophages. Infect Immun 1981;33:811–819.
    • (1981) Infect Immun , vol.33 , pp. 811-819
    • Verbrugh, H.A.1    Peterson, P.K.2    Smith, D.F.3
  • 37
    • 0018861495 scopus 로고
    • Phagocytosis by human alveolar macrophages and neutrophils: Qualitative differences in the opsonic requirements for uptake of Staphylococcus aureus and Streptococcus pneumoniae in vitro
    • Hof DG, Repine JE, Peterson PK, et al: Phagocytosis by human alveolar macrophages and neutrophils: Qualitative differences in the opsonic requirements for uptake of Staphylococcus aureus and Streptococcus pneumoniae in vitro. Am Rev Respir Dis 1980;121:65–71.
    • (1980) Am Rev Respir Dis , vol.121 , pp. 65-71
    • Hof, D.G.1    Repine, J.E.2    Peterson, P.K.3
  • 38
    • 0018840819 scopus 로고
    • Reticuloendothelial clearance of blood-borne particulates
    • Niehaus GD, Schumacker PR, Saba TM: Reticuloendothelial clearance of blood-borne particulates. Ann Surg 1980;191:479–487.
    • (1980) Ann Surg , vol.191 , pp. 479-487
    • Niehaus, G.D.1    Schumacker, P.R.2    Saba, T.M.3
  • 39
    • 0020618104 scopus 로고
    • Treponema pallidum receptor binding protein interacts with fibronectin
    • Peterson KM, Baseman JB, Alderete JF: Treponema pallidum receptor binding protein interacts with fibronectin. J Exp Med 1983;157:1958–1970.
    • (1983) J Exp Med , vol.157 , pp. 1958-1970
    • Peterson, K.M.1    Baseman, J.B.2    Alderete, J.F.3
  • 40
    • 0020628737 scopus 로고
    • Interaction of viral envelope glycoproteins with fibronectin
    • Julkunen I, Hautanen A, Keski-Oja J: Interaction of viral envelope glycoproteins with fibronectin. Infect Immun 1983; 40:876–881.
    • (1983) Infect Immun , vol.40 , pp. 876-881
    • Julkunen, I.1    Hautanen, A.2    Keski-Oja, J.3
  • 41
    • 0020614844 scopus 로고
    • Fibronectin binds to some bacteria but does not promote their uptake by phagocytic cells
    • Van de Water L, Destree AT, Hynes RO: Fibronectin binds to some bacteria but does not promote their uptake by phagocytic cells. Science 1983;220:201–204.
    • (1983) Science , vol.220 , pp. 201-204
    • Van de Water, L.1    Destree, A.T.2    Hynes, R.O.3
  • 42
    • 0022558695 scopus 로고
    • Phagocytosis of particulate activators of the alternative complement pathway: Effects of fibronectin
    • Czop JK: Phagocytosis of particulate activators of the alternative complement pathway: Effects of fibronectin. Adv Immunol 1986;38:361–398.
    • (1986) Adv Immunol , vol.38 , pp. 361-398
    • Czop, J.K.1
  • 43
    • 0019379338 scopus 로고
    • Receptors for cold-insoluble globulin (plasma fibronectin) on human monocytes
    • Bevilacqua MP, Amrani D, Mosesson MW, et al: Receptors for cold-insoluble globulin (plasma fibronectin) on human monocytes. J Exp Med 1981;153:42–60.
    • (1981) J Exp Med , vol.153 , pp. 42-60
    • Bevilacqua, M.P.1    Amrani, D.2    Mosesson, M.W.3
  • 44
    • 0020554853 scopus 로고
    • Plasma fibronectin enhances phagocytosis of opsonized particles by human peripheral blood monocytes
    • Pommier CG, Inada S, Fried LF, et al: Plasma fibronectin enhances phagocytosis of opsonized particles by human peripheral blood monocytes. J Exp Med 1983;157:1844–1845.
    • (1983) J Exp Med , vol.157 , pp. 1844-1845
    • Pommier, C.G.1    Inada, S.2    Fried, L.F.3
  • 45
    • 0022606167 scopus 로고
    • The role of extracellular matrix proteins in the control of phagocytosis
    • Brown EJ: The role of extracellular matrix proteins in the control of phagocytosis. J Leuk Biol 1986;39:579–591.
    • (1986) J Leuk Biol , vol.39 , pp. 579-591
    • Brown, E.J.1
  • 46
    • 0018407792 scopus 로고
    • Initial adhesion of human fibroblasts in serum-free medium: Possible role of secreted fibronectin
    • Grinnell F, Feld MK: Initial adhesion of human fibroblasts in serum-free medium: Possible role of secreted fibronectin. Cell 1979;17:117–129.
    • (1979) Cell , vol.17 , pp. 117-129
    • Grinnell, F.1    Feld, M.K.2
  • 47
    • 0021849453 scopus 로고
    • Fibronectin, as well as other extracellular matrix proteins, mediates human keratinocyte adherence
    • Clark RAF, Folkvord JM, Wertz RL: Fibronectin, as well as other extracellular matrix proteins, mediates human keratinocyte adherence. J Invest Dermatol 1985;84:378–383.
    • (1985) J Invest Dermatol , vol.84 , pp. 378-383
    • Clark, R.A.F.1    Folkvord, J.M.2    Wertz, R.L.3
  • 48
    • 0021823943 scopus 로고
    • Spreading and enhanced motility of human keratinocytes on fibronectin
    • O'Keefe EJ, Payne RE Jr, Russell N, et al: Spreading and enhanced motility of human keratinocytes on fibronectin. J Invest Dermatol 1985;85:125–130.
    • (1985) J Invest Dermatol , vol.85 , pp. 125-130
    • O'Keefe, E.J.1    Payne, R.E.2    Russell, N.3
  • 49
    • 0020631409 scopus 로고
    • Adhesion of endothelial cells to extracellular matrix proteins
    • Macarak EJ, Howard PS: Adhesion of endothelial cells to extracellular matrix proteins. J Cell Physiol 1983;116:76–86.
    • (1983) J Cell Physiol , vol.116 , pp. 76-86
    • Macarak, E.J.1    Howard, P.S.2
  • 50
    • 0020637870 scopus 로고
    • Components of subendothelial aorta basement membrane: Immunohistochemical localization and role in cell attachment
    • Palotie A, Tryggvason K, Peltonen L, et al: Components of subendothelial aorta basement membrane: Immunohistochemical localization and role in cell attachment. Lab Invest 1983;49:362–370.
    • (1983) Lab Invest , vol.49 , pp. 362-370
    • Palotie, A.1    Tryggvason, K.2    Peltonen, L.3
  • 51
    • 0022735995 scopus 로고
    • Either exogenous or endogenous fibronectin can promote adherence of human endothelial cells
    • Clark RAF, Folkvord JM, Nielsen LD: Either exogenous or endogenous fibronectin can promote adherence of human endothelial cells. J Cell Sci 1986;82:263–280.
    • (1986) J Cell Sci , vol.82 , pp. 263-280
    • Clark, R.A.F.1    Folkvord, J.M.2    Nielsen, L.D.3
  • 52
    • 0023154497 scopus 로고
    • Lymphokines and platelets promote human monocyte adherence to fibrinogen and fibronectin in vitro
    • Horsburgh CR, Clark RAF, Kirkpatrick CH: Lymphokines and platelets promote human monocyte adherence to fibrinogen and fibronectin in vitro. J Leuk Biol 1987;41:14–24.
    • (1987) J Leuk Biol , vol.41 , pp. 14-24
    • Horsburgh, C.R.1    Clark, R.A.F.2    Kirkpatrick, C.H.3
  • 53
    • 0016719143 scopus 로고
    • Cross-linking of cold-insoluble globulin by fibrin-stabilizing factor
    • Mosher DF: Cross-linking of cold-insoluble globulin by fibrin-stabilizing factor. J Biol Chem 1975;250:6614–6621.
    • (1975) J Biol Chem , vol.250 , pp. 6614-6621
    • Mosher, D.F.1
  • 54
    • 0020645335 scopus 로고
    • Specificity of fibronectin-fibrin cross-linking
    • Mosher DF, Johnson RB: Specificity of fibronectin-fibrin cross-linking. Ann NY Acad Sci 1983;408:583–594.
    • (1983) Ann NY Acad Sci , vol.408 , pp. 583-594
    • Mosher, D.F.1    Johnson, R.B.2
  • 55
    • 0022627105 scopus 로고
    • Macrophage migration in fibrin gel matrices
    • Ciano PS, Colvin RB, Dvorak AM, et al: Macrophage migration in fibrin gel matrices. Lab Invest 1986;54:62–70.
    • (1986) Lab Invest , vol.54 , pp. 62-70
    • Ciano, P.S.1    Colvin, R.B.2    Dvorak, A.M.3
  • 56
    • 0018838451 scopus 로고
    • Fibroblast adhesion to fibrinogen and fibrin substrata: Requirement for cold-insoluble globulin (plasma fibronectin)
    • Grinnell F, Feld M, Minter D: Fibroblast adhesion to fibrinogen and fibrin substrata: Requirement for cold-insoluble globulin (plasma fibronectin). Cell 1980;19:517–525.
    • (1980) Cell , vol.19 , pp. 517-525
    • Grinnell, F.1    Feld, M.2    Minter, D.3
  • 57
    • 0019462552 scopus 로고
    • Distribution of fibronectin during wound healing in vivo
    • Grinnell F, Billingham RE, Burgess L: Distribution of fibronectin during wound healing in vivo. J Invest Dermatol 1981; 76:181–189.
    • (1981) J Invest Dermatol , vol.76 , pp. 181-189
    • Grinnell, F.1    Billingham, R.E.2    Burgess, L.3
  • 58
    • 0020447183 scopus 로고
    • Fibronectin involvement in granulation tissue and wound healing in rabbits
    • Repesh LA, Fitzgerald TJ, Furcht LT: Fibronectin involvement in granulation tissue and wound healing in rabbits. J Histochem Cytochem 1982;30:351–358.
    • (1982) J Histochem Cytochem , vol.30 , pp. 351-358
    • Repesh, L.A.1    Fitzgerald, T.J.2    Furcht, L.T.3
  • 59
    • 0020264236 scopus 로고
    • Fibronectin and fibrin provide a provisional matrix for epidermal cell migration during wound reepithelialization
    • Clark RAF, Lanigan JM, DellaPelle P, et al: Fibronectin and fibrin provide a provisional matrix for epidermal cell migration during wound reepithelialization. J Invest Dermatol 1982;70:264–269.
    • (1982) J Invest Dermatol , vol.70 , pp. 264-269
    • Clark, R.A.F.1    Lanigan, J.M.2    DellaPelle, P.3
  • 60
    • 0020315282 scopus 로고
    • Blood vessel fibronectin increases in conjunction with endothelial cell proliferation and capillary ingrowth during wound healing
    • Clark RAF, DellaPelle P, Manseau E, et al: Blood vessel fibronectin increases in conjunction with endothelial cell proliferation and capillary ingrowth during wound healing. J Invest Dermatol 1982;79:269–276.
    • (1982) J Invest Dermatol , vol.79 , pp. 269-276
    • Clark, R.A.F.1    DellaPelle, P.2    Manseau, E.3
  • 61
    • 0021085369 scopus 로고
    • Fibronectin promotes epithelial migration of cultured rabbit cornea in situ
    • Nishida T, Nakagawa S, Awata T, et al: Fibronectin promotes epithelial migration of cultured rabbit cornea in situ. J Cell Biol 1983;97:1653–1657.
    • (1983) J Cell Biol , vol.97 , pp. 1653-1657
    • Nishida, T.1    Nakagawa, S.2    Awata, T.3
  • 62
    • 0021808133 scopus 로고
    • Location of a fibronectin domain involved in newt epidermal cell migration
    • Donaldson DJ, Mahan JT, Hasty DL, et al: Location of a fibronectin domain involved in newt epidermal cell migration. J Cell Biol 1985;101:73–78.
    • (1985) J Cell Biol , vol.101 , pp. 73-78
    • Donaldson, D.J.1    Mahan, J.T.2    Hasty, D.L.3
  • 63
    • 0020608690 scopus 로고
    • Fibronectin: A new therapy for corneal trophic ulcer
    • Nishida T, Ohashi Y, Awata T, et al: Fibronectin: A new therapy for corneal trophic ulcer. Arch Ophthalmol 1983;101:1046–1048.
    • (1983) Arch Ophthalmol , vol.101 , pp. 1046-1048
    • Nishida, T.1    Ohashi, Y.2    Awata, T.3
  • 64
    • 0021275947 scopus 로고
    • In vivo codistribution of fibronectin and actin fibers in granulation tissue: Immunofluorescence and electron microscope studies of the fibronexus at the myofibroblast surface
    • Singer II, Kawka DW, Kazazis DM, et al: In vivo codistribution of fibronectin and actin fibers in granulation tissue: Immunofluorescence and electron microscope studies of the fibronexus at the myofibroblast surface. J Cell Biol 1984;98:2091–2106.
    • (1984) J Cell Biol , vol.98 , pp. 2091-2106
    • Singer, I.I.1    Kawka, D.W.2    Kazazis, D.M.3
  • 65
    • 0022256413 scopus 로고
    • Localization of the fibronexus at the surface of granulation tissue myofibroblasts using double-label immunogold electron microscopy on ultrathin frozen sections
    • Singer II, Kawka DW, Kazazis DM: Localization of the fibronexus at the surface of granulation tissue myofibroblasts using double-label immunogold electron microscopy on ultrathin frozen sections. Eur J Cell Biol 1985;38:94–101.
    • (1985) Eur J Cell Biol , vol.38 , pp. 94-101
    • Singer, I.I.1    Kawka, D.W.2    Kazazis, D.M.3
  • 66
    • 0344038731 scopus 로고
    • Ultrastructural identification of extension aminopeptides of type I and III collagens in human skin
    • Fleischmajer R, Timpl R, Tuderman L, et al: Ultrastructural identification of extension aminopeptides of type I and III collagens in human skin. Proc Natl Acad Sci USA 1981;78:7360–7364.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 7360-7364
    • Fleischmajer, R.1    Timpl, R.2    Tuderman, L.3
  • 67
    • 0018346005 scopus 로고
    • Isolation of the pericellular matrix of human fibroblast cultures
    • Hedman K, Kurkinen M, Alitalo K, et al: Isolation of the pericellular matrix of human fibroblast cultures. J Cell Biol 1979; 81:83–91.
    • (1979) J Cell Biol , vol.81 , pp. 83-91
    • Hedman, K.1    Kurkinen, M.2    Alitalo, K.3
  • 68
    • 0020030958 scopus 로고
    • Structure of the pericellular matrix: Association of heparan and chondroitin sulfate with fibronectin-procollagen fibers
    • Hedman K, Johansson S, Vartio T, et al: Structure of the pericellular matrix: Association of heparan and chondroitin sulfate with fibronectin-procollagen fibers. Cell 1982;28:663–671.
    • (1982) Cell , vol.28 , pp. 663-671
    • Hedman, K.1    Johansson, S.2    Vartio, T.3
  • 69
    • 0021397224 scopus 로고
    • Integrity of the pericellular fibronectin matrix of fibroblasts is independent of sulfated glycosaminoglycans
    • Hedman K, Vartio T, Johansson S, et al: Integrity of the pericellular fibronectin matrix of fibroblasts is independent of sulfated glycosaminoglycans. EMBO J 1984;3:581–584.
    • (1984) EMBO J , vol.3 , pp. 581-584
    • Hedman, K.1    Vartio, T.2    Johansson, S.3
  • 70
    • 0021262427 scopus 로고
    • The role of intermolecular disulfide bonding in deposition of GP 140 in the extracellular matrix
    • Carter WG: The role of intermolecular disulfide bonding in deposition of GP 140 in the extracellular matrix. J Cell Biol 1984;99:105–114.
    • (1984) J Cell Biol , vol.99 , pp. 105-114
    • Carter, W.G.1
  • 71
    • 0020072924 scopus 로고
    • Role of fibronectin in collagen deposition: Fab1 to the gelatin-binding domain of fibronectin inhibits both fibronectin and collagen organization in fibroblast extracellular matrix
    • McDonald JA, Kelley DG, Broekelmann TJ: Role of fibronectin in collagen deposition: Fab1 to the gelatin-binding domain of fibronectin inhibits both fibronectin and collagen organization in fibroblast extracellular matrix. J Cell Biol 1982;92:485–492.
    • (1982) J Cell Biol , vol.92 , pp. 485-492
    • McDonald, J.A.1    Kelley, D.G.2    Broekelmann, T.J.3
  • 72
    • 0022457822 scopus 로고
    • The biology of platelet-derived growth factor
    • Ross R, Raines EW, Bowen-Pope DF: The biology of platelet-derived growth factor. Cell 1986;46:155–169.
    • (1986) Cell , vol.46 , pp. 155-169
    • Ross, R.1    Raines, E.W.2    Bowen-Pope, D.F.3
  • 73
    • 0019467882 scopus 로고
    • The removal of extracellular fibronectin from areas of cell-substrate contact
    • Avnur Z, Geiger B: The removal of extracellular fibronectin from areas of cell-substrate contact. Cell 1981;25:121–132.
    • (1981) Cell , vol.25 , pp. 121-132
    • Avnur, Z.1    Geiger, B.2
  • 74
    • 0021946006 scopus 로고
    • Development of cell surface linkage complexes in cultured fibroblasts
    • Chen WT, Hasegawa E, Hasegawa T, et al: Development of cell surface linkage complexes in cultured fibroblasts. J Cell Biol 1985;100:1103–1114.
    • (1985) J Cell Biol , vol.100 , pp. 1103-1114
    • Chen, W.T.1    Hasegawa, E.2    Hasegawa, T.3
  • 75
    • 0021957079 scopus 로고
    • Distribution of the cell substratum attachment (CSAT) antigen on myogenic and fibroblastic cells in culture
    • Damskey CH, Knudsen KA, Bradley D, et al: Distribution of the cell substratum attachment (CSAT) antigen on myogenic and fibroblastic cells in culture. J Cell Biol 1985;100:1528–1539.
    • (1985) J Cell Biol , vol.100 , pp. 1528-1539
    • Damskey, C.H.1    Knudsen, K.A.2    Bradley, D.3
  • 76
    • 0019253791 scopus 로고
    • An axial periodic fibrillar arrangement of antigenic determinants for fibronectin and procollagen on ascorbate treated human fibroblasts
    • Furcht LT, Wendelschafer C, Mosher DF, et al: An axial periodic fibrillar arrangement of antigenic determinants for fibronectin and procollagen on ascorbate treated human fibroblasts. J Supramol Struct 1980;13:15–33.
    • (1980) J Supramol Struct , vol.13 , pp. 15-33
    • Furcht, L.T.1    Wendelschafer, C.2    Mosher, D.F.3
  • 77
    • 0020681386 scopus 로고
    • Immunocytochemical localization of fibronectin in human fibroblast cultures using a cell surface replica technique
    • Irish PS, Hasty DL: Immunocytochemical localization of fibronectin in human fibroblast cultures using a cell surface replica technique. J Histochem Cytochem 1980;31:69–77.
    • (1980) J Histochem Cytochem , vol.31 , pp. 69-77
    • Irish, P.S.1    Hasty, D.L.2
  • 79
    • 0021990020 scopus 로고
    • Incorporation of cellular and plasma (fibronectin) into smooth muscle cell extracellular matrix in vitro
    • Millis AJ, Hoyle M, Mann DM, et al: Incorporation of cellular and plasma (fibronectin) into smooth muscle cell extracellular matrix in vitro. Proc Natl Acad Sci USA 1985;82:2746–2750.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 2746-2750
    • Millis, A.J.1    Hoyle, M.2    Mann, D.M.3
  • 80
    • 0023178166 scopus 로고
    • Both the cell adhesive domain and an aminoterminal matrix assembly domain participate in fibronectin assembly into fibroblast pericellular matrix
    • McDonald JA, Quade BJ, Broekelmann TJ, et al: Both the cell adhesive domain and an aminoterminal matrix assembly domain participate in fibronectin assembly into fibroblast pericellular matrix. J Biol Chem 1987;262:2957–2967.
    • (1987) J Biol Chem , vol.262 , pp. 2957-2967
    • McDonald, J.A.1    Quade, B.J.2    Broekelmann, T.J.3
  • 81
    • 0021926873 scopus 로고
    • Interaction of the 70 000-mol-wt aminoterminal fragment of fibronectin with the matrixassembly receptor of fibroblasts
    • McKeown-Longo PJ, Mosher DF: Interaction of the 70 000-mol-wt aminoterminal fragment of fibronectin with the matrixassembly receptor of fibroblasts. J Cell Biol 1985;100:364–374.
    • (1985) J Cell Biol , vol.100 , pp. 364-374
    • McKeown-Longo, P.J.1    Mosher, D.F.2
  • 82
    • 0021017503 scopus 로고
    • Role of fibronectin as a growth factor for fibroblasts
    • Bitterman PB, Rennard SI, Adelbert S, et al: Role of fibronectin as a growth factor for fibroblasts. J Cell Biol 1983; 97:1925–1932.
    • (1983) J Cell Biol , vol.97 , pp. 1925-1932
    • Bitterman, P.B.1    Rennard, S.I.2    Adelbert, S.3
  • 83
    • 0023240580 scopus 로고
    • Fibronectin-associated transforming growth factor
    • Fava RA, McClure DB: Fibronectin-associated transforming growth factor. J Cell Physiol 1987;131:184–189.
    • (1987) J Cell Physiol , vol.131 , pp. 184-189
    • Fava, R.A.1    McClure, D.B.2
  • 84
    • 0342674048 scopus 로고
    • Type β-transforming growth factor: A bifunctional regulator of cellular growth
    • Roberts AB, Anzano MA, Wakefield LM: Type β-transforming growth factor: A bifunctional regulator of cellular growth. Proc Natl Acad Sci USA 1985;82:119–123.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 119-123
    • Roberts, A.B.1    Anzano, M.A.2    Wakefield, L.M.3
  • 85
    • 37049184914 scopus 로고
    • Polypeptide transforming growth factors isolated from bovine sources and used for wound healing in vivo
    • Sporn MB, Roberts AB, Shull JH, et al: Polypeptide transforming growth factors isolated from bovine sources and used for wound healing in vivo. Science 1983;219:1329–1331.
    • (1983) Science , vol.219 , pp. 1329-1331
    • Sporn, M.B.1    Roberts, A.B.2    Shull, J.H.3
  • 86
    • 0022471924 scopus 로고
    • Transforming growth factor type β: Rapid induction of fibrosis and angiogenesis in vivo and stimulation of collagen formation in vitro
    • Roberts AB, Sporn MB, Assoian RK, et al: Transforming growth factor type β: Rapid induction of fibrosis and angiogenesis in vivo and stimulation of collagen formation in vitro. Proc Natl Acad Sci USA 1986;83:4167–4171.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4167-4171
    • Roberts, A.B.1    Sporn, M.B.2    Assoian, R.K.3
  • 87
    • 0022666942 scopus 로고    scopus 로고
    • The reversal of an adriamycin-induced healing impairment with chemoattractants and growth factors
    • Lawrence WT, Norton JA, Sporn MB, et al: The reversal of an adriamycin-induced healing impairment with chemoattractants and growth factors. Ann Surg 196;203:142–147.
    • Ann Surg 196 , vol.203 , pp. 142-147
    • Lawrence, W.T.1    Norton, J.A.2    Sporn, M.B.3
  • 88
    • 0019984778 scopus 로고
    • Fibronectin is produced by blood vessels in response to injury
    • Clark RAF, Quinn JH, Winn HJ, et al: Fibronectin is produced by blood vessels in response to injury. J Exp Med 1982; 156:646–651.
    • (1982) J Exp Med , vol.156 , pp. 646-651
    • Clark, R.A.F.1    Quinn, J.H.2    Winn, H.J.3
  • 89
    • 0020584786 scopus 로고
    • Fibronectin beneath reepithelializing epidermis in vivo: Sources and significance
    • Clark RAF, Winn HJ, Dvorak HF, et al: Fibronectin beneath reepithelializing epidermis in vivo: Sources and significance. J Invest Dermatol 1983;80(suppl):26S–30S.
    • (1983) J Invest Dermatol , vol.80 , pp. 26S-30S
    • Clark, R.A.F.1    Winn, H.J.2    Dvorak, H.F.3
  • 90
    • 0018093807 scopus 로고
    • Cryoprecipitate reversal of opsonic alpha-2-surface binding glycoprotein deficiencies in septic surgical trauma patients
    • Saba TM, Blumenstock FA, Bernard H: Cryoprecipitate reversal of opsonic alpha-2-surface binding glycoprotein deficiencies in septic surgical trauma patients. Science 1978:201:622–624.
    • (1978) Science , vol.201 , pp. 622-624
    • Saba, T.M.1    Blumenstock, F.A.2    Bernard, H.3
  • 91
    • 0022392581 scopus 로고
    • Purified fibronectin administration to patients with severe abdominal infections: A controlled study
    • Lundsgaard-Hansen P, Doran JE, Ruli E, et al: Purified fibronectin administration to patients with severe abdominal infections: A controlled study. Ann Surg 1985;202:745–759.
    • (1985) Ann Surg , vol.202 , pp. 745-759
    • Lundsgaard-Hansen, P.1    Doran, J.E.2    Ruli, E.3


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