메뉴 건너뛰기




Volumn 10, Issue 1, 1998, Pages 12-32

Cutaneous wound repair

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0032331067     PISSN: 10447946     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (67)

References (252)
  • 1
    • 0028212519 scopus 로고
    • Definitions and guidelines for assessment of wounds and evaluation of healing
    • Lazarus GS, Cooper DM, Knighton DR, et al. Definitions and guidelines for assessment of wounds and evaluation of healing. Arch Dermatol 1994;130:489-493.
    • (1994) Arch Dermatol , vol.130 , pp. 489-493
    • Lazarus, G.S.1    Cooper, D.M.2    Knighton, D.R.3
  • 2
    • 4944267611 scopus 로고    scopus 로고
    • Responses to cellular injury
    • Underwood JCE (ed). London, UK, Churchill Livingstone
    • Goepel JR. Responses to cellular injury. In: Underwood JCE (ed). General and Systemic Pathology, Second Edition. London, UK, Churchill Livingstone, 1996, pp 121-122.
    • (1996) General and Systemic Pathology, Second Edition , pp. 121-122
    • Goepel, J.R.1
  • 3
    • 0015538642 scopus 로고
    • Mechanical, biochemical and architectural features of surgical repair
    • Forrester JC. Mechanical, biochemical and architectural features of surgical repair. Adv Biol Med Phys 1973;14:1-3.
    • (1973) Adv Biol Med Phys , vol.14 , pp. 1-3
    • Forrester, J.C.1
  • 4
    • 0442273830 scopus 로고    scopus 로고
    • Wound healing
    • Walter and Israel (eds). London, UK, Churchill Livingstone
    • Walter JB, Talbot IC. Wound healing. In: Walter and Israel (eds). General Pathology, Seventh Edition. London, UK, Churchill Livingstone, 1996, pp 165-180.
    • (1996) General Pathology, Seventh Edition , pp. 165-180
    • Walter, J.B.1    Talbot, I.C.2
  • 9
    • 0023889023 scopus 로고
    • Macrophage migration in fibrin gel matrices II. Effects of clotting factor XIII, fibronectin and glycosaminoglycan content on cell migration
    • Lanir N, Ciano PS, van de Water L, et al. Macrophage migration in fibrin gel matrices II. Effects of clotting factor XIII, fibronectin and glycosaminoglycan content on cell migration. J Immunol 1988;140:2340-2349.
    • (1988) J Immunol , vol.140 , pp. 2340-2349
    • Lanir, N.1    Ciano, P.S.2    Van De Water, L.3
  • 11
    • 0021068821 scopus 로고
    • Hageman factor-dependent pathways: Mechanism of initiation and bradykinin formation
    • Kaplan AP. Hageman factor-dependent pathways: mechanism of initiation and bradykinin formation. Fed Proc 1983;42:3123-3127.
    • (1983) Fed Proc , vol.42 , pp. 3123-3127
    • Kaplan, A.P.1
  • 12
    • 0020456713 scopus 로고
    • An alternative extrinsic pathway of human blood coagulation
    • Marlar K, Kleiss A, Griffin JH. An alternative extrinsic pathway of human blood coagulation. Blood 1982;60:1353-1356.
    • (1982) Blood , vol.60 , pp. 1353-1356
    • Marlar, K.1    Kleiss, A.2    Griffin, J.H.3
  • 14
    • 0007514819 scopus 로고
    • Role of platelets in inflammation and rheumatic disease
    • Ginsberg M. Role of platelets in inflammation and rheumatic disease. Adv Inflam Res 1981;2:53-55.
    • (1981) Adv Inflam Res , vol.2 , pp. 53-55
    • Ginsberg, M.1
  • 15
    • 0025721834 scopus 로고
    • Human wound fluid from acute wounds stimulates fibroblast and endothelial cell growth
    • Katz MH, Kirsner RS, Eaglstein WH, et al. Human wound fluid from acute wounds stimulates fibroblast and endothelial cell growth. J Am Acad Dermatol 1991;25:1054-1058.
    • (1991) J Am Acad Dermatol , vol.25 , pp. 1054-1058
    • Katz, M.H.1    Kirsner, R.S.2    Eaglstein, W.H.3
  • 17
    • 0001299207 scopus 로고
    • Platelet factor 4 is a chemotactic factor for neutrophils and monocytes
    • Deuel TF, Senior RM, Chang D, et al. Platelet factor 4 is a chemotactic factor for neutrophils and monocytes. Proc Natl Acad Sci USA 1981;74:4584-1587.
    • (1981) Proc Natl Acad Sci USA , vol.74 , pp. 4584-11587
    • Deuel, T.F.1    Senior, R.M.2    Chang, D.3
  • 18
    • 0025905809 scopus 로고
    • EGF and TGFa in wound healing and repair
    • Schultz G, Rotari DS, Clark W. EGF and TGFa in wound healing and repair. J Cell Biochem 1991;45:346-352.
    • (1991) J Cell Biochem , vol.45 , pp. 346-352
    • Schultz, G.1    Rotari, D.S.2    Clark, W.3
  • 19
    • 0026445528 scopus 로고
    • Transforming growth factor beta: Recent progress and new challenges
    • Sporn MB, Roberts AM. Transforming growth factor beta: recent progress and new challenges. J Cell Biol 1992;119:1017-1021.
    • (1992) J Cell Biol , vol.119 , pp. 1017-1021
    • Sporn, M.B.1    Roberts, A.M.2
  • 20
    • 0017094798 scopus 로고
    • An enzyme isolated from arteries transforms prostaglandin endoperoxidases to an unstable substance that inhibits platelet aggregation
    • Moncada S, Gryglewski R, Bunting S, et al. An enzyme isolated from arteries transforms prostaglandin endoperoxidases to an unstable substance that inhibits platelet aggregation. Nature 1976;263:663-665.
    • (1976) Nature , vol.263 , pp. 663-665
    • Moncada, S.1    Gryglewski, R.2    Bunting, S.3
  • 21
    • 0021993442 scopus 로고
    • Interaction of antithrombin III with bovine aortic segments
    • Stern DM, Nawroth PP, Marcum J, et al. Interaction of antithrombin III with bovine aortic segments. J Clin Invest 1985;75:272-279.
    • (1985) J Clin Invest , vol.75 , pp. 272-279
    • Stern, D.M.1    Nawroth, P.P.2    Marcum, J.3
  • 22
    • 0023744090 scopus 로고
    • Inactivation of human factor VII by activated protein C: Cofactor activity of protein S and protective effect of von Willebrand factor
    • Loedam JA, Meijers JCM, Sixma JJ, et al. Inactivation of human factor VII by activated protein C: cofactor activity of protein S and protective effect of von Willebrand factor. J Clin Invest 1988;82:1236-1243.
    • (1988) J Clin Invest , vol.82 , pp. 1236-1243
    • Loedam, J.A.1    Meijers, J.C.M.2    Sixma, J.J.3
  • 23
    • 0030007064 scopus 로고    scopus 로고
    • Impaired wound healing in mice with a disrupted plasminogen gene
    • Romer J, Bugge TH, Pyke C, et al. Impaired wound healing in mice with a disrupted plasminogen gene. Nature Medicine 1996;2(3):287-292.
    • (1996) Nature Medicine , vol.2 , Issue.3 , pp. 287-292
    • Romer, J.1    Bugge, T.H.2    Pyke, C.3
  • 24
    • 0024152111 scopus 로고
    • Kinin formation: Mechanisms and role in inflammatory disorders
    • Proud D, Kaplan AP. Kinin formation: mechanisms and role in inflammatory disorders. Ann Rev Immunol 1988;6:49-83.
    • (1988) Ann Rev Immunol , vol.6 , pp. 49-83
    • Proud, D.1    Kaplan, A.P.2
  • 25
    • 0019471542 scopus 로고
    • Activation of classic pathway of complement, by hageman factor fragment
    • Ghebrehiwet B, Silverberg M, Kaplan AP. Activation of classic pathway of complement, by hageman factor fragment. J Exp Med 1981;153:665-676.
    • (1981) J Exp Med , vol.153 , pp. 665-676
    • Ghebrehiwet, B.1    Silverberg, M.2    Kaplan, A.P.3
  • 26
    • 0017413401 scopus 로고
    • Haemodialysis leukopenia: Pulmonary vascular leukostasis resulting from complement activation by dialyzer cellophane membrane
    • Craddock P, Fehr J, Dalmasso A, et al. Haemodialysis leukopenia: pulmonary vascular leukostasis resulting from complement activation by dialyzer cellophane membrane. J Clin Invest 1977;59:879-888.
    • (1977) J Clin Invest , vol.59 , pp. 879-888
    • Craddock, P.1    Fehr, J.2    Dalmasso, A.3
  • 27
    • 0019363448 scopus 로고
    • Medication of increased vascular permeability after complement activation: Histamine independent activation of C5a
    • Williams TJ, Jose PL. Medication of increased vascular permeability after complement activation: histamine independent activation of C5a. J Exp Med 1981;153:136-153.
    • (1981) J Exp Med , vol.153 , pp. 136-153
    • Williams, T.J.1    Jose, P.L.2
  • 28
    • 0015508445 scopus 로고
    • The relationship of the renal vasodilator action of bradykinin to the release of PGE-like substances
    • Terragno NA, Lonigro AJ, Malik KW, et al. The relationship of the renal vasodilator action of bradykinin to the release of PGE-like substances. Experimentia 1972;28:437-439.
    • (1972) Experimentia , vol.28 , pp. 437-439
    • Terragno, N.A.1    Lonigro, A.J.2    Malik, K.W.3
  • 29
    • 0004781612 scopus 로고
    • Factors that affect vessel reactivity and leukocyte emigration
    • Clark RAF, Henson PM (eds). London, UK, Plenum Press
    • Williams TJ. Factors that affect vessel reactivity and leukocyte emigration. In: Clark RAF, Henson PM (eds). The Molecular and Cellular Biology of Wound Repair. London, UK, Plenum Press, 1988, pp 115-183.
    • (1988) The Molecular and Cellular Biology of Wound Repair , pp. 115-183
    • Williams, T.J.1
  • 30
    • 0019514812 scopus 로고
    • Control of vascular permeability by polymorphonuclear leukocytes, in inflammation
    • Wedmore CV, Williams TJ. Control of vascular permeability by polymorphonuclear leukocytes, in inflammation. Nature 1981;289:646-650.
    • (1981) Nature , vol.289 , pp. 646-650
    • Wedmore, C.V.1    Williams, T.J.2
  • 31
    • 0021952732 scopus 로고
    • Chemotactic responses of human peripheral blood monocytes to the complement-derived peptides C5a and C5a des Arg
    • Marder SR, Chenoweth DE, Goldstein IM, et al. Chemotactic responses of human peripheral blood monocytes to the complement-derived peptides C5a and C5a des Arg. J Immunol 1985;134:3325-3331.
    • (1985) J Immunol , vol.134 , pp. 3325-3331
    • Marder, S.R.1    Chenoweth, D.E.2    Goldstein, I.M.3
  • 32
    • 0009763056 scopus 로고
    • A histochemical analysis of mononuclear cell infiltrates of the skin, with particular reference to delayed hypersensitivity in the guinea pig
    • Turk JL, Heather CJ, Diengdoh JV. A histochemical analysis of mononuclear cell infiltrates of the skin, with particular reference to delayed hypersensitivity in the guinea pig. Int Arch Allergy Appl Immunol 1976;29:278-289.
    • (1976) Int Arch Allergy Appl Immunol , vol.29 , pp. 278-289
    • Turk, J.L.1    Heather, C.J.2    Diengdoh, J.V.3
  • 33
    • 0022534483 scopus 로고
    • Effects of fibrinogen derivatives upon the inflammatory response
    • Senior RM, Skogen WF, Griffin GI. Effects of fibrinogen derivatives upon the inflammatory response. J Clin Invest 1986;77:1014-1019.
    • (1986) J Clin Invest , vol.77 , pp. 1014-1019
    • Senior, R.M.1    Skogen, W.F.2    Griffin, G.I.3
  • 34
    • 0016637528 scopus 로고
    • The generation of chemotactic activity for human leukocytes by the action of plasmin on human fibrinogen
    • McKenzie R, Pepper DS, Kay AB. The generation of chemotactic activity for human leukocytes by the action of plasmin on human fibrinogen. Thromb Res 1975;6:1-8.
    • (1975) Thromb Res , vol.6 , pp. 1-8
    • McKenzie, R.1    Pepper, D.S.2    Kay, A.B.3
  • 35
    • 0019311062 scopus 로고
    • Leukotriene B, a potent chemokinetic and aggregating substance, released from polymorphonuclear leukocytes
    • Ford-Hutchinson AW, Bray MA, Doig MV, et al. Leukotriene B, a potent chemokinetic and aggregating substance, released from polymorphonuclear leukocytes. Nature 1980;286:264-265.
    • (1980) Nature , vol.286 , pp. 264-265
    • Ford-Hutchinson, A.W.1    Bray, M.A.2    Doig, M.V.3
  • 36
    • 0019333893 scopus 로고
    • Further studies on the structural requirement for synthetic peptide chemoattractants
    • Freer RJ, Day AR, Radding JA, et al. Further studies on the structural requirement for synthetic peptide chemoattractants. Biochem 1980;19:2404-2410.
    • (1980) Biochem , vol.19 , pp. 2404-2410
    • Freer, R.J.1    Day, A.R.2    Radding, J.A.3
  • 37
    • 0022555858 scopus 로고
    • Platelet activating factor: A biologically active phosphoglyceride
    • Hanahan DJ. Platelet activating factor: a biologically active phosphoglyceride. Ann Rev Biochem 1986;55:483-509.
    • (1986) Ann Rev Biochem , vol.55 , pp. 483-509
    • Hanahan, D.J.1
  • 38
    • 0023091309 scopus 로고
    • Tumour necrosis factor is chemotactic for monocytes and polymorphonuclear leukocytes
    • Ming WJ, Bersani L, Mantovani A. Tumour necrosis factor is chemotactic for monocytes and polymorphonuclear leukocytes. J Immunol 1987;138:469-474.
    • (1987) J Immunol , vol.138 , pp. 469-474
    • Ming, W.J.1    Bersani, L.2    Mantovani, A.3
  • 39
    • 0024360854 scopus 로고
    • Platelet derived growth factor and transforming growth factor-beta enhance tissue repair activities by unique mechanisms
    • Pierce GF, Mustoe TA, Lingelbach J, et al. Platelet derived growth factor and transforming growth factor-beta enhance tissue repair activities by unique mechanisms. J Cell Biol 1989;109:429-440.
    • (1989) J Cell Biol , vol.109 , pp. 429-440
    • Pierce, G.F.1    Mustoe, T.A.2    Lingelbach, J.3
  • 40
    • 0002612813 scopus 로고    scopus 로고
    • Macrophage involvement in wound repair, remodelling and fibrosis
    • Clark RAF (ed). London, UK, Plenum Press
    • Riches DWH. Macrophage involvement in wound repair, remodelling and fibrosis. In: Clark RAF (ed). The Molecular and Cellualr Biology of Wound Repair, Second Edition. London, UK, Plenum Press, 1996, pp 95-141.
    • (1996) The Molecular and Cellualr Biology of Wound Repair, Second Edition , pp. 95-141
    • Riches, D.W.H.1
  • 41
    • 0028052968 scopus 로고
    • Interleukin-8 and related chemotactic cytokines-CXC and CC chemokines
    • Baggiolini M, Dewald B, Moser B. Interleukin-8 and related chemotactic cytokines-CXC and CC chemokines. Adv Immunol 1994;55:97-179.
    • (1994) Adv Immunol , vol.55 , pp. 97-179
    • Baggiolini, M.1    Dewald, B.2    Moser, B.3
  • 42
    • 0025724929 scopus 로고
    • Stimulus specific induction of monocyte chemotactic protein-1 (MCP-1) gene expression
    • Kunkel SL, Standiford T, Kasahara K, et al. Stimulus specific induction of monocyte chemotactic protein-1 (MCP-1) gene expression. Adv Exp Med Biol 1991;305:65-71.
    • (1991) Adv Exp Med Biol , vol.305 , pp. 65-71
    • Kunkel, S.L.1    Standiford, T.2    Kasahara, K.3
  • 43
    • 0024208591 scopus 로고
    • Resolution of the two components of macrophage inflammatory protein 1, and cloming and characterisation of one of those components, macrophage inflammatory protein 1 beta
    • Sherry B, Tekamp O, Gallegos C, et al. Resolution of the two components of macrophage inflammatory protein 1, and cloming and characterisation of one of those components, macrophage inflammatory protein 1 beta. J Exp Med 1988;168:2251-2259.
    • (1988) J Exp Med , vol.168 , pp. 2251-2259
    • Sherry, B.1    Tekamp, O.2    Gallegos, C.3
  • 44
    • 11644269215 scopus 로고
    • Platelet-derived endothelial cell growth factor (PD-ECGF) in angiogenesis and wound healing
    • Cited from abstract, Oxford, UK
    • Pierce GF, Yanagihara D, Costigan V, et al. Platelet-derived endothelial cell growth factor (PD-ECGF) in angiogenesis and wound healing. Cited from abstract, 1st European Issue Repair Society Meeting, Oxford, UK, 1991.
    • (1991) 1st European Issue Repair Society Meeting
    • Pierce, G.F.1    Yanagihara, D.2    Costigan, V.3
  • 45
    • 0020662680 scopus 로고
    • Chemotactic response of monocytes to thrombin
    • Bar-Shavit R, Kahn A, Fenton JW, et al. Chemotactic response of monocytes to thrombin. J Cell Biol 1983;96:282-285.
    • (1983) J Cell Biol , vol.96 , pp. 282-285
    • Bar-Shavit, R.1    Kahn, A.2    Fenton, J.W.3
  • 46
    • 85012405294 scopus 로고
    • Collagen and collagen peptide-induced chemotaxis of human blood monocytes
    • Postlethwaite AE, Kang AH. Collagen and collagen peptide-induced 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
  • 47
    • 0018893350 scopus 로고
    • Chemotactic activity of elastin-derived peptides
    • Senior 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
    • Senior, R.M.1    Griffin, G.L.2    Mecham, R.P.3
  • 48
    • 0021170197 scopus 로고
    • Val-Gly-Val-Ala-Pro-Gly, a repeating peptide in elastin, is chemotactic for fibroblasts and monocytes
    • Senior RM, Griffin GL, Mecham RP, et al. Val-Gly-Val-Ala-Pro-Gly, a repeating peptide in elastin, is chemotactic for fibroblasts and monocytes. J Cell Biol 1984;99:870-874.
    • (1984) J Cell Biol , vol.99 , pp. 870-874
    • Senior, R.M.1    Griffin, G.L.2    Mecham, R.P.3
  • 49
    • 0001674312 scopus 로고
    • Cutaneous wound repair
    • Goldsmith LE (ed). Oxford, UK, Oxford University Press
    • Clark RAF. Cutaneous wound repair. In: Goldsmith LE (ed). Biochemistry and Physiology of the Skin. Oxford, UK, Oxford University Press, 1990, pp 575-601.
    • (1990) Biochemistry and Physiology of the Skin , pp. 575-601
    • Clark, R.A.F.1
  • 51
    • 0025182959 scopus 로고
    • Adhesion receptors of the immune system
    • Springer TA. Adhesion receptors of the immune system. Nature 1990;346:425-434.
    • (1990) Nature , vol.346 , pp. 425-434
    • Springer, T.A.1
  • 52
    • 0023083976 scopus 로고
    • Leucocyte adhesion deficiency: An inherited defect in the Mac-1, LFA-1 and gp150,95 glycoproteins
    • Anderson DC, Springer TA. Leucocyte adhesion deficiency: an inherited defect in the Mac-1, LFA-1 and gp150,95 glycoproteins. Annu Rev Med 1987;38:175-194.
    • (1987) Annu Rev Med , vol.38 , pp. 175-194
    • Anderson, D.C.1    Springer, T.A.2
  • 53
    • 0025195758 scopus 로고
    • Leucocyte adhesion molecule deficiency: Its structural basis, pathophysiology and implications for modulating the inflammatory response
    • Amaout MA. Leucocyte adhesion molecule deficiency: its structural basis, pathophysiology and implications for modulating the inflammatory response. Immunol Rev 1990;114:145-180.
    • (1990) Immunol Rev , vol.114 , pp. 145-180
    • Amaout, M.A.1
  • 54
    • 0026499960 scopus 로고
    • Endothelial cell interactions with granulocytes: Tethering and signalling molecules
    • Zimmerman GA, Prescott SM, McIntyre TM. Endothelial cell interactions with granulocytes: tethering and signalling molecules. Immunol Today 1992;13:93-102.
    • (1992) Immunol Today , vol.13 , pp. 93-102
    • Zimmerman, G.A.1    Prescott, S.M.2    McIntyre, T.M.3
  • 55
    • 0025854524 scopus 로고
    • Leucocytes roll on a selectin at physiological flow rates: Distinction from and prerequisite for adhesion through integrins
    • Lawrence MB, Springer TA. Leucocytes roll on a selectin at physiological flow rates: distinction from and prerequisite for adhesion through integrins. Cell 1991;65:859-867.
    • (1991) Cell , vol.65 , pp. 859-867
    • Lawrence, M.B.1    Springer, T.A.2
  • 56
    • 0026690271 scopus 로고
    • Simulation of cell rolling and adhesion on surfaces in shear flow: General results and analysis of selectin-mediated neutrophil adhesion
    • Hammer DA, Apte SM. Simulation of cell rolling and adhesion on surfaces in shear flow: general results and analysis of selectin-mediated neutrophil adhesion. Biophys J 1992;63:35-43.
    • (1992) Biophys J , vol.63 , pp. 35-43
    • Hammer, D.A.1    Apte, S.M.2
  • 57
    • 0026661573 scopus 로고
    • P-selectin and E-selectin. Distinct but overlapping leucocyte ligand specificities
    • Larsen GR, Sako D, Ahern TJ, et al. P-selectin and E-selectin. Distinct but overlapping leucocyte ligand specificities. J Biol Chem 1992;267:11104-11112.
    • (1992) J Biol Chem , vol.267 , pp. 11104-11112
    • Larsen, G.R.1    Sako, D.2    Ahern, T.J.3
  • 58
    • 0024411402 scopus 로고
    • Co-operative interactions of LFA-1 and Mac-1 with intercellular adhesion molecule-1 in facilitating adherence and transendothelial migration of human neutrophils in vitro
    • Smith CW, Marlin SD, Rothlein R, et al. Co-operative interactions of LFA-1 and Mac-1 with intercellular adhesion molecule-1 in facilitating adherence and transendothelial migration of human neutrophils in vitro. J Clin Invest 1989;83:2008-2017.
    • (1989) J Clin Invest , vol.83 , pp. 2008-2017
    • Smith, C.W.1    Marlin, S.D.2    Rothlein, R.3
  • 59
    • 0028231065 scopus 로고
    • Adhesion molecules and inflammatory injury
    • Albelda SM, Smith CW, Ward PA. Adhesion molecules and inflammatory injury. FASEB J 1994;8(8):504-512.
    • (1994) FASEB J , vol.8 , Issue.8 , pp. 504-512
    • Albelda, S.M.1    Smith, C.W.2    Ward, P.A.3
  • 60
    • 0027988669 scopus 로고
    • Essential involvement of interleukin-8 (IL-8) in acute inflammation
    • Harada A, Sekido N, Akahoshi T, et al. Essential involvement of interleukin-8 (IL-8) in acute inflammation. J Leukocyte Biol 1994;56(5):559-564.
    • (1994) J Leukocyte Biol , vol.56 , Issue.5 , pp. 559-564
    • Harada, A.1    Sekido, N.2    Akahoshi, T.3
  • 61
    • 0024420563 scopus 로고
    • Neutrophil Mac-1 and MEL-14 adhesion proteins inversely regulated by chemotactic factors
    • Kishimoto TK, Jutila MA, Berg EL, et al. Neutrophil Mac-1 and MEL-14 adhesion proteins inversely regulated by chemotactic factors. Science 1989;245:1238-1245.
    • (1989) Science , vol.245 , pp. 1238-1245
    • Kishimoto, T.K.1    Jutila, M.A.2    Berg, E.L.3
  • 62
    • 0026095304 scopus 로고
    • Regulation of transendothelial neutrophil migration by endogenous interleukin-8
    • Huber R, Kunkel SL, Todd RF III, et al. Regulation of transendothelial neutrophil migration by endogenous interleukin-8. Science 1991;254:99-107.
    • (1991) Science , vol.254 , pp. 99-107
    • Huber, R.1    Kunkel, S.L.2    Todd III, R.F.3
  • 63
    • 0002137941 scopus 로고
    • Functions of neutrophils
    • Beutler E, Lichtman MA, Coller BS, et al. (eds). New York, NY, McGraw-Hill
    • Smolen JE, Boxer LA. Functions of neutrophils. In: Beutler E, Lichtman MA, Coller BS, et al. (eds). Williams Hematology, Fifth Edition. New York, NY, McGraw-Hill, 1995, pp 779-798.
    • (1995) Williams Hematology, Fifth Edition , pp. 779-798
    • Smolen, J.E.1    Boxer, L.A.2
  • 65
    • 0011330658 scopus 로고
    • Acute and chronic inflammation
    • Zembala M, Asherson GL (eds). London, UK, Academic Press
    • Wahl SM. Acute and chronic inflammation. In: Zembala M, Asherson GL (eds). Human Monocytes. London, UK, Academic Press, 1989, pp 361-371.
    • (1989) Human Monocytes , pp. 361-371
    • Wahl, S.M.1
  • 66
    • 0023556409 scopus 로고
    • Oxidants and human disease: Some new concepts
    • Halliwell B. Oxidants and human disease: some new concepts. FASEB J 1987;1:358-365.
    • (1987) FASEB J , vol.1 , pp. 358-365
    • Halliwell, B.1
  • 67
    • 0015383163 scopus 로고
    • The neurophilic leukocyte in wound repair. A study with antineutrophil serum
    • Simpson DM, Ross R. The neurophilic leukocyte in wound repair. A study with antineutrophil serum. J Clin Invest 1972;51:2009-2023.
    • (1972) J Clin Invest , vol.51 , pp. 2009-2023
    • Simpson, D.M.1    Ross, R.2
  • 68
    • 0029932695 scopus 로고    scopus 로고
    • Biologic control of injury and inflammation: Much more than too little or too late
    • Guirao X, Lowry SF. Biologic control of injury and inflammation: much more than too little or too late. World J Surg 1996;20(4):437-446.
    • (1996) World J Surg , vol.20 , Issue.4 , pp. 437-446
    • Guirao, X.1    Lowry, S.F.2
  • 69
    • 0001882728 scopus 로고
    • Complement: Chemistry and pathways
    • Gallin JI, Goldstein IM, Synderman R (eds). New York, NY, Raven Press
    • Muller-Eberhard HJ. Complement: chemistry and pathways. In: Gallin JI, Goldstein IM, Synderman R (eds). Inflammation: Basic Principles and Clinical Correlates. New York, NY, Raven Press, 1992, pp 33-61.
    • (1992) Inflammation: Basic Principles and Clinical Correlates , pp. 33-61
    • Muller-Eberhard, H.J.1
  • 72
    • 11644293748 scopus 로고
    • Prospective: A retrospective perspective on the nature of wounds
    • Barbul A, Pines E, Caldwell M, et al. (eds). New York, NY, Liss
    • Hunt TK. Prospective: a retrospective perspective on the nature of wounds. In: Barbul A, Pines E, Caldwell M, et al. (eds). Growth Factors and Other Aspects of Wound Healing. New York, NY, Liss, 1987.
    • (1987) Growth Factors and Other Aspects of Wound Healing
    • Hunt, T.K.1
  • 73
    • 0023262053 scopus 로고
    • Chemoattractant induced activation of c-fos gene expression in human monocytes
    • Ho YS, Lee WMF, Synderman R. Chemoattractant induced activation of c-fos gene expression in human monocytes. J Exp Med 1987;165:1524-1538.
    • (1987) J Exp Med , vol.165 , pp. 1524-1538
    • Ho, Y.S.1    Lee, W.M.F.2    Synderman, R.3
  • 74
    • 0019955375 scopus 로고
    • Phagocytosis of senescent neutrophils by human monocyte derived macrophages and rabbit inflammatory macrophages
    • Newman SL, Henson JE, Henson PM. Phagocytosis of senescent neutrophils by human monocyte derived macrophages and rabbit inflammatory macrophages. J Exp Med 1982;156:430-442.
    • (1982) J Exp Med , vol.156 , pp. 430-442
    • Newman, S.L.1    Henson, J.E.2    Henson, P.M.3
  • 75
    • 0019410436 scopus 로고
    • Macrophage production of fibronectin, a chemoattractant for fibroblasts
    • Tsukamoto Y, Helsel WE, Wahl SM. Macrophage production of fibronectin, a chemoattractant for fibroblasts. J Immunol 1981;127:673-678.
    • (1981) J Immunol , vol.127 , pp. 673-678
    • Tsukamoto, Y.1    Helsel, W.E.2    Wahl, S.M.3
  • 76
    • 0023665299 scopus 로고
    • Monocyte procollagenase and tissue inhibitor of metalloproteinases. Identification, characterisation and regulation of secretion
    • Campbell EJ, Cury JD, Lazarus CJ, et al. Monocyte procollagenase and tissue inhibitor of metalloproteinases. Identification, characterisation and regulation of secretion. J Biol Chem 1987;262:15862-15868.
    • (1987) J Biol Chem , vol.262 , pp. 15862-15868
    • Campbell, E.J.1    Cury, J.D.2    Lazarus, C.J.3
  • 77
    • 0029088127 scopus 로고
    • Growth factors in skin wound healing
    • Moulin V. Growth factors in skin wound healing. Eur J Cell Biol 1995;68(1):1-7.
    • (1995) Eur J Cell Biol , vol.68 , Issue.1 , pp. 1-7
    • Moulin, V.1
  • 78
    • 0030054791 scopus 로고    scopus 로고
    • The role of growth factors in wound healing
    • Greenhalgh DG. The role of growth factors in wound healing. J Trauma 1996;41(1):159-167.
    • (1996) J Trauma , vol.41 , Issue.1 , pp. 159-167
    • Greenhalgh, D.G.1
  • 79
    • 0022404365 scopus 로고
    • A significant part of macrophage derived growth factor consists of 2 forms of PDGF
    • Shimokado K, Raines EW, Madles DK, et al. A significant part of macrophage derived growth factor consists of 2 forms of PDGF. Cell 1985;43:277-286.
    • (1985) Cell , vol.43 , pp. 277-286
    • Shimokado, K.1    Raines, E.W.2    Madles, D.K.3
  • 80
    • 0010331829 scopus 로고
    • Expression and secretion of type beta TGF, by activated human macrophages
    • Assoian RK, Fleurdelys BE, Stevenson HC, et al. Expression and secretion of type beta TGF, by activated human macrophages. Proc Natl Acad Sci USA 1987;84:6020-6024.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6020-6024
    • Assoian, R.K.1    Fleurdelys, B.E.2    Stevenson, H.C.3
  • 81
    • 0023941214 scopus 로고
    • Induction of transforming growth factor alpha in activated human alveolar macrophages
    • Madtes DK, Raines EW, Sakariassen KS, et al. Induction of transforming growth factor alpha in activated human alveolar macrophages. Cell 1988;53:285-293.
    • (1988) Cell , vol.53 , pp. 285-293
    • Madtes, D.K.1    Raines, E.W.2    Sakariassen, K.S.3
  • 82
    • 0022001120 scopus 로고
    • Immunoreactive fibroblast growth factor in cells of peritoneal exudate suggest its identity with macrophage growth factor
    • Baird A, Mormede P, Bohlen P. Immunoreactive fibroblast growth factor in cells of peritoneal exudate suggest its identity with macrophage growth factor. Biochem Biophys Res Commun 1985;126:358-364.
    • (1985) Biochem Biophys Res Commun , vol.126 , pp. 358-364
    • Baird, A.1    Mormede, P.2    Bohlen, P.3
  • 83
    • 0024560643 scopus 로고
    • Human monocyte inflammatory mediator gene expression is selectively regulated by adherence substrates
    • Eierman DF, Johnson CE, Haskill JS. Human monocyte inflammatory mediator gene expression is selectively regulated by adherence substrates. J Immunol 1989;142:1970-1976.
    • (1989) J Immunol , vol.142 , pp. 1970-1976
    • Eierman, D.F.1    Johnson, C.E.2    Haskill, J.S.3
  • 84
    • 0016428338 scopus 로고
    • The role of macrophages in wound repair. A study of hydrocortisone and anti-macrophage serum
    • Leibovich SJ, Ross R. The role of macrophages in wound repair. A study of hydrocortisone and anti-macrophage serum. Am J Pathol 1975;78:71-100.
    • (1975) Am J Pathol , vol.78 , pp. 71-100
    • Leibovich, S.J.1    Ross, R.2
  • 85
    • 84937092509 scopus 로고
    • Wound healing: The role of the macrophage and other immune cells
    • DiPietro LA. Wound healing: the role of the macrophage and other immune cells. Shock 1995;4(4):233-240.
    • (1995) Shock , vol.4 , Issue.4 , pp. 233-240
    • DiPietro, L.A.1
  • 86
    • 0027818981 scopus 로고
    • Basics of cutaneous wound repair
    • Clark RAF. Basics of cutaneous wound repair. J Dermatol Surg Oncol 1993;19:693-706.
    • (1993) J Dermatol Surg Oncol , vol.19 , pp. 693-706
    • Clark, R.A.F.1
  • 88
    • 0011268320 scopus 로고
    • The fibroblast in normal repair
    • Hunt TK, Dunphy JE (eds). New York, NY, Appleton-Centruy-Crofts
    • Hunt TK, van Winkle W. The fibroblast in normal repair. In: Hunt TK, Dunphy JE (eds). Fundamentals of Wound Management. New York, NY, Appleton-Centruy-Crofts, 1979.
    • (1979) Fundamentals of Wound Management
    • Hunt, T.K.1    Van Winkle, W.2
  • 89
    • 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;54:62-79.
    • (1986) Lab Invest , vol.54 , pp. 62-79
    • Ciano, P.S.1    Colvin, R.B.2    Dvorak, A.M.3
  • 93
    • 36949072834 scopus 로고
    • Formation of the scab and the rate of epithelialization of superficial wounds in the skin of the young domestic pig
    • Winter GD. Formation of the scab and the rate of epithelialization of superficial wounds in the skin of the young domestic pig. Nature 1962;193:293-294.
    • (1962) Nature , vol.193 , pp. 293-294
    • Winter, G.D.1
  • 95
    • 0017812674 scopus 로고
    • Cytoplasmic filaments and gap junctions in epithelial cells and myofibroblasts, during wound healing
    • Gabbiani G, Chapponier C, Huttner I. Cytoplasmic filaments and gap junctions in epithelial cells and myofibroblasts, during wound healing. J Cell Biol 1978;76:561-568.
    • (1978) J Cell Biol , vol.76 , pp. 561-568
    • Gabbiani, G.1    Chapponier, C.2    Huttner, I.3
  • 96
    • 0014337880 scopus 로고
    • Human wound repair I. Epidermal regeneration
    • Odland G, Ross R. Human wound repair I. Epidermal regeneration. J Cell Biol 1968;39:135-151.
    • (1968) J Cell Biol , vol.39 , pp. 135-151
    • Odland, G.1    Ross, R.2
  • 98
    • 0002690092 scopus 로고
    • Epidermal regeneration studied in the domestic pig
    • Maibach HI, Rovee DT (eds). Chicago, IL, Year Book Medical Pub
    • Winter GD. Epidermal regeneration studied in the domestic pig. In: Maibach HI, Rovee DT (eds). Epidermal Wound Healing. Chicago, IL, Year Book Medical Pub, 1972, pp 71-112.
    • (1972) Epidermal Wound Healing , pp. 71-112
    • Winter, G.D.1
  • 99
    • 0027448632 scopus 로고
    • Reepithelialization - Human keratinocyte locomotion
    • Woodley DT, Chen JD, Kim JP, et al. Reepithelialization - human keratinocyte locomotion. Dermatologic Clinics 1993;11(4):641-646.
    • (1993) Dermatologic Clinics , vol.11 , Issue.4 , pp. 641-646
    • Woodley, D.T.1    Chen, J.D.2    Kim, J.P.3
  • 100
    • 0030061336 scopus 로고    scopus 로고
    • Influence of extracellular matrix proteins on human keratinocyte attachment, proliferation and transfer to a dermal wound model
    • Dawson RA, Goberdhan NJ, Freedlander E, et al. Influence of extracellular matrix proteins on human keratinocyte attachment, proliferation and transfer to a dermal wound model. Burns 1996;22(2):93-100.
    • (1996) Burns , vol.22 , Issue.2 , pp. 93-100
    • Dawson, R.A.1    Goberdhan, N.J.2    Freedlander, E.3
  • 101
    • 0021254214 scopus 로고
    • Human keratinocytes synthesise, secrete and deposit fibronectin in the pericellular matrix
    • Kubo M, Norris DA, Howell SE, et al. Human keratinocytes synthesise, secrete and deposit fibronectin in the pericellular matrix. J Invest Dermatol 1984;82:580-586.
    • (1984) J Invest Dermatol , vol.82 , pp. 580-586
    • Kubo, M.1    Norris, D.A.2    Howell, S.E.3
  • 102
    • 0020264236 scopus 로고
    • Fibronectin and fibrin provide a provisional matrix for epidermal cell migration during wound reepithelialisation
    • Clark RAF, Lanigan JM, Dellapelle P. Fibronectin and fibrin provide a provisional matrix for epidermal cell migration during wound reepithelialisation. 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
  • 104
    • 0023946446 scopus 로고
    • Urokinase- and tissue-type plasminogen activators in keratinocytes during wound reepithelialisation in vivo
    • Grondahl-Hansen J, Lund LR, Ralfkiaer E, et al. Urokinase- and tissue-type plasminogen activators in keratinocytes during wound reepithelialisation in vivo. J Invest Dermatol 1980;90:790-795.
    • (1980) J Invest Dermatol , vol.90 , pp. 790-795
    • Grondahl-Hansen, J.1    Lund, L.R.2    Ralfkiaer, E.3
  • 105
    • 0023766455 scopus 로고
    • Transforming growth factor beta stimulates the expression of fibronectin by human keratinocytes
    • Wikner NE, Persichitte KA, Baskin JB, et al. Transforming growth factor beta stimulates the expression of fibronectin by human keratinocytes. J Invest Dermatol 1988;91:207-212.
    • (1988) J Invest Dermatol , vol.91 , pp. 207-212
    • Wikner, N.E.1    Persichitte, K.A.2    Baskin, J.B.3
  • 106
    • 0003496745 scopus 로고
    • The role of cell-cell interaction in the regulation of endothelial cell growth
    • Clark RAF, Henson PM (eds). London, UK, Plenum Press
    • Heinmark RL, Schwartz SM. The role of cell-cell interaction in the regulation of endothelial cell growth. In: Clark RAF, Henson PM (eds). The Molecular and Cellular Biology of Wound Repair. London, UK, Plenum Press, 1988, pp 359-371.
    • (1988) The Molecular and Cellular Biology of Wound Repair , pp. 359-371
    • Heinmark, R.L.1    Schwartz, S.M.2
  • 107
    • 0005640453 scopus 로고
    • The effect of injury upon the uptake of H thymidine by guinea pig epidermis
    • Hell E, Cruickshank CND. The effect of injury upon the uptake of H thymidine by guinea pig epidermis. Exp Cell Res 1963;31:128-139.
    • (1963) Exp Cell Res , vol.31 , pp. 128-139
    • Hell, E.1    Cruickshank, C.N.D.2
  • 108
    • 0005082439 scopus 로고
    • Kinetic aspects of epidermal healing
    • Maibach HI, Rovee DT (eds). Chicago, IL, Year Book Medical Pub
    • Christopher E. Kinetic aspects of epidermal healing. In: Maibach HI, Rovee DT (eds). Epidermal Wound Healing. Chicago, IL, Year Book Medical Pub, 1972, pp 53-70.
    • (1972) Epidermal Wound Healing , pp. 53-70
    • Christopher, E.1
  • 109
    • 0028004471 scopus 로고
    • Induction of keratinocyte growth factor expression is reduced and delayed during wound heling in the genetically diabetic mouse
    • Werner S, Breeden M, Hubner G, et al. Induction of keratinocyte growth factor expression is reduced and delayed during wound heling in the genetically diabetic mouse. J Invest Dermatol 1994;103:469-475.
    • (1994) J Invest Dermatol , vol.103 , pp. 469-475
    • Werner, S.1    Breeden, M.2    Hubner, G.3
  • 110
    • 0029089228 scopus 로고
    • Effect of growth factors on cell proliferation and epithelialisation in human skin
    • Bhora FY, Dunkin BJ, Batzri S, et al. Effect of growth factors on cell proliferation and epithelialisation in human skin. J Surg Res 1995;59(2):236-244.
    • (1995) J Surg Res , vol.59 , Issue.2 , pp. 236-244
    • Bhora, F.Y.1    Dunkin, B.J.2    Batzri, S.3
  • 111
    • 0023624729 scopus 로고
    • Cell migration is essential for sustained growth of keratinocyte colonies: The roles of transforming growth factor alpha and epidermal growth factor
    • Barrandon Y, Green H. Cell migration is essential for sustained growth of keratinocyte colonies: The roles of transforming growth factor alpha and epidermal growth factor. Cell 1987;50:1131-1137.
    • (1987) Cell , vol.50 , pp. 1131-1137
    • Barrandon, Y.1    Green, H.2
  • 112
    • 0026695949 scopus 로고
    • Large induction of keratinocyte growth factor in the dermis during wound healing
    • Werner S, Peters KG, Longaker MT, et al. Large induction of keratinocyte growth factor in the dermis during wound healing. Proc Natl Acad Sci USA 1992;89:6896-6900.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6896-6900
    • Werner, S.1    Peters, K.G.2    Longaker, M.T.3
  • 113
    • 0025904265 scopus 로고
    • A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF
    • Higashiyama S, Abraham JA, Miller J, et al. A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF. Science 1991;251:936-939.
    • (1991) Science , vol.251 , pp. 936-939
    • Higashiyama, S.1    Abraham, J.A.2    Miller, J.3
  • 114
    • 0030018863 scopus 로고    scopus 로고
    • New concepts in tissue repair: Skin as an example
    • Meddahi A, Caruelle JP, Gold L, et al. New concepts in tissue repair: skin as an example. Diabetes and Metabolism 1996;22(4):274-278.
    • (1996) Diabetes and Metabolism , vol.22 , Issue.4 , pp. 274-278
    • Meddahi, A.1    Caruelle, J.P.2    Gold, L.3
  • 115
    • 0026088637 scopus 로고
    • Injury induces in vivo expression PDGF and PDGF receptor mRNAs in skin epithelial cells and PDGF mRNA in connective tissue fibroblasts
    • Antoniades HN, Galanopoulos T, Neville-Golden J, et al. Injury induces in vivo expression PDGF and PDGF receptor mRNAs in skin epithelial cells and PDGF mRNA in connective tissue fibroblasts. Proc Natl Acad Sci USA 1991;88:565-569.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 565-569
    • Antoniades, H.N.1    Galanopoulos, T.2    Neville-Golden, J.3
  • 116
    • 0343019918 scopus 로고
    • Interleukin 6 is expressed in high levels in psoriatic skin and stimulates proliferation of cultured human keratinocytes
    • Grossman RM, Krueger J, Yourish D, et al. Interleukin 6 is expressed in high levels in psoriatic skin and stimulates proliferation of cultured human keratinocytes. Proc Natl Acad Sci USA 1989;86:6367-6371.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6367-6371
    • Grossman, R.M.1    Krueger, J.2    Yourish, D.3
  • 117
    • 0025754054 scopus 로고
    • Synergistic effects of epidermal growth factor and insulin-like growth factor 1/somatemedin C on keratinocyte proliferation may be mediated by IGF 1 transmodulation of the EGF receptor
    • Krane JF, Murphy DP, Carter DM, et al. Synergistic effects of epidermal growth factor and insulin-like growth factor 1/somatemedin C on keratinocyte proliferation may be mediated by IGF 1 transmodulation of the EGF receptor. J Invest Dermatol 1991;96:419-124.
    • (1991) J Invest Dermatol , vol.96 , pp. 419-1124
    • Krane, J.F.1    Murphy, D.P.2    Carter, D.M.3
  • 118
    • 0023274128 scopus 로고
    • Induction and autoinduction of TGFα in human keratinocytes
    • Coffrey RJ, Derynck R, Wilcox JN, et al. Induction and autoinduction of TGFα in human keratinocytes. Nature 1987;328:817-820.
    • (1987) Nature , vol.328 , pp. 817-820
    • Coffrey, R.J.1    Derynck, R.2    Wilcox, J.N.3
  • 119
    • 0030307261 scopus 로고    scopus 로고
    • A comparison of the ability of intra-oral and extra-oral fibroblasts to stimulate extracellular matrix reorganisation in a model of wound contraction
    • Stephens P, Davies KJ, al-Khateeb T, et al. A comparison of the ability of intra-oral and extra-oral fibroblasts to stimulate extracellular matrix reorganisation in a model of wound contraction. J Dent Res 1996;75(6):1358-1364.
    • (1996) J Dent Res , vol.75 , Issue.6 , pp. 1358-1364
    • Stephens, P.1    Davies, K.J.2    Al-Khateeb, T.3
  • 120
    • 0025020148 scopus 로고
    • Temporal relationships of F-actin bundle formation, collagen and fibronectin matrix assembly, and fibronectin receptor expression in wound contraction
    • Welch MP, Odland GF, Clark RAF. Temporal relationships of F-actin bundle formation, collagen and fibronectin matrix assembly, and fibronectin receptor expression in wound contraction. J Cell Biol 1990;110:133-145.
    • (1990) J Cell Biol , vol.110 , pp. 133-145
    • Welch, M.P.1    Odland, G.F.2    Clark, R.A.F.3
  • 121
    • 0018297273 scopus 로고
    • The role of contractile proteins in wound healing, and fibrocontractive disease
    • Gabbiani G. The role of contractile proteins in wound healing, and fibrocontractive disease. Methods Achiev Exp Pathol 1979;9:187-206.
    • (1979) Methods Achiev Exp Pathol , vol.9 , pp. 187-206
    • Gabbiani, G.1
  • 122
    • 0018574804 scopus 로고
    • The story of myofibroblasts
    • Majno G. The story of myofibroblasts. Am Surg Pathol 1979;3:535-542.
    • (1979) Am Surg Pathol , vol.3 , pp. 535-542
    • Majno, G.1
  • 123
    • 0001502914 scopus 로고    scopus 로고
    • The role of the myofibroblast in wound healing and fibrocontractive diseases
    • Clark RAF (ed). London, UK, Plenum Press
    • Desmouliere A, Gabbiani G. The role of the myofibroblast in wound healing and fibrocontractive diseases. In: Clark RAF (ed). The Molecular and Cellular Biology of Wound Repair, Second Edition. London, UK, Plenum Press, 1996, pp 391-426.
    • (1996) The Molecular and Cellular Biology of Wound Repair, Second Edition , pp. 391-426
    • Desmouliere, A.1    Gabbiani, G.2
  • 125
    • 0000615463 scopus 로고
    • Mechanisms of cutaneous wound repair
    • Fitzpatrick TB, Eisen AZ, Wolff K, et al. (eds). New York, NY, McGraw-Hill
    • Clark RAF. Mechanisms of cutaneous wound repair. In: Fitzpatrick TB, Eisen AZ, Wolff K, et al. (eds). Dermatology in General Medicine, Fourth Edition. New York, NY, McGraw-Hill, 1993, pp 473-186.
    • (1993) Dermatology in General Medicine, Fourth Edition , pp. 473-1186
    • Clark, R.A.F.1
  • 126
    • 0023781639 scopus 로고
    • Human C5a and C5a des arg exhibit chemotactic activity for fibroblasts
    • Senior RM, Griffin GL, Perez HD, et al. Human C5a and C5a des arg exhibit chemotactic activity for fibroblasts. J Immunol 1988;141:3570-3574.
    • (1988) J Immunol , vol.141 , pp. 3570-3574
    • Senior, R.M.1    Griffin, G.L.2    Perez, H.D.3
  • 127
    • 0020625308 scopus 로고
    • Chemotactic activity of platelet alpha granule proteins for fibroblasts
    • Senior RM, Griffin GL, Huang JS, et al. Chemotactic activity of platelet alpha granule proteins for fibroblasts. J Cell Biol 1983;96:382-385.
    • (1983) J Cell Biol , vol.96 , pp. 382-385
    • Senior, R.M.1    Griffin, G.L.2    Huang, J.S.3
  • 128
    • 0025316140 scopus 로고
    • Transforming growth factor-β1-induced changes in cell migration, proliferation and angiogenesis in the chicken chorioallantoic membrane
    • Yang EY, Moses HL. Transforming growth factor-β1-induced changes in cell migration, proliferation and angiogenesis in the chicken chorioallantoic membrane. J Cell Biol 1990;111:731-741.
    • (1990) J Cell Biol , vol.111 , pp. 731-741
    • Yang, E.Y.1    Moses, H.L.2
  • 129
    • 0030039840 scopus 로고    scopus 로고
    • In vitro fibroplasia: Matrix contraction, cell growth, and collagen production of fibroblasts cultured in fibrin gels
    • Tuan TL, Song A, Chang S, et al. In vitro fibroplasia: matrix contraction, cell growth, and collagen production of fibroblasts cultured in fibrin gels. Exp Cell Res 1996;223(1):127-134.
    • (1996) Exp Cell Res , vol.223 , Issue.1 , pp. 127-134
    • Tuan, T.L.1    Song, A.2    Chang, S.3
  • 130
    • 0025998184 scopus 로고
    • Fibroblast chemotaxis induction by human recombinant interleukin-4: Identification by synthetic peptide analysis of two chemotactic domains residing in amino acid sequences 70-88 and 89-122
    • Postlethwaite AE, Seyer JM. Fibroblast chemotaxis induction by human recombinant interleukin-4: identification by synthetic peptide analysis of two chemotactic domains residing in amino acid sequences 70-88 and 89-122. J Clin Invest 1991;87:2147-2152.
    • (1991) J Clin Invest , vol.87 , pp. 2147-2152
    • Postlethwaite, A.E.1    Seyer, J.M.2
  • 131
    • 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
  • 132
    • 0021926871 scopus 로고
    • Close and focal contact adhesions of fibroblasts to a fibronectin-containing matrix
    • Lark MW, Laterra J, Culp LA. Close and focal contact adhesions of fibroblasts to a fibronectin-containing matrix. Fed Proc 1985;44:394-403.
    • (1985) Fed Proc , vol.44 , pp. 394-403
    • Lark, M.W.1    Laterra, J.2    Culp, L.A.3
  • 133
    • 0030023905 scopus 로고    scopus 로고
    • Extracellular matrix alters PDGF regulation of fibroblast integrins
    • Xu J, Clark RA. Extracellular matrix alters PDGF regulation of fibroblast integrins. J Cell Biol 1996; 132(1-2):239-249.
    • (1996) J Cell Biol , vol.132 , Issue.1-2 , pp. 239-249
    • Xu, J.1    Clark, R.A.2
  • 134
    • 0018843173 scopus 로고
    • Plasma fibronectin (opsonic glycoprotein): Its synthesis by vascular endothelial cells, and role in cardiopulmonary integrity after trauma, as related to reticuloendothelial function
    • Saba TM, Jaffe E. Plasma fibronectin (opsonic glycoprotein): Its synthesis by vascular endothelial cells, and role in cardiopulmonary integrity after trauma, as related to reticuloendothelial function. Am J Med 1980;68:577-580.
    • (1980) Am J Med , vol.68 , pp. 577-580
    • Saba, T.M.1    Jaffe, E.2
  • 135
    • 0002064476 scopus 로고
    • Glycosaminoglycans in morphogenesis
    • Hay ED (ed) New York, NY, Plenum Press
    • Toole BP. Glycosaminoglycans in morphogenesis. In: Hay ED (ed) Cell Biology of Extracellular Martix. New York, NY, Plenum Press, 1981, pp 259-294.
    • (1981) Cell Biology of Extracellular Martix , pp. 259-294
    • Toole, B.P.1
  • 136
    • 0343949321 scopus 로고
    • Induction of DNA synthesis in BALB/C 3T3 cells by serum components: Reevaluation of the commitment process
    • Pledger WJ, Stiles CD, Antonides HN, et al. Induction of DNA synthesis in BALB/C 3T3 cells by serum components: reevaluation of the commitment process. Proc Natl Acad Sci USA 1977;74:4488-4490.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 4488-4490
    • Pledger, W.J.1    Stiles, C.D.2    Antonides, H.N.3
  • 137
    • 0018286271 scopus 로고
    • PDGF and the regulation of the mammalian fibroblast cell cycle
    • Scher CD, Shepard RC, Antoniades HN, et al. PDGF and the regulation of the mammalian fibroblast cell cycle. Biochem Biophys Acta 1979;560:217-219.
    • (1979) Biochem Biophys Acta , vol.560 , pp. 217-219
    • Scher, C.D.1    Shepard, R.C.2    Antoniades, H.N.3
  • 139
    • 0018827756 scopus 로고
    • Sequential appearance of fibronectin and collagen in experimental granulation tissue
    • Kurkinen M, Vaheri A, Roberts PJ, et al. Sequential appearance of fibronectin and collagen in experimental granulation tissue. Lab Invest 1980;43:47-51.
    • (1980) Lab Invest , vol.43 , pp. 47-51
    • Kurkinen, M.1    Vaheri, A.2    Roberts, P.J.3
  • 140
    • 36849153535 scopus 로고
    • Fibronectins - Adhesive glycoproteins of cell surface and blood
    • Yamada K, Olden K. Fibronectins - adhesive glycoproteins of cell surface and blood. Nature 1978;275:179-184.
    • (1978) Nature , vol.275 , pp. 179-184
    • Yamada, K.1    Olden, K.2
  • 141
    • 0023203710 scopus 로고
    • Gamma interferon inhibits collagen synthesis in vivo in the mouse
    • Granstein RD, Murphy GF, Margolis RJ, et al. Gamma interferon inhibits collagen synthesis in vivo in the mouse. J Clin Invest 1987;79:1254-1258.
    • (1987) J Clin Invest , vol.79 , pp. 1254-1258
    • Granstein, R.D.1    Murphy, G.F.2    Margolis, R.J.3
  • 142
    • 0028929288 scopus 로고
    • Collagen matrices attenuate the collagen synthetic response of cultured fibroblasts to TGFß
    • Clark RAF, Nielsen LD, Welch MP, et al. Collagen matrices attenuate the collagen synthetic response of cultured fibroblasts to TGFß. J Cell Sci 1995;108:1251-1261.
    • (1995) J Cell Sci , vol.108 , pp. 1251-1261
    • Clark, R.A.F.1    Nielsen, L.D.2    Welch, M.P.3
  • 143
    • 0002311696 scopus 로고
    • Contraction
    • Peacock EE (ed). Philadelphia, PA, WB Saunders
    • Peacock EE. Contraction. In: Peacock EE (ed). Wound Repair, Third Edition. Philadelphia, PA, WB Saunders, 1984, 39-55.
    • (1984) Wound Repair, Third Edition , pp. 39-55
    • Peacock, E.E.1
  • 144
  • 146
    • 0015225464 scopus 로고
    • Presence of modified fibroblasts in granulation tissue, and their possible role in wound contraction
    • Gabbiani G, Ryan GB, Majno G. Presence of modified fibroblasts in granulation tissue, and their possible role in wound contraction. Experientia 1971;27:549-551.
    • (1971) Experientia , vol.27 , pp. 549-551
    • Gabbiani, G.1    Ryan, G.B.2    Majno, G.3
  • 147
    • 0025078397 scopus 로고
    • Cell location forces versus cell contraction forces, for collagen lattice contraction. An in vitro model for wound contraction
    • Ehrlich HP, Rajaratnam JBM. Cell location forces versus cell contraction forces, for collagen lattice contraction. An in vitro model for wound contraction. Tissue and Cell 1990;22:407-411.
    • (1990) Tissue and Cell , vol.22 , pp. 407-411
    • Ehrlich, H.P.1    Rajaratnam, J.B.M.2
  • 148
    • 0018344535 scopus 로고
    • The fibronexus; a transmembrane association of fibronectin-containing fibres and bundles of 5 run filaments in hamster and human fibroblasts
    • Singer II. The fibronexus; a transmembrane association of fibronectin-containing fibres and bundles of 5 run filaments in hamster and human fibroblasts. Cell 1979;16:675-685.
    • (1979) Cell , vol.16 , pp. 675-685
    • Singer, I.I.1
  • 149
    • 0026006498 scopus 로고
    • Integrin α2ß1 (VLA-2) mediates reorganisation and contraction of collagen matrices by human cells
    • Schiro JA, Chan BMC, Roswit WR, et al. Integrin α2ß1 (VLA-2) mediates reorganisation and contraction of collagen matrices by human cells. Cell 1991;67:403-410.
    • (1991) Cell , vol.67 , pp. 403-410
    • Schiro, J.A.1    Chan, B.M.C.2    Roswit, W.R.3
  • 150
    • 0019129846 scopus 로고
    • Contraction and the control of contraction
    • Rudolph R. Contraction and the control of contraction. World J Surg 1980;4:279-287.
    • (1980) World J Surg , vol.4 , pp. 279-287
    • Rudolph, R.1
  • 151
    • 0020067094 scopus 로고
    • Connective tissue morphogenesis by fibroblasts traction I; tissue culture observations
    • Stopak D, Harris AK. Connective tissue morphogenesis by fibroblasts traction I; tissue culture observations. Developmental Biology 1982;90:383-387.
    • (1982) Developmental Biology , vol.90 , pp. 383-387
    • Stopak, D.1    Harris, A.K.2
  • 152
    • 0023902610 scopus 로고
    • Wound closure: Evidence of cooperation between fibroblasts and collagen matrix
    • Ehrlich HP. Wound closure: evidence of cooperation between fibroblasts and collagen matrix. Eye 1988;2:149-157.
    • (1988) Eye , vol.2 , pp. 149-157
    • Ehrlich, H.P.1
  • 153
    • 0025306468 scopus 로고
    • α-smooth muscle actin is transiently expressed by myofibroblasts during experimental wound healing
    • Darby I, Skalli O, Gabbiani G. α-smooth muscle actin is transiently expressed by myofibroblasts during experimental wound healing. Lab Invest 1990;63:21-29.
    • (1990) Lab Invest , vol.63 , pp. 21-29
    • Darby, I.1    Skalli, O.2    Gabbiani, G.3
  • 154
    • 0023795580 scopus 로고
    • Wound macrophages express TGFα and other growth factors in vivo: Analysis by mRNA phenotyping
    • Rappolee DA, Mark D, Banda MJ, et al. Wound macrophages express TGFα and other growth factors in vivo: Analysis by mRNA phenotyping. Science 1988;241:708-712.
    • (1988) Science , vol.241 , pp. 708-712
    • Rappolee, D.A.1    Mark, D.2    Banda, M.J.3
  • 155
    • 0024450186 scopus 로고
    • Platelet isoforms of platelet-derived growth factor stimulate fibroblasts to contract collagen matrices
    • Clark RAF, Folkvord JM, Hart CE, et al. Platelet isoforms of platelet-derived growth factor stimulate fibroblasts to contract collagen matrices. J Clin Invest 1989;84:1036-1040.
    • (1989) J Clin Invest , vol.84 , pp. 1036-1040
    • Clark, R.A.F.1    Folkvord, J.M.2    Hart, C.E.3
  • 156
    • 0000233823 scopus 로고
    • Repair and regenerative responses
    • McGee J, Isaacson PG, Wright NA, et al. (eds). Oxford, UK, Oxford Uniersity Press
    • Alison MR. Repair and regenerative responses. In: McGee J, Isaacson PG, Wright NA, et al. (eds). Oxford Textbook of Pathology; Volume 1 Principles of Pathology. Oxford, UK, Oxford Uniersity Press, 1992, pp 365-388.
    • (1992) Oxford Textbook of Pathology; Volume 1 Principles of Pathology , vol.1 , pp. 365-388
    • Alison, M.R.1
  • 157
    • 0023025302 scopus 로고
    • Angiogenesis in reproductive tissues
    • Findlay JK. Angiogenesis in reproductive tissues. J Endocr 1986;111:357-366.
    • (1986) J Endocr , vol.111 , pp. 357-366
    • Findlay, J.K.1
  • 158
    • 0024504371 scopus 로고
    • In vitro angiogenesis on the human amniotic membrane: Requirement for bFGF-induced proteinases
    • Magnati P, Tsuboi R, Robbins E, et al. In vitro angiogenesis on the human amniotic membrane: requirement for bFGF-induced proteinases. J Cell Biol 1989;108:671-682.
    • (1989) J Cell Biol , vol.108 , pp. 671-682
    • Magnati, P.1    Tsuboi, R.2    Robbins, E.3
  • 159
    • 0019394536 scopus 로고
    • Proteoglycans in the microvasculature II. Histochemical localization in proliferating capillaries of the rabbt cornea
    • Ausprunk DK, Boudreau CL, Nelson DA. Proteoglycans in the microvasculature II. Histochemical localization in proliferating capillaries of the rabbt cornea. Am J Pathol 1981;103:367-375.
    • (1981) Am J Pathol , vol.103 , pp. 367-375
    • Ausprunk, D.K.1    Boudreau, C.L.2    Nelson, D.A.3
  • 160
    • 0020631281 scopus 로고
    • Basement membrane collagen: Degradation by migrating endothelial cells
    • Kalebic T, Garbisa S, Glaser B, et al. Basement membrane collagen: degradation by migrating endothelial cells. Science 1983;221:281-283.
    • (1983) Science , vol.221 , pp. 281-283
    • Kalebic, T.1    Garbisa, S.2    Glaser, B.3
  • 162
    • 0027319870 scopus 로고
    • Pericyte physiology
    • Shepro D, Morel NM. Pericyte physiology. FASEB J 1993;7(11):1031-1038.
    • (1993) FASEB J , vol.7 , Issue.11 , pp. 1031-1038
    • Shepro, D.1    Morel, N.M.2
  • 163
    • 11644264654 scopus 로고    scopus 로고
    • Tissue repair
    • Kitchen S, Bazin S (eds). London, UK, W.B. Saunders
    • Kitchen S, Young SR. Tissue repair. In: Kitchen S, Bazin S (eds). Clayton's Electrotherapy 10E. London, UK, W.B. Saunders, 1996 pp 47-60.
    • (1996) Clayton's Electrotherapy 10E , pp. 47-60
    • Kitchen, S.1    Young, S.R.2
  • 164
    • 0028851160 scopus 로고
    • Apoptosis mediates the decrease in cellularity during the transition between granulation tissue and scar
    • Desmouliere A, Redard M, Darby I, et al. Apoptosis mediates the decrease in cellularity during the transition between granulation tissue and scar. Am J Path 1995;146(1):56-66.
    • (1995) Am J Path , vol.146 , Issue.1 , pp. 56-66
    • Desmouliere, A.1    Redard, M.2    Darby, I.3
  • 165
    • 0020331685 scopus 로고
    • Angiogenesis: Initiation and control
    • Folkman J. Angiogenesis: initiation and control. Ann NY Acad Sci 1982;401:212-227.
    • (1982) Ann NY Acad Sci , vol.401 , pp. 212-227
    • Folkman, J.1
  • 166
  • 167
    • 0027097806 scopus 로고
    • Interleukin 8 as a macrophage-derived mediator of angiogenesis
    • Koch AE, Polverini PJ, Kunkel SL, et al. Interleukin 8 as a macrophage-derived mediator of angiogenesis. Science 1992;258:1798-1801.
    • (1992) Science , vol.258 , pp. 1798-1801
    • Koch, A.E.1    Polverini, P.J.2    Kunkel, S.L.3
  • 168
    • 0037486459 scopus 로고
    • Studies on the mechanism of retinal neovascularization. Role of lactic acid
    • Imre G. Studies on the mechanism of retinal neovascularization. Role of lactic acid. Br J Ophthalmol 1964;48:75-82.
    • (1964) Br J Ophthalmol , vol.48 , pp. 75-82
    • Imre, G.1
  • 169
    • 0014443539 scopus 로고
    • Stimulation of neovascularization of the cornea by biogenie amines
    • Zauberman H, Michaelson IC, Bergmann F, et al. Stimulation of neovascularization of the cornea by biogenie amines. Exp Eye Res 1969;8:77-83.
    • (1969) Exp Eye Res , vol.8 , pp. 77-83
    • Zauberman, H.1    Michaelson, I.C.2    Bergmann, F.3
  • 170
    • 0020557197 scopus 로고
    • Oxygen tension regulates the expression of angiogenesis factor by macrophages
    • Knighton DR, Hunt TK, Schevenstuhl, et al. Oxygen tension regulates the expression of angiogenesis factor by macrophages. Science 1983;221:1283-1285.
    • (1983) Science , vol.221 , pp. 1283-1285
    • Knighton, D.R.1    Hunt, T.K.2    Schevenstuhl3
  • 171
    • 0024563134 scopus 로고
    • Identification of angiogenic activity and the cloning and expression of PD-ECGF
    • Ishikawa F, Miyazono K, Hellman U, et al. Identification of angiogenic activity and the cloning and expression of PD-ECGF. Nature 1989;338:557-562.
    • (1989) Nature , vol.338 , pp. 557-562
    • Ishikawa, F.1    Miyazono, K.2    Hellman, U.3
  • 172
    • 0024212247 scopus 로고
    • Transforming growth factor beta is chemotactic for human monocytes and induces their expression of angiogenic activity
    • Weisman DM, Polverini PJ, Kamp DW. Transforming growth factor beta is chemotactic for human monocytes and induces their expression of angiogenic activity. Biochem Biophys Res Commun 1988;157:793-800.
    • (1988) Biochem Biophys Res Commun , vol.157 , pp. 793-800
    • Weisman, D.M.1    Polverini, P.J.2    Kamp, D.W.3
  • 173
    • 0028355888 scopus 로고
    • PDGF-BB modulates endothelial proliferation and angiogenesis in vitro via PDGF ß receptors
    • Battegay EF, Rupp J, Iruela-Arispe L, et al. PDGF-BB modulates endothelial proliferation and angiogenesis in vitro via PDGF ß receptors. J Cell Biol 1994;125:917-928.
    • (1994) J Cell Biol , vol.125 , pp. 917-928
    • Battegay, E.F.1    Rupp, J.2    Iruela-Arispe, L.3
  • 174
    • 0018936563 scopus 로고
    • Mast cell heparin stimulates migration of capillary endothelial cells in vitro
    • Azizkhan RG, Azizkhan JC, Zetter BR, et al. Mast cell heparin stimulates migration of capillary endothelial cells in vitro. J Exp Med 1980;152:931-944.
    • (1980) J Exp Med , vol.152 , pp. 931-944
    • Azizkhan, R.G.1    Azizkhan, J.C.2    Zetter, B.R.3
  • 175
    • 0018102645 scopus 로고
    • Identification, localisation and the role of fibronectin in cultured bovine endothelial cells
    • Birdwell CR, Gospodarowicz D, Nicholson GL. Identification, localisation and the role of fibronectin in cultured bovine endothelial cells. Proc Natl Acad Sci USA 1978;75:3273-3277.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 3273-3277
    • Birdwell, C.R.1    Gospodarowicz, D.2    Nicholson, G.L.3
  • 176
    • 0020044766 scopus 로고
    • Aortic endothelial cell migration I. Matrix requirements and composition
    • Madri JA, Stenn KS. Aortic endothelial cell migration I. Matrix requirements and composition. Am J Path 1982;106:180-186.
    • (1982) Am J Path , vol.106 , pp. 180-186
    • Madri, J.A.1    Stenn, K.S.2
  • 177
    • 0023585264 scopus 로고
    • Inhibition of capillary endothelial cell growth by pericytes and smooth muscle cells
    • Orlidge A, D'Amore PA. Inhibition of capillary endothelial cell growth by pericytes and smooth muscle cells. J Cell Biol 1987;105:1455-1462.
    • (1987) J Cell Biol , vol.105 , pp. 1455-1462
    • Orlidge, A.1    D'Amore, P.A.2
  • 178
    • 0030069231 scopus 로고    scopus 로고
    • Control of apoptosis by the cellular ATP level
    • Richter C, Schweizer M, Cossarizza A, et al. Control of apoptosis by the cellular ATP level. FEBS Letters 1996;378(2):107-110.
    • (1996) FEBS Letters , vol.378 , Issue.2 , pp. 107-110
    • Richter, C.1    Schweizer, M.2    Cossarizza, A.3
  • 179
    • 0029998678 scopus 로고    scopus 로고
    • Epithelial injury induces keratocyte apoptosis: Hypothesised role for the interleukin-1 system in the modulation of corneal tissue organisation and wound healing
    • Wilson SE, He YG, Weng J, et al. Epithelial injury induces keratocyte apoptosis: hypothesised role for the interleukin-1 system in the modulation of corneal tissue organisation and wound healing. Exp Eye Res 1996;62(4):325-327.
    • (1996) Exp Eye Res , vol.62 , Issue.4 , pp. 325-327
    • Wilson, S.E.1    He, Y.G.2    Weng, J.3
  • 180
    • 0029959882 scopus 로고    scopus 로고
    • Apoptosis: Molecular regulation of cell death
    • Hale AJ, Smith CA, Sutherland LC, et al. Apoptosis: molecular regulation of cell death. Eur J Biochem 1996;236(1):1-26.
    • (1996) Eur J Biochem , vol.236 , Issue.1 , pp. 1-26
    • Hale, A.J.1    Smith, C.A.2    Sutherland, L.C.3
  • 181
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORTl/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • Boldin MP, Goncharov TM, Goltsev YV, et al. Involvement of MACH, a novel MORTl/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell 1996;85:803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3
  • 182
    • 0028306029 scopus 로고
    • Macrophage recruitment during limb development and wound healing in the embryonic and foetal mouse
    • Hopkinson-Woolley J, Hughes D, Gordon S, et al. Macrophage recruitment during limb development and wound healing in the embryonic and foetal mouse. J Cell Sci 1994;107(5):1159-1167.
    • (1994) J Cell Sci , vol.107 , Issue.5 , pp. 1159-1167
    • Hopkinson-Woolley, J.1    Hughes, D.2    Gordon, S.3
  • 183
    • 0021241967 scopus 로고
    • Scar formation: Physiology and pathological states
    • Chvapil M, Koopman CF. Scar formation: physiology and pathological states. Otolaryngol Clin N Am 1984;17:265-272.
    • (1984) Otolaryngol Clin N Am , vol.17 , pp. 265-272
    • Chvapil, M.1    Koopman, C.F.2
  • 186
    • 0024358264 scopus 로고
    • Skin regenerated from cultured epithelial autographs on full-thickness burn wounds from 6 days to 5 years after grafting. A light electron microscope and immunohistochemical study
    • Compton CC, Gill JM, Bradford DA, et al. Skin regenerated from cultured epithelial autographs on full-thickness burn wounds from 6 days to 5 years after grafting. A light electron microscope and immunohistochemical study. Lab Invest 1989;60:600-612.
    • (1989) Lab Invest , vol.60 , pp. 600-612
    • Compton, C.C.1    Gill, J.M.2    Bradford, D.A.3
  • 187
    • 0016750248 scopus 로고
    • Characterization of the collagen of human hypertrophic and normal scars
    • Bailey AJ, Bazin S, Sims TJ, et al. Characterization of the collagen of human hypertrophic and normal scars. Biochem Biophys Acta 1975;405:412-421.
    • (1975) Biochem Biophys Acta , vol.405 , pp. 412-421
    • Bailey, A.J.1    Bazin, S.2    Sims, T.J.3
  • 188
    • 0023656288 scopus 로고
    • Epidermal growth factor increases collagen production in granulation tissue by stimulation of fibroblast proliferation and not by activation of procollagen genes
    • Laato M, Kahari VM, Niniikoski J, et al. Epidermal growth factor increases collagen production in granulation tissue by stimulation of fibroblast proliferation and not by activation of procollagen genes. Biochem 1987;247:385-388.
    • (1987) Biochem , vol.247 , pp. 385-388
    • Laato, M.1    Kahari, V.M.2    Niniikoski, J.3
  • 189
    • 0029009330 scopus 로고
    • Transforming growth factor beta 1, extracellular matrix, and inflammatory cells in wound repair using a closed duodenal loop pancreatitis model rat
    • Kimura Y, Torimura T, Ueno T, et al. Transforming growth factor beta 1, extracellular matrix, and inflammatory cells in wound repair using a closed duodenal loop pancreatitis model rat. Immunohistochemical Study 1995;30(7):707-714.
    • (1995) Immunohistochemical Study , vol.30 , Issue.7 , pp. 707-714
    • Kimura, Y.1    Torimura, T.2    Ueno, T.3
  • 190
    • 0022168434 scopus 로고
    • Molecular biology of fibronectin
    • Hynes R. Molecular biology of fibronectin. Annu Rev Cell Biol 1985;1:67-71.
    • (1985) Annu Rev Cell Biol , vol.1 , pp. 67-71
    • Hynes, R.1
  • 191
    • 0000280766 scopus 로고
    • Fibronectin and other cell interactive glycoproteins
    • Hay ED (ed). New York, NY, Plenum Press
    • Yamada KM. Fibronectin and other cell interactive glycoproteins. In: Hay ED (ed). Cell Biology of Extracellular Matrix, Second Edition. New York, NY, Plenum Press, 1991, pp 111-139.
    • (1991) Cell Biology of Extracellular Matrix, Second Edition , pp. 111-139
    • Yamada, K.M.1
  • 192
    • 0027715980 scopus 로고
    • Macrophages and fibroblasts express "embryonic" fibronectins during cutaneous wound healing
    • Brown LF, Dubin D, Lavinge L, et al. Macrophages and fibroblasts express "embryonic" fibronectins during cutaneous wound healing. Am J Pathol 1993;142:793-801.
    • (1993) Am J Pathol , vol.142 , pp. 793-801
    • Brown, L.F.1    Dubin, D.2    Lavinge, L.3
  • 193
    • 0029947854 scopus 로고    scopus 로고
    • Changes in cell spreading and cytoskeletal organisation are induced by adhesion to a fibronectin-fibrin matrix
    • Corbett SA, Wilson CL, Schwarzbauer JE. Changes in cell spreading and cytoskeletal organisation are induced by adhesion to a fibronectin-fibrin matrix. Blood 1996;88(1):158-166.
    • (1996) Blood , vol.88 , Issue.1 , pp. 158-166
    • Corbett, S.A.1    Wilson, C.L.2    Schwarzbauer, J.E.3
  • 194
    • 0018838451 scopus 로고
    • Fibroblast adhesion to fibrinogen and fibrin substrata: Requirement for cold-insolule globulin (plasma fibronectin)
    • Grinnell F, Feld M, Minter D. Fibroblast adhesion to fibrinogen and fibrin substrata: requirement for cold-insolule globulin (plasma fibronectin). Cell 1980;19:517-525.
    • (1980) Cell , vol.19 , pp. 517-525
    • Grinnell, F.1    Feld, M.2    Minter, D.3
  • 195
    • 0023900180 scopus 로고
    • Fibronectin receptors of phagocytes. Characterisation of the arg-gly-asp binding proteins of human monocytes and polymorphonuclear leucocytes
    • Brown EJ, Goodwin JL. Fibronectin receptors of phagocytes. Characterisation of the arg-gly-asp binding proteins of human monocytes and polymorphonuclear leucocytes. J Exp Med 1988;167:777-793.
    • (1988) J Exp Med , vol.167 , pp. 777-793
    • Brown, E.J.1    Goodwin, J.L.2
  • 196
    • 0023851909 scopus 로고
    • Potential roles of fibronectin in cutaneous wound repair
    • Clark RAF. Potential roles of fibronectin in cutaneous wound repair. Arch Dermatol 1988;124:201-206.
    • (1988) Arch Dermatol , vol.124 , pp. 201-206
    • Clark, R.A.F.1
  • 197
    • 0019876460 scopus 로고
    • Susceptibility of soluble and matrix fibronectins to degradation by tissue proteases, mast cell chymase and cathepepsin
    • Vartio T, Seppa H, Vaheri A. Susceptibility of soluble and matrix fibronectins to degradation by tissue proteases, mast cell chymase and cathepepsin. J Biol Chem 1981;256:471-177.
    • (1981) J Biol Chem , vol.256 , pp. 471-1177
    • Vartio, T.1    Seppa, H.2    Vaheri, A.3
  • 199
    • 0026492073 scopus 로고
    • Cytokine regulation of human lung fibroblast hyaluronan (hyaluronic acid) production: Evidence for cytokine-regulated hyaluronan (hyaluronic acid) degradation and human lung fibroblast-derived hyaluronidase
    • Sampson PM, Rochester CL, Freundlich B, et al. Cytokine regulation of human lung fibroblast hyaluronan (hyaluronic acid) production: evidence for cytokine-regulated hyaluronan (hyaluronic acid) degradation and human lung fibroblast-derived hyaluronidase. J Clin Invest 1992;90:1492-1503.
    • (1992) J Clin Invest , vol.90 , pp. 1492-1503
    • Sampson, P.M.1    Rochester, C.L.2    Freundlich, B.3
  • 200
    • 0041346979 scopus 로고
    • The basic dye-uptake and the presence of growth inhibiting substance in the healing tissue of skin wounds
    • Balazs A, Holmgren HJ. The basic dye-uptake and the presence of growth inhibiting substance in the healing tissue of skin wounds. Exp Cell Res 1950;1:206-216.
    • (1950) Exp Cell Res , vol.1 , pp. 206-216
    • Balazs, A.1    Holmgren, H.J.2
  • 201
    • 0014051831 scopus 로고
    • Rate of chondroitin sulphate formation in wound healing
    • Bentley JP. Rate of chondroitin sulphate formation in wound healing. Ann Surg 1967;165:186-191.
    • (1967) Ann Surg , vol.165 , pp. 186-191
    • Bentley, J.P.1
  • 202
    • 0015423469 scopus 로고
    • Hyaluronate turnover during chondrogenesis in the developing chick limb and axial skeleton
    • Toole BP. Hyaluronate turnover during chondrogenesis in the developing chick limb and axial skeleton. Dev Biol 1972;29:321-329.
    • (1972) Dev Biol , vol.29 , pp. 321-329
    • Toole, B.P.1
  • 204
    • 0018561566 scopus 로고
    • Fibronectin and proteoglycans as determinants of cell-substratum adhesion
    • Culp LA, Murray BA, Rollins BJ. Fibronectin and proteoglycans as determinants of cell-substratum adhesion. J Supramol Struct 1979;11:401-427.
    • (1979) J Supramol Struct , vol.11 , pp. 401-427
    • Culp, L.A.1    Murray, B.A.2    Rollins, B.J.3
  • 205
    • 0026446637 scopus 로고
    • CD44: The hyaluronan receptor
    • Underhill C. CD44: the hyaluronan receptor. J Cell Sci 1992;103:293-298.
    • (1992) J Cell Sci , vol.103 , pp. 293-298
    • Underhill, C.1
  • 206
    • 0026559653 scopus 로고
    • Hyaluronan and cell locomotion
    • Turley EA. Hyaluronan and cell locomotion. Cancer Metastasis Rev 1992;11:21-30.
    • (1992) Cancer Metastasis Rev , vol.11 , pp. 21-30
    • Turley, E.A.1
  • 207
    • 0028966693 scopus 로고
    • Hyaluronic acid receptors
    • Ruoslahti E, Engvall E (eds). San Diego, CA, Academic Press
    • Stamenkovic I, Aruffo A. Hyaluronic acid receptors. In: Ruoslahti E, Engvall E (eds). Methods in Enzymology. San Diego, CA, Academic Press, 1994, pp 195-218.
    • (1994) Methods in Enzymology , pp. 195-218
    • Stamenkovic, I.1    Aruffo, A.2
  • 208
    • 0028097742 scopus 로고
    • Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44 and link protein
    • Yang B. Yang B, Savani RC, et al. Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44 and link protein. EMBO J 1994;13:286-296.
    • (1994) EMBO J , vol.13 , pp. 286-296
    • Yang, B.1    Yang, B.2    Savani, R.C.3
  • 209
    • 0026670584 scopus 로고
    • CD44H regulates tumour cell migration on hyaluronate-coated substrate
    • Thomas L, Byers HR, Vink J, et al. CD44H regulates tumour cell migration on hyaluronate-coated substrate. J Cell Biol 1992;118:971-977.
    • (1992) J Cell Biol , vol.118 , pp. 971-977
    • Thomas, L.1    Byers, H.R.2    Vink, J.3
  • 210
    • 0017683621 scopus 로고
    • Glycosaminoglycan synthesis by cultured human skin fibroblasts after transformation with simian virus 40
    • Hopwood JJ, Dorfman A. Glycosaminoglycan synthesis by cultured human skin fibroblasts after transformation with simian virus 40. J Bio Chem 1977;252:4777-4785.
    • (1977) J Bio Chem , vol.252 , pp. 4777-4785
    • Hopwood, J.J.1    Dorfman, A.2
  • 211
    • 0016725047 scopus 로고
    • Induction of hyaluronic acid synthetase activity in rat fibroblasts by medium change of confluent cultures
    • Tomida M, Koyama H, Ono T. Induction of hyaluronic acid synthetase activity in rat fibroblasts by medium change of confluent cultures. J Cell Physiol 1975;86:121-130.
    • (1975) J Cell Physiol , vol.86 , pp. 121-130
    • Tomida, M.1    Koyama, H.2    Ono, T.3
  • 212
    • 0016661476 scopus 로고
    • Increased hyaluronic acid production on stimulation of DNA synthesis in chick embryo fibroblasts
    • Moscatelli D, Rubin H. Increased hyaluronic acid production on stimulation of DNA synthesis in chick embryo fibroblasts. Nature 1975;254:65-66.
    • (1975) Nature , vol.254 , pp. 65-66
    • Moscatelli, D.1    Rubin, H.2
  • 213
    • 0017105080 scopus 로고
    • Enhanced synthesis and extracellular accumulation of hyaluronic acid during stimulation of quiescent human fibroblasts by mouse epidermal growth factor
    • Lembach KJ. Enhanced synthesis and extracellular accumulation of hyaluronic acid during stimulation of quiescent human fibroblasts by mouse epidermal growth factor. J Cell Physiol 1976;89:277-288.
    • (1976) J Cell Physiol , vol.89 , pp. 277-288
    • Lembach, K.J.1
  • 214
    • 0024516433 scopus 로고
    • The hyaluronate receptor is preferentially expressed on proliferating epithelial cells
    • Alho AM, Underhill CM. The hyaluronate receptor is preferentially expressed on proliferating epithelial cells. J Cell Biol 1989;108:1557-1566.
    • (1989) J Cell Biol , vol.108 , pp. 1557-1566
    • Alho, A.M.1    Underhill, C.M.2
  • 215
    • 0023371532 scopus 로고
    • Hyaluronidase activity of rabbit skin wound granulation tissue fibroblasts
    • Ruggiero SL, Bertolami CN, Bronson RE, et al. Hyaluronidase activity of rabbit skin wound granulation tissue fibroblasts. J Dent Res 1987;66:1283-1287.
    • (1987) J Dent Res , vol.66 , pp. 1283-1287
    • Ruggiero, S.L.1    Bertolami, C.N.2    Bronson, R.E.3
  • 217
    • 0024007172 scopus 로고
    • Interleukin 1 induced changes in extracellular glycosaminoglycan composition of cutaneous scar-derived fibroblasts in culture
    • Bronson RE, Argenta JG, Bertolami N. Interleukin 1 induced changes in extracellular glycosaminoglycan composition of cutaneous scar-derived fibroblasts in culture. Coll Rel Res 1988;8:199-208.
    • (1988) Coll Rel Res , vol.8 , pp. 199-208
    • Bronson, R.E.1    Argenta, J.G.2    Bertolami, N.3
  • 219
    • 0019957222 scopus 로고
    • Platelet-derived growth factor: High yield purification and evidence for multiple forms
    • Raines EW, Ross R. Platelet-derived growth factor: high yield purification and evidence for multiple forms. J Biol Chem 1985;257:5154-5157.
    • (1985) J Biol Chem , vol.257 , pp. 5154-5157
    • Raines, E.W.1    Ross, R.2
  • 220
    • 0001466363 scopus 로고
    • Proteoglycan-fibrillar collagen interactions in tissues: Dermatan sulphate proteoglycan as a tissue organiser
    • London, UK, Portland Press
    • Scott JE. Proteoglycan-fibrillar collagen interactions in tissues: dermatan sulphate proteoglycan as a tissue organiser. Dermatan Sulphate Proteoglycans: Chemistry, Biology, Chemical Pathology. London, UK, Portland Press, 1993, pp 165-181.
    • (1993) Dermatan Sulphate Proteoglycans: Chemistry, Biology, Chemical Pathology , pp. 165-181
    • Scott, J.E.1
  • 221
    • 0013573321 scopus 로고
    • Platelet-derived growth factor and cell proliferation
    • Sara VR (ed). New York, NY, Raven Press
    • Ross RR, Raines EW. Platelet-derived growth factor and cell proliferation. In: Sara VR (ed). Growth Factors: From Genes to Clinical Application. New York, NY, Raven Press, 1990, pp 193-199.
    • (1990) Growth Factors: From Genes to Clinical Application , pp. 193-199
    • Ross, R.R.1    Raines, E.W.2
  • 222
    • 0023691850 scopus 로고
    • Characterisation and N-terminal sequence of human platelet proteoglycan
    • Perin JP, Bonnet F, Mailet P, et al. Characterisation and N-terminal sequence of human platelet proteoglycan. Biochem J 1988;255:1007-1013.
    • (1988) Biochem J , vol.255 , pp. 1007-1013
    • Perin, J.P.1    Bonnet, F.2    Mailet, P.3
  • 223
    • 0016369349 scopus 로고
    • Collagen and mucopolysaccharides in the hypertrophic scar
    • Kischer CW, Shetlar MR. Collagen and mucopolysaccharides in the hypertrophic scar. Connect Tissue Res 1974;2:205-213.
    • (1974) Connect Tissue Res , vol.2 , pp. 205-213
    • Kischer, C.W.1    Shetlar, M.R.2
  • 224
    • 0015293774 scopus 로고
    • The hypertrophic scar. Hexosamine containing components of burn scars
    • Shetlar MR, Shetlar CL, Chien SF, et al. The hypertrophic scar. Hexosamine containing components of burn scars. Proc Soc Exp Biol Med 1972;139:544-547.
    • (1972) Proc Soc Exp Biol Med , vol.139 , pp. 544-547
    • Shetlar, M.R.1    Shetlar, C.L.2    Chien, S.F.3
  • 225
    • 0017171182 scopus 로고
    • Density dependent changes in the amount of sulphated glycosaminoglycans associated with mouse 3T3 cells
    • Underhill CB, Keller JM. Density dependent changes in the amount of sulphated glycosaminoglycans associated with mouse 3T3 cells. J Cell Physiol 1976;89:53-63.
    • (1976) J Cell Physiol , vol.89 , pp. 53-63
    • Underhill, C.B.1    Keller, J.M.2
  • 226
    • 0015451872 scopus 로고
    • Cell-cycle-dependent desquamation of heparan sulphate from the cell surface
    • Kraemer PM, Tobey RA. Cell-cycle-dependent desquamation of heparan sulphate from the cell surface. J Cell Biol 1972;55:713-717.
    • (1972) J Cell Biol , vol.55 , pp. 713-717
    • Kraemer, P.M.1    Tobey, R.A.2
  • 227
    • 0028707911 scopus 로고
    • Non-fibrillar collagens
    • Ruoslahti E, Engvall E (eds). San Diego, CA, Academic Press
    • Fukai N, Apte SS, Olsen BR. Non-fibrillar collagens. In: Ruoslahti E, Engvall E (eds). Extracellular Matrix Components. San Diego, CA, Academic Press, 1994, pp 3-28.
    • (1994) Extracellular Matrix Components , pp. 3-28
    • Fukai, N.1    Apte, S.S.2    Olsen, B.R.3
  • 229
    • 0012017284 scopus 로고
    • The extracellular matrix in wound healing: Collagen in wound healing
    • Hopkinson I. The extracellular matrix in wound healing: collagen in wound healing. WOUNDS 1992;4(4):124-132.
    • (1992) WOUNDS , vol.4 , Issue.4 , pp. 124-132
    • Hopkinson, I.1
  • 230
    • 0021062269 scopus 로고
    • The effect of occlusive dressings on collagen synthesis and reepithelialisation in superficial wounds
    • Alvarez OM. The effect of occlusive dressings on collagen synthesis and reepithelialisation in superficial wounds. J Surg Res 1983;35:142-145.
    • (1983) J Surg Res , vol.35 , pp. 142-145
    • Alvarez, O.M.1
  • 231
    • 0018134564 scopus 로고
    • Collagen types in early phases of wound healing in children
    • Gay S, Viljanto J, Raekallio J, et al. Collagen types in early phases of wound healing in children. Acta Chir Scand 1978;144:205-207.
    • (1978) Acta Chir Scand , vol.144 , pp. 205-207
    • Gay, S.1    Viljanto, J.2    Raekallio, J.3
  • 232
    • 0018758569 scopus 로고
    • Quantitation of the collagen types I and III during wound healing in the rat skin
    • Clone JN, Cohen IK, Diegelmann RF. Quantitation of the collagen types I and III during wound healing in the rat skin. Proc Soc Exp Biol Med 1979;161:337-340.
    • (1979) Proc Soc Exp Biol Med , vol.161 , pp. 337-340
    • Clone, J.N.1    Cohen, I.K.2    Diegelmann, R.F.3
  • 233
    • 0020577973 scopus 로고
    • Type V collagen during granulation tissue development
    • Hering TM, Marchant RE, Anderson JM. Type V collagen during granulation tissue development. Exp Mol Pathol 1983;39:219-229.
    • (1983) Exp Mol Pathol , vol.39 , pp. 219-229
    • Hering, T.M.1    Marchant, R.E.2    Anderson, J.M.3
  • 234
    • 0019462518 scopus 로고
    • The identification of A and B collagen chains in hypertrophic scars
    • Ehrlich HP, White BS. The identification of A and B collagen chains in hypertrophic scars. Exp Mol Pathol 1981;34:1-8.
    • (1981) Exp Mol Pathol , vol.34 , pp. 1-8
    • Ehrlich, H.P.1    White, B.S.2
  • 235
    • 0027466950 scopus 로고
    • Expression of type VI collagen mRNA during wound healing
    • Oono T, Specks U, Eckes B. Expression of type VI collagen mRNA during wound healing. J Invest Dermatol 1993;100:329-334.
    • (1993) J Invest Dermatol , vol.100 , pp. 329-334
    • Oono, T.1    Specks, U.2    Eckes, B.3
  • 236
    • 0023821420 scopus 로고
    • Ultrastructure of type VI collagen in human skin and cartilage suggests an anchoring function for this filamentous work
    • Keene DR, Engvall E, Glanvill RW. Ultrastructure of type VI collagen in human skin and cartilage suggests an anchoring function for this filamentous work. J Cell Biol 1988;107:1995-2006.
    • (1988) J Cell Biol , vol.107 , pp. 1995-2006
    • Keene, D.R.1    Engvall, E.2    Glanvill, R.W.3
  • 240
    • 0041436616 scopus 로고
    • Chemotactic attraction of human fibroblast to type I, II and III collagens and collagen derived peptides
    • Postlethwaite AE, Seyer JM, Kang AH. Chemotactic attraction of human fibroblast to type I, II and III collagens and collagen derived peptides. Proc Natl Acad Sci USA 1978;75:871-875.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 871-875
    • Postlethwaite, A.E.1    Seyer, J.M.2    Kang, A.H.3
  • 241
    • 0027955331 scopus 로고
    • Fibroblasts, myofibroblasts and wound contraction
    • Grinnell F. Fibroblasts, myofibroblasts and wound contraction. J Cell Biol 1994;124:401-404.
    • (1994) J Cell Biol , vol.124 , pp. 401-404
    • Grinnell, F.1
  • 242
    • 0022977704 scopus 로고
    • Reorganisation of polymerized actin: A possible trigger for induction of procollagenase in fibroblasts in and on collagen gels
    • Unemore EN, Werb Z. Reorganisation of polymerized actin: a possible trigger for induction of procollagenase in fibroblasts in and on collagen gels. J Cell Biol 1986;103:1021-1031.
    • (1986) J Cell Biol , vol.103 , pp. 1021-1031
    • Unemore, E.N.1    Werb, Z.2
  • 243
    • 0025880917 scopus 로고
    • Integrin α2ß1 is up-regulated in fibroblasts and highly aggressive melanoma cells in three dimensional collagen lattices and mediates the re-organisation of collagen I fibrils
    • Klein CE, Dressel D, Steinmayer T, et al. Integrin α2ß1 is up-regulated in fibroblasts and highly aggressive melanoma cells in three dimensional collagen lattices and mediates the re-organisation of collagen I fibrils. J Cell Biol 1991;115:1427-1436.
    • (1991) J Cell Biol , vol.115 , pp. 1427-1436
    • Klein, C.E.1    Dressel, D.2    Steinmayer, T.3
  • 244
    • 0027761345 scopus 로고
    • Localisation of mRNAs representing collagenase and TIMP in sections of healing human burn wounds
    • Stricklin GP, Li L, Jancic V, et al. Localisation of mRNAs representing collagenase and TIMP in sections of healing human burn wounds. Am J Pathol 1993;143:1657-1666.
    • (1993) Am J Pathol , vol.143 , pp. 1657-1666
    • Stricklin, G.P.1    Li, L.2    Jancic, V.3
  • 246
    • 0023279003 scopus 로고
    • The activation of human skin fibroblast procollagenase. Sequence identification of the major conversion products
    • Grant GA, Eisen AZ, Marmer BL, et al. The activation of human skin fibroblast procollagenase. Sequence identification of the major conversion products. J Biol Chem 1987;262:5886-5889.
    • (1987) J Biol Chem , vol.262 , pp. 5886-5889
    • Grant, G.A.1    Eisen, A.Z.2    Marmer, B.L.3
  • 247
    • 0023514969 scopus 로고
    • Expression of metalloproteinase that degrades native type V collagen and denatured collagens by cultured human alveolar macrophages
    • Hibbs MS, Hoidal JR, Kang AH. Expression of metalloproteinase that degrades native type V collagen and denatured collagens by cultured human alveolar macrophages. J Clin Invest 1987;80:1644-1650.
    • (1987) J Clin Invest , vol.80 , pp. 1644-1650
    • Hibbs, M.S.1    Hoidal, J.R.2    Kang, A.H.3
  • 248
    • 0024493129 scopus 로고
    • The activation of human type IV collagenase proenzyme. Sequence identification of the major conversion product following organomercurial activation
    • Stetler-Stevenson WG, Krutzsch HC, Wacher MP, et al. The activation of human type IV collagenase proenzyme. Sequence identification of the major conversion product following organomercurial activation. J Biol Chem 1989;264:1353-1356.
    • (1989) J Biol Chem , vol.264 , pp. 1353-1356
    • Stetler-Stevenson, W.G.1    Krutzsch, H.C.2    Wacher, M.P.3
  • 249
    • 0023942417 scopus 로고
    • The complete primary structure of human matrix metalloproteinase 3. Identity with stromelysin
    • Saus J, Quinones S, Otani Y, et al. The complete primary structure of human matrix metalloproteinase 3. Identity with stromelysin. J Biol Chem 1988;263:6742-6745.
    • (1988) J Biol Chem , vol.263 , pp. 6742-6745
    • Saus, J.1    Quinones, S.2    Otani, Y.3
  • 250
    • 0023597604 scopus 로고
    • Some recent advances in the chemistry and biology of transforming growth factor beta
    • Sporn MB, Roberts AB, Wakefield L, et al. Some recent advances in the chemistry and biology of transforming growth factor beta. J Cell Biol 1987;105:1039-1045.
    • (1987) J Cell Biol , vol.105 , pp. 1039-1045
    • Sporn, M.B.1    Roberts, A.B.2    Wakefield, L.3
  • 251
    • 0028986030 scopus 로고
    • Neutralisation of TGF-beta 1 and TGF-beta 2 or exogenous addition of TGF-beta 3 to cutaneous rat wounds reduces scarring
    • Shah M, Foreman DM, Ferguson MW. Neutralisation of TGF-beta 1 and TGF-beta 2 or exogenous addition of TGF-beta 3 to cutaneous rat wounds reduces scarring. J Cell Sci 1995;108(3):985-1002.
    • (1995) J Cell Sci , vol.108 , Issue.3 , pp. 985-1002
    • Shah, M.1    Foreman, D.M.2    Ferguson, M.W.3
  • 252
    • 0024687481 scopus 로고
    • Genes for extracellular matrix-degrading metalloproteases and their inhibitor TIMP are expressed during early mammalian development
    • Brenner CA, Adler RR, Rappolee DA, et al. Genes for extracellular matrix-degrading metalloproteases and their inhibitor TIMP are expressed during early mammalian development. Genes Dev 1989;3:848-859.
    • (1989) Genes Dev , vol.3 , pp. 848-859
    • Brenner, C.A.1    Adler, R.R.2    Rappolee, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.