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Volumn 90, Issue 12, 2011, Pages 1367-1376

Epithelial integrins with special reference to oral epithelia

Author keywords

cell matrix interactions; extracellular matrix (ECM); gingiva; keratinocyte(s); receptors; wound healing

Indexed keywords


EID: 81555220107     PISSN: 00220345     EISSN: 15440591     Source Type: Journal    
DOI: 10.1177/0022034511402207     Document Type: Review
Times cited : (96)

References (120)
  • 1
    • 0034835590 scopus 로고    scopus 로고
    • Immunohistochemical localization of large chondroitin sulphate proteoglycan in porcine gingival epithelia
    • DOI 10.1076/ejom.39.2.99.7372
    • Abiko Y, Nishimura M, Rahemtulla F, Mizoguchi I, Kaku T. Immunohistochemical localization of large chondroitin sulphate proteoglycan in porcine gingival epithelia. Eur J Morphol. 2001 ; 39: 99-104 (Pubitemid 32881434)
    • (2001) European Journal of Morphology , vol.39 , Issue.2 , pp. 99-104
    • Abiko, Y.1    Nishimura, M.2    Rahemtulla, F.3    Mizoguchi, I.4    Kaku, T.5
  • 2
    • 0030224033 scopus 로고    scopus 로고
    • The peri-implant hard and soft tissues at different implant systems: A comparative study in the dog
    • Abrahamsson I, Berglundh T, Wennstrom J, Lindhe J. The peri-implant hard and soft tissue characteristics at different implant systems. A comparative study in dogs. Clin Oral Implants Res. 1996 ; 7: 212-219 (Pubitemid 126670527)
    • (1996) Clinical Oral Implants Research , vol.7 , Issue.3 , pp. 212-219
    • Abrahamsson, I.1    Berglundh, T.2    Wennstrom, J.3    Lindhe, J.4
  • 3
    • 0033194955 scopus 로고    scopus 로고
    • Peri-implant tissues at submerged and non-submerged titanium implants
    • Abrahamsson I, Berglundh T, Moon IS, Lindhe J. Peri-implant tissues at submerged and non-submerged titanium implants. J Clin Periodontol. 1999 ; 26: 600-607
    • (1999) J Clin Periodontol , vol.26 , pp. 600-607
    • Abrahamsson, I.1    Berglundh, T.2    Moon, I.S.3    Lindhe, J.4
  • 4
    • 9644294245 scopus 로고    scopus 로고
    • Increase of laminin 5 synthesis in human keratinocytes by acute wound fluid, inflammatory cytokines and growth factors, and lysophospholipids
    • DOI 10.1111/j.1365-2133.2004.06175.x
    • Amano S, Akutsu N, Ogura Y, Nishiyama T. Increase of laminin 5 synthesis in human keratinocytes by acute wound fluid, inflammatory cytokines and growth factors, and lysophospholipids. Br J Dermatol. 2004 ; 151: 961-970 (Pubitemid 39573883)
    • (2004) British Journal of Dermatology , vol.151 , Issue.5 , pp. 961-970
    • Amano, S.1    Akutsu, N.2    Ogura, Y.3    Nishiyama, T.4
  • 6
    • 9644255532 scopus 로고    scopus 로고
    • Changes in the distribution of laminin-5 during peri-implant epithelium formation after immediate titanium implantation in rats
    • DOI 10.1016/j.biomaterials.2004.05.033, PII S0142961204005095
    • Atsuta I, Yamaza T, Yoshinari M, Mino S, Goto T, Kido MA, et al. Changes in the distribution of laminin-5 during peri-implant epithelium formation after immediate titanium implantation in rats. Biomaterials. 2005a ; 26: 1751-1760 (Pubitemid 39575318)
    • (2005) Biomaterials , vol.26 , Issue.14 , pp. 1751-1760
    • Atsuta, I.1    Yamaza, T.2    Yoshinari, M.3    Mino, S.4    Goto, T.5    Kido, M.A.6    Terada, Y.7    Tanaka, T.8
  • 7
    • 20444473693 scopus 로고    scopus 로고
    • Ultrastructural localization of laminin-5 (γ2 chain) in the rat peri-implant oral mucosa around a titanium-dental implant by immuno-electron microscopy
    • DOI 10.1016/j.biomaterials.2005.03.046, PII S014296120500298X
    • Atsuta I, Yamaza T, Yoshinari M, Goto T, Kido MA, Kagiya T, et al. Ultrastructural localization of laminin-5 (?2 chain) in the rat peri-implant oral mucosa around a titanium-dental implant by immuno-electron microscopy. Biomaterials. 2005b ; 26: 6280-6287 (Pubitemid 40828384)
    • (2005) Biomaterials , vol.26 , Issue.32 , pp. 6280-6287
    • Atsuta, I.1    Yamaza, T.2    Yoshinari, M.3    Goto, T.4    Kido, M.A.5    Kagiya, T.6    Mino, S.7    Shimono, M.8    Tanaka, T.9
  • 8
    • 0037361399 scopus 로고    scopus 로고
    • Laminin 5 processing and its integration into the ECM
    • DOI 10.1016/S0945-053X(03)00013-1, PII S0945053X03000131
    • Aumailley M, El Khal A, Knöss N, Tunggal L. Laminin 5 processing and its integration into the ECM. Matrix Biol. 2003 ; 22: 49-54 (Pubitemid 36444506)
    • (2003) Matrix Biology , vol.22 , Issue.1 , pp. 49-54
    • Aumailley, M.1    El Khal, A.2    Knoss, N.3    Tunggal, L.4
  • 9
    • 0030253561 scopus 로고    scopus 로고
    • Dimension of the periimplant mucosa Biological width revisited
    • Berglundh T, Lindhe J. Dimension of the periimplant mucosa. Biological width revisited. J Clin Periodontol. 1996 ; 23: 971-973 (Pubitemid 126732066)
    • (1996) Journal of Clinical Periodontology , vol.23 , Issue.10 , pp. 971-973
    • Berglundh, T.1
  • 10
    • 0032908323 scopus 로고    scopus 로고
    • Structure and function of hemidesmosomes: More than simple adhesion complexes
    • DOI 10.1046/j.1523-1747.1999.00546.x
    • Borradori L, Sonnenberg A. Structure and function of hemidesmosomes: more than simple adhesion complexes. J Invest Dermatol. 1999 ; 112: 411-418 (Pubitemid 29171928)
    • (1999) Journal of Investigative Dermatology , vol.112 , Issue.4 , pp. 411-418
    • Borradori, L.1    Sonnenberg, A.2
  • 11
    • 16644396846 scopus 로고    scopus 로고
    • The junctional epithelium: From health to disease
    • DOI 10.1177/154405910508400102
    • Bosshardt DD, Lang NP. The junctional epithelium: from health to disease. J Dent Res. 2005 ; 84: 9-20 (Pubitemid 43822055)
    • (2005) Journal of Dental Research , vol.84 , Issue.1 , pp. 9-20
    • Bosshardt, D.D.1    Lang, N.P.2
  • 14
    • 0025887362 scopus 로고
    • Epiligrin, a new cell adhesion ligand for integrin ?3?1 in epithelial basement membranes
    • Carter WG, Ryan MC, Gahr PJ. Epiligrin, a new cell adhesion ligand for integrin ?3?1 in epithelial basement membranes. Cell. 1991 ; 65: 599-610
    • (1991) Cell , vol.65 , pp. 599-610
    • Carter, W.G.1    Ryan, M.C.2    Gahr, P.J.3
  • 16
    • 0036904895 scopus 로고    scopus 로고
    • Genetic analysis of the mammalian transforming growth factor-β superfamily
    • DOI 10.1210/er.2002-0003
    • Chang H, Brown CW, Matzuk MM. Genetic analysis of the mammalian transforming growth factor-ß superfamily. Endocr Rev. 2002 ; 23: 787-823 (Pubitemid 35454589)
    • (2002) Endocrine Reviews , vol.23 , Issue.6 , pp. 787-823
    • Chang, H.1    Brown, C.W.2    Matzuk, M.M.3
  • 17
    • 0029944242 scopus 로고    scopus 로고
    • Re-epithelialization of normal human excisional wounds is associated with a switch from αvβ5 to αvβ6 integrins
    • Clark RA, Ashcroft GS, Spencer MJ, Larjava H, Ferguson MW. Re-epithelialization of normal human excisional wounds is associated with a switch from vß5 to vß6 integrins. Br J Dermatol. 1996 ; 135: 46-51 (Pubitemid 26225114)
    • (1996) British Journal of Dermatology , vol.135 , Issue.1 , pp. 46-51
    • Clark, R.A.F.1    Ashcroft, G.S.2    Spencer, M.-J.3    Larjava, H.4    Ferguson, M.W.J.5
  • 18
    • 0031067775 scopus 로고    scopus 로고
    • Biologic Width Around Titanium Implants. A Histometric Analysis of the Implanto-Gingival Junction Around Unloaded and Loaded Nonsubmerged Implants in the Canine Mandible
    • Cochran DL, Hermann JS, Schenk RK, Higginbottom FL, Buser D. Biologic width around titanium implants. A histometric analysis of the implanto-gingival junction around unloaded and loaded nonsubmerged implants in the canine mandible. J Periodontol. 1997 ; 68: 186-198 (Pubitemid 127518261)
    • (1997) Journal of Periodontology , vol.68 , Issue.2 , pp. 186-198
    • Cochran, D.L.1    Hermann, J.S.2    Schenk, R.K.3    Higginbottom, F.L.4    Buser, D.5
  • 19
    • 33847787559 scopus 로고    scopus 로고
    • Distinct molecular composition of human interdental papilla
    • Csiszar A, Wiebe C, Larjava H, Häkkinen L. Distinct molecular composition of human interdental papilla. J Periodontol. 2007 ; 78: 304-314
    • (2007) J Periodontol , vol.78 , pp. 304-314
    • Csiszar, A.1    Wiebe, C.2    Larjava, H.3    Häkkinen, L.4
  • 20
    • 0033847622 scopus 로고    scopus 로고
    • Regulation of tissue injury responses by the exposure of matricryptic sites within extracellular matrix molecules
    • Davis GE, Bayless KJ, Davis MJ, Meininger GA. Regulation of tissue injury responses by the exposure of matricryptic sites within extracellular matrix molecules. Am J Pathol. 2000 ; 156: 1489-1498 (Pubitemid 30646688)
    • (2000) American Journal of Pathology , vol.156 , Issue.5 , pp. 1489-1498
    • Davis, G.E.1    Bayless, K.J.2    Davis, M.J.3    Meininger, G.A.4
  • 21
    • 0035085802 scopus 로고    scopus 로고
    • Keratinocyte migration requires α2β1 integrin-mediated interaction with the laminin 5 γ2 chain
    • Décline F, Rousselle P. Keratinocyte migration requires ?2ß1 integrin-mediated interaction with the laminin 5?2 chain. J Cell Sci. 2001 ; 114 (Pt 4). 811-823 (Pubitemid 32241778)
    • (2001) Journal of Cell Science , vol.114 , Issue.4 , pp. 811-823
    • Decline, F.1    Rousselle, P.2
  • 22
    • 0037330988 scopus 로고    scopus 로고
    • The role of α3β1 integrin in determining the supramolecular organization of laminin-5 in the extracellular matrix of keratinocytes
    • DOI 10.1016/S0014-4827(02)00028-9
    • deHart GW, Healy KE, Jones JC. The role of 3ß1 integrin in determining the supramolecular organization of laminin-5 in the extracellular matrix of keratinocytes. Exp Cell Res. 2003 ; 283: 67-79 (Pubitemid 36259896)
    • (2003) Experimental Cell Research , vol.283 , Issue.1 , pp. 67-79
    • DeHart, G.W.1    Healy, K.E.2    Jones, J.C.R.3
  • 23
    • 64949151593 scopus 로고    scopus 로고
    • Over-expression of forkhead box P3 and its association with receptor activator of nuclear factor-? B ligand, interleukin (IL) -17, IL-10 and transforming growth factor-ß during the progression of chronic periodontitis
    • Dutzan N, Gamonal J, Silva A, Sanz M, Vernal R. Over-expression of forkhead box P3 and its association with receptor activator of nuclear factor-? B ligand, interleukin (IL) -17, IL-10 and transforming growth factor-ß during the progression of chronic periodontitis. J Clin Periodontol. 2009 ; 36: 396-403
    • (2009) J Clin Periodontol , vol.36 , pp. 396-403
    • Dutzan, N.1    Gamonal, J.2    Silva, A.3    Sanz, M.4    Vernal, R.5
  • 24
    • 0024344620 scopus 로고
    • Reappearance of an embryonic pattern of fibronectin splicing during wound healing in the adult rat
    • Ffrench-Constant C, van de Water L, Dvorak HF, Hynes RO. Re-appearance of an embryonic pattern of fibronectin splicing during wound healing in the adult rat. J Cell Biol. 1989 ; 109: 903-914 (Pubitemid 19197047)
    • (1989) Journal of Cell Biology , vol.109 , Issue.2 , pp. 903-914
    • French-Constant, C.1    Van De Water, L.2    Dvorak, H.F.3    Hynes, R.O.4
  • 25
    • 3843076714 scopus 로고    scopus 로고
    • An experimental study on the features of peri-implant epithelium: Immunohistochemical and electron-microscopic observations
    • Fujiseki M, Matsuzaka K, Yoshinari M, Shimono M, Inoue T. An experimental study on the features of peri-implant epithelium: immunohistochemical and electron-microscopic observations. Bull Tokyo Dent Coll. 2003 ; 44: 185-199
    • (2003) Bull Tokyo Dent Coll , vol.44 , pp. 185-199
    • Fujiseki, M.1    Matsuzaka, K.2    Yoshinari, M.3    Shimono, M.4    Inoue, T.5
  • 26
    • 0027990415 scopus 로고
    • Wound repair in the context of extracellular matrix
    • Gailit J, Clark RA. Wound repair in the context of extracellular matrix. Curr Opin Cell Biol. 1994 ; 6: 717-725 (Pubitemid 24295306)
    • (1994) Current Opinion in Cell Biology , vol.6 , Issue.5 , pp. 717-725
    • Gailit, J.1    Clark, R.A.F.2
  • 27
    • 0000171086 scopus 로고
    • Dimensions and relations of the dentogingival junction in humans
    • Gargiulo AW, Wentz FM, Orban B. Dimensions and relations of the dentogingival junction in humans. J Periodontol. 1961 ; 32: 261-267
    • (1961) J Periodontol , vol.32 , pp. 261-267
    • Gargiulo, A.W.1    Wentz, F.M.2    Orban, B.3
  • 29
    • 0037105657 scopus 로고    scopus 로고
    • 5 integrins and promotes cell motility
    • Gillan L, Matei D, Fishman DA, Gerbin CS, Karlan BY, Chang DD. Periostin secreted by epithelial ovarian carcinoma is a ligand for alpha(V)beta(3) and alpha(V)beta(5) integrins and promotes cell motility. Cancer Res. 2002 ; 62: 5358-5364 (Pubitemid 35024613)
    • (2002) Cancer Research , vol.62 , Issue.18 , pp. 5358-5364
    • Gillan, L.1    Matei, D.2    Fishman, D.A.3    Gerbin, C.S.4    Karlan, B.Y.5    Chang, D.D.6
  • 31
    • 0032841440 scopus 로고    scopus 로고
    • The α3 laminin subunit, α6β4 and α3β1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin
    • Goldfinger LE, Hopkinson SB, deHart GW, Collawn S, Couchman JR, Jones JC. The ?3 laminin subunit, 6ß4 and 3ß1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin. J Cell Sci. 1999 ; 112 (Pt 16). 2615-2629 (Pubitemid 29429785)
    • (1999) Journal of Cell Science , vol.112 , Issue.16 , pp. 2615-2629
    • Goldfinger, L.E.1    Hopkinson, S.B.2    Dehart, G.W.3    Collawn, S.4    Couchman, J.R.5    Jones, J.C.R.6
  • 32
    • 0021484833 scopus 로고
    • Ultrastructural study of the attachment of human gingiva to titanium in vivo
    • Gould TR, Westbury L, Brunette DM. Ultrastructural study of the attachment of human gingiva to titanium in vivo. J Prosthet Dent. 1984 ; 52: 418-420
    • (1984) J Prosthet Dent , vol.52 , pp. 418-420
    • Gould, T.R.1    Westbury, L.2    Brunette, D.M.3
  • 33
    • 0036333993 scopus 로고    scopus 로고
    • A crucial role of β1 integrins for keratinocyte migration in vitro and during cutaneous wound repair
    • Grose R, Hutter C, Bloch W, Thorey I, Watt FM, Fassler R, et al. A crucial role of ß1 integrins for keratinocyte migration in vitro and during cutaneous wound repair. Development. 2002 ; 129: 2303-2315 (Pubitemid 34874240)
    • (2002) Development , vol.129 , Issue.9 , pp. 2303-2315
    • Grose, R.1    Hutter, C.2    Bloch, W.3    Thorey, I.4    Watt, F.M.5    Fassler, R.6    Brakebusch, C.7    Werner, S.8
  • 34
    • 0029039807 scopus 로고
    • Expression of epithelial adhesion proteins and integrins in chronic inflammation
    • Haapasalmi K, Makela M, Oksala O, Heino J, Yamada KM, Uitto VJ, et al. Expression of epithelial adhesion proteins and integrins in chronic inflammation. Am J Pathol. 1995 ; 147: 193-206
    • (1995) Am J Pathol , vol.147 , pp. 193-206
    • Haapasalmi, K.1    Makela, M.2    Oksala, O.3    Heino, J.4    Yamada, K.M.5    Uitto, V.J.6
  • 37
  • 40
    • 34247152600 scopus 로고    scopus 로고
    • Laminin-5-deficient human keratinocytes: Defective adhesion results in a saltatory and inefficient mode of migration
    • DOI 10.1016/j.yexcr.2007.02.003, PII S0014482707000584
    • Hartwig B, Borm B, Schneider H, Arin MJ, Kirfel G, Herzog V. Laminin-5-deficient human keratinocytes: defective adhesion results in a saltatory and inefficient mode of migration. Exp Cell Res. 2007 ; 313: 1575-1587 (Pubitemid 46589435)
    • (2007) Experimental Cell Research , vol.313 , Issue.8 , pp. 1575-1587
    • Hartwig, B.1    Borm, B.2    Schneider, H.3    Arin, M.J.4    Kirfel, G.5    Herzog, V.6
  • 41
    • 73549105028 scopus 로고    scopus 로고
    • Kindlin-1 is required for RhoGTPase-mediated lamellipodia formation in keratinocytes
    • Has C, Herz C, Zimina E, Qu HY, He Y, Zhang ZG, et al. Kindlin-1 is required for RhoGTPase-mediated lamellipodia formation in keratinocytes. Am J Pathol. 2009 ; 175: 1442-1452
    • (2009) Am J Pathol , vol.175 , pp. 1442-1452
    • Has, C.1    Herz, C.2    Zimina, E.3    Qu, H.Y.4    He, Y.5    Zhang, Z.G.6
  • 43
    • 0032904231 scopus 로고    scopus 로고
    • Tenascin-C inhibits β1 integrin-dependent T lymphocyte adhesion to fibronectin through the binding of its fnIII 1-5 repeats to fibronectin
    • DOI 10.1002/(SICI)1521-4141(199905)29:05<1435::AID-IMMU1435>3.0. CO;2-N
    • Hauzenberger D, Olivier P, Gundersen D, Ruegg C. Tenascin-C inhibits ß1 integrin-dependent T lymphocyte adhesion to fibronectin through the binding of its fnIII 1-5 repeats to fibronectin. Eur J Immunol. 1999 ; 29: 1435-1447 (Pubitemid 29224448)
    • (1999) European Journal of Immunology , vol.29 , Issue.5 , pp. 1435-1447
    • Hauzenberger, D.1    Olivier, P.2    Gundersen, D.3    Ruegg, C.4
  • 45
    • 33845990287 scopus 로고    scopus 로고
    • Kindlin-1 is a phosphoprotein involved in regulation of polarity, proliferation, and motility of epidermal keratinocytes
    • DOI 10.1074/jbc.M606259200
    • Herz C, Aumailley M, Schulte C, Schlötzer-Schrehardt U, Bruckner-Tuderman L, Has C. Kindlin-1 is a phosphoprotein involved in regulation of polarity, proliferation, and motility of epidermal keratinocytes. J Biol Chem. 2006 ; 281: 36082-36090 (Pubitemid 46041341)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.47 , pp. 36082-36090
    • Herz, C.1    Aumailley, M.2    Schulte, C.3    Schlotzer-Schrehardt, U.4    Bruckner-Tuderman, L.5    Has, C.6
  • 46
    • 0032493934 scopus 로고    scopus 로고
    • Novel roles for α3β1 integrin as a regulator of cytoskeletal assembly and as a trans-dominant inhibitor of integrin receptor function in mouse keratinocytes
    • DOI 10.1083/jcb.142.5.1357
    • Hodivala-Dilke KM, DiPersio CM, Kreidberg JA, Hynes RO. Novel roles for 3ß1 integrin as a regulator of cytoskeletal assembly and as a trans-dominant inhibitor of integrin receptor function in mouse keratinocytes. J Cell Biol. 1998 ; 142: 1357-1369 (Pubitemid 28429116)
    • (1998) Journal of Cell Biology , vol.142 , Issue.5 , pp. 1357-1369
    • Hodivala-Dilke, K.M.1    DiPersio, C.M.2    Kreidberg, J.A.3    Hynes, R.O.4
  • 47
    • 0026902305 scopus 로고
    • Immunolocalization of integrin ?6ß4 in mouse junctional epithelium suggests an anchoring function to both the internal and the external basal lamina
    • Hormia M, Virtanen I, Quaranta V. Immunolocalization of integrin ?6ß4 in mouse junctional epithelium suggests an anchoring function to both the internal and the external basal lamina. J Dent Res. 1992 ; 71: 1503-1508
    • (1992) J Dent Res , vol.71 , pp. 1503-1508
    • Hormia, M.1    Virtanen, I.2    Quaranta, V.3
  • 48
    • 0032223676 scopus 로고    scopus 로고
    • The epithelium-tooth interface - A basal lamina rich in laminin-5 and lacking other known laminin isoforms
    • Hormia M, Sahlberg C, Thesleff I, Airenne T. The epithelium-tooth interface-a basal lamina rich in laminin-5 and lacking other known laminin isoforms. J Dent Res. 1998 ; 77: 1479-1485 (Pubitemid 32770519)
    • (1998) Journal of Dental Research , vol.77 , Issue.7 , pp. 1479-1485
    • Hormia, M.1    Sahlberg, C.2    Thesleff, I.3    Airenne, T.4
  • 49
    • 0035381134 scopus 로고    scopus 로고
    • The dento-epithelial junction: Cell adhesion by type I hemidesmosomes in the absence of a true lamina
    • DOI 10.1902/jop.2001.72.6.788
    • Hormia M, Owaribe K, Virtanen I. The dento-epithelial junction: cell adhesion by type I hemidesmosomes in the absence of a true basal lamina. J Periodontol. 2001 ; 72: 788-797 (Pubitemid 33606562)
    • (2001) Journal of Periodontology , vol.72 , Issue.6 , pp. 788-797
    • Hormia, M.1    Owaribe, K.2    Virtanen, I.3
  • 50
    • 15844376477 scopus 로고    scopus 로고
    • Inactivation of the integrin β6 subunit gene reveals a role of epithelial integrins in regulating inflammation in the lungs and skin
    • DOI 10.1083/jcb.133.4.921
    • Huang XZ, Wu JF, Cass D, Erle DJ, Corry D, Young SG, et al. Inactivation of the integrin ß6 subunit gene reveals a role of epithelial integrins in regulating inflammation in the lung and skin. J Cell Biol. 1996 ; 133: 921-928 (Pubitemid 26160991)
    • (1996) Journal of Cell Biology , vol.133 , Issue.4 , pp. 921-928
    • Huang, X.-Z.1    Wu, J.F.2    Cass, D.3    Erie, D.J.4    Corry, D.5    Young, S.G.6    Farese Jr., R.V.7    Sheppard, D.8
  • 51
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • DOI 10.1016/S0092-8674(02)00971-6
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell. 2002 ; 110: 673-687 (Pubitemid 35283958)
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 52
    • 0034204162 scopus 로고    scopus 로고
    • Ultrastructural and immunoelectron microscopic studies of the peri-implant epithelium-implant (Ti-6Al-4V) interface of rat maxilla
    • Ikeda H, Yamaza T, Yoshinari M, Ohsaki Y, Ayukawa Y, Kido MA, et al. Ultrastructural and immunoelectron microscopic studies of the peri-implant epithelium-implant (Ti-6Al-4V) interface of rat maxilla. J Periodontol. 2000 ; 71: 961-973
    • (2000) J Periodontol , vol.71 , pp. 961-973
    • Ikeda, H.1    Yamaza, T.2    Yoshinari, M.3    Ohsaki, Y.4    Ayukawa, Y.5    Kido, M.A.6
  • 53
    • 0036617089 scopus 로고    scopus 로고
    • Difference in penetration of horseradish peroxidase tracer as a foreign substance into the peri-implant or junctional epithelium of rat gingivae
    • DOI 10.1034/j.1600-0501.2002.130303.x
    • Ikeda H, Shiraiwa M, Yamaza T, Yoshinari M, Kido MA, Ayukawa Y, et al. Difference in penetration of horseradish peroxidase tracer as a foreign substance into the peri-implant or junctional epithelium of rat gingivae. Clin Oral Implants Res. 2002 ; 13: 243-251 (Pubitemid 41698461)
    • (2002) Clinical Oral Implants Research , vol.13 , Issue.3 , pp. 243-251
    • Ikeda, H.1    Shiraiwa, M.2    Yamaza, T.3    Yoshinari, M.4    Kido, M.A.5    Ayukawa, Y.6    Inoue, T.7    Koyano, K.8    Tanaka, T.9
  • 54
    • 0347916989 scopus 로고    scopus 로고
    • Differential expression of matrilysin-I (MMP-7), 92 kD gelatinase (MMP-9), and metalloelastase (MMP-12) in oral verrucous and squamous cell cancer
    • DOI 10.1002/path.1479
    • Impola U, Uitto VJ, Hietanen J, Häkkinen L, Zhang L, Larjava H, et al. Differential expression of matrilysin-1 (MMP-7), 92 kD gelatinase (MMP-9), and metalloelastase (MMP-12) in oral verrucous and squamous cell cancer. J Pathol. 2004 ; 202: 14-22 (Pubitemid 38072841)
    • (2004) Journal of Pathology , vol.202 , Issue.1 , pp. 14-22
    • Impola, U.1    Uitto, V.J.2    Hietanen, J.3    Hakkinen, L.4    Zhang, L.5    Larjava, H.6    Isaka, K.7    Saarialho-Kere, U.8
  • 55
    • 3142655415 scopus 로고    scopus 로고
    • Localization of a cryptic binding site for tenascin on fibronectin
    • DOI 10.1074/jbc.M312785200
    • Ingham KC, Brew SA, Erickson HP. Localization of a cryptic binding site for tenascin on fibronectin. J Biol Chem. 2004 ; 279: 28132-28135 (Pubitemid 38900086)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 28132-28135
    • Ingham, K.C.1    Brew, S.A.2    Erickson, H.P.3
  • 56
    • 0031197158 scopus 로고    scopus 로고
    • Immunolocalization of proliferating cell nuclear antigen in the peri-implant epithelium
    • Inoue T, Takeda T, Lee CY, Abiko Y, Ayukawa Y, Tanaka T, et al. Immunolocalization of proliferating cell nuclear antigen in the peri-implant epithelium. Bull Tokyo Dent Coll. 1997 ; 38: 187-193
    • (1997) Bull Tokyo Dent Coll , vol.38 , pp. 187-193
    • Inoue, T.1    Takeda, T.2    Lee, C.Y.3    Abiko, Y.4    Ayukawa, Y.5    Tanaka, T.6
  • 59
    • 0027744501 scopus 로고
    • Regulation of extracellular matrix proteins and integrin cell substratum adhesion receptors on epithelium during cutaneous human wound healing in vivo
    • Juhasz I, Murphy GF, Yan HC, Herlyn M, Albelda SM. Regulation of extracellular matrix proteins and integrin cell substratum adhesion receptors on epithelium during cutaneous human wound healing in vivo. Am J Pathol. 1993 ; 143: 1458-1469 (Pubitemid 24057116)
    • (1993) American Journal of Pathology , vol.143 , Issue.5 , pp. 1458-1469
    • Juhasz, I.1    Murphy, G.F.2    Yan, H.-C.3    Herlyn, M.4    Albelda, S.M.5
  • 61
    • 0025328916 scopus 로고
    • Transforming growth factor-ß1 localization in normal and psoriatic epidermal keratinocytes in situ
    • Kane CJ, Knapp AM, Mansbridge JN, Hanawalt PC. Transforming growth factor-ß1 localization in normal and psoriatic epidermal keratinocytes in situ. J Cell Physiol. 1990 ; 144: 144-150
    • (1990) J Cell Physiol , vol.144 , pp. 144-150
    • Kane, C.J.1    Knapp, A.M.2    Mansbridge, J.N.3    Hanawalt, P.C.4
  • 62
    • 0026647568 scopus 로고
    • Mechanism of human keratinocyte migration on fibronectin, unique roles of RGD site and integrins
    • Kim JP, Zhang K, Chen JD, Wynn KC, Kramer RH, Woodley DT. Mechanism of human keratinocyte migration on fibronectin, unique roles of RGD site and integrins. J Cell Physiol. 1992a ; 151: 443-450
    • (1992) J Cell Physiol , vol.151 , pp. 443-450
    • Kim, J.P.1    Zhang, K.2    Chen, J.D.3    Wynn, K.C.4    Kramer, R.H.5    Woodley, D.T.6
  • 63
    • 0026523180 scopus 로고
    • Integrin receptors and RGD sequences in human keratinocyte migration: Unique anti-migratory function of ?3ß1 epiligrin receptor
    • Kim JP, Zhang K, Kramer RH, Schall TJ, Woodley DT. Integrin receptors and RGD sequences in human keratinocyte migration: unique anti-migratory function of ?3ß1 epiligrin receptor. J Invest Dermatol. 1992b ; 98: 764-770
    • (1992) J Invest Dermatol , vol.98 , pp. 764-770
    • Kim, J.P.1    Zhang, K.2    Kramer, R.H.3    Schall, T.J.4    Woodley, D.T.5
  • 64
    • 58149330370 scopus 로고    scopus 로고
    • Involvement of laminin and integrins in adhesion and migration of junctional epithelium cells
    • Kinumatsu T, Hashimoto S, Muramatsu T, Sasaki H, Jung HS, Yamada S, et al. Involvement of laminin and integrins in adhesion and migration of junctional epithelium cells. J Periodontal Res. 2009 ; 44: 13-20
    • (2009) J Periodontal Res , vol.44 , pp. 13-20
    • Kinumatsu, T.1    Hashimoto, S.2    Muramatsu, T.3    Sasaki, H.4    Jung, H.S.5    Yamada, S.6
  • 65
    • 0032794389 scopus 로고    scopus 로고
    • Different integrins mediate cell spreading, haptotaxis and lateral migration of HaCaT keratinocytes on fibronectin
    • Koivisto L, Larjava K, Häkkinen L, Uitto V-J, Heino J, Larjava H. Different integrins mediate cell spreading, haptotaxis and lateral migration of HaCaT keratinocytes on fibronectin. Cell Adhes Commun. 1999 ; 7: 245-257 (Pubitemid 129725808)
    • (1999) Cell Communication and Adhesion , vol.7 , Issue.3 , pp. 245-257
    • Koivisto, L.1    Larjava, K.2    Hakkinen, L.3    Uitto, V.-J.4    Heino, J.5    Larjava, H.6
  • 66
    • 77649198273 scopus 로고    scopus 로고
    • Prevalence of peri-implantitis related to severity of the disease with different degrees of bone loss
    • Koldsland OC, Scheie AA, Aass AM. Prevalence of peri-implantitis related to severity of the disease with different degrees of bone loss. J Periodontol. 2010 ; 81: 231-238
    • (2010) J Periodontol , vol.81 , pp. 231-238
    • Koldsland, O.C.1    Scheie, A.A.2    Aass, A.M.3
  • 68
    • 49549083034 scopus 로고    scopus 로고
    • Colocalization of kindlin-1, kindlin-2, and migfilin at keratinocyte focal adhesion and relevance to the pathophysiology of Kindler syndrome
    • Lai-Cheong JE, Ussar S, Arita K, Hart IR, McGrath JA. Colocalization of kindlin-1, kindlin-2, and migfilin at keratinocyte focal adhesion and relevance to the pathophysiology of Kindler syndrome. J Invest Dermatol. 2008 ; 128: 2156-2165
    • (2008) J Invest Dermatol , vol.128 , pp. 2156-2165
    • Lai-Cheong, J.E.1    Ussar, S.2    Arita, K.3    Hart, I.R.4    McGrath, J.A.5
  • 70
    • 57049169143 scopus 로고    scopus 로고
    • Kindlins: Essential regulators of integrin signaling and cell-matrix adhesion
    • Larjava H, Plow EF, Wu C. Kindlins: essential regulators of integrin signaling and cell-matrix adhesion. EMBO Rep. 2008 ; 9: 1203-1208
    • (2008) EMBO Rep , vol.9 , pp. 1203-1208
    • Larjava, H.1    Plow, E.F.2    Wu, C.3
  • 71
    • 15744403811 scopus 로고    scopus 로고
    • Keratinocyte growth factor-1 expression in healthy and diseased human periodontal tissues
    • DOI 10.1111/j.1600-0765.2004.00780.x
    • Li M, Firth JD, Putnins EE. Keratinocyte growth factor-1 expression in healthy and diseased human periodontal tissues. J Periodontal Res. 2005 ; 40: 118-128 (Pubitemid 40417310)
    • (2005) Journal of Periodontal Research , vol.40 , Issue.2 , pp. 118-128
    • Li, M.1    Firth, J.D.2    Putnins, E.E.3
  • 72
    • 33748448717 scopus 로고    scopus 로고
    • Transforming Growth Factor-β Controls Development, Homeostasis, and Tolerance of T Cells by Regulatory T Cell-Dependent and -Independent Mechanisms
    • DOI 10.1016/j.immuni.2006.07.011, PII S1074761306003876
    • Li MO, Sanjabi S, Flavell RA. Transforming growth factor-ß controls development, homeostasis, and tolerance of T cells by regulatory T cell dependent and independent mechanisms. Immunity. 2006 ; 25: 455-471 (Pubitemid 44354214)
    • (2006) Immunity , vol.25 , Issue.3 , pp. 455-471
    • Li, M.O.1    Sanjabi, S.2    Flavell, RichardA.3
  • 73
    • 0037177894 scopus 로고    scopus 로고
    • 1 providing a novel mechanism for regulating cell adhesion by alternative splicing
    • DOI 10.1074/jbc.M201100200
    • Liao YF, Gotwals PJ, Koteliansky VE, Sheppard D, Van De Water L. The EIIIA segment of fibronectin is a ligand for integrins ?9ß1 and ?4ß1 providing a novel mechanism for regulating cell adhesion by alternative splicing. J Biol Chem. 2002 ; 277: 14467-14474 (Pubitemid 34952511)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.17 , pp. 14467-14474
    • Liao, Y.-F.1    Gotwals, P.J.2    Koteliansky, V.E.3    Sheppard, D.4    Van Water, L.D.5
  • 74
    • 33745947286 scopus 로고    scopus 로고
    • Current insights into the formation and breakdown of hemidesmosomes
    • DOI 10.1016/j.tcb.2006.05.004, PII S0962892406001395
    • Litjens SH, de Pereda JM, Sonnenberg A. Current insights into the formation and breakdown of hemidesmosomes. Trends Cell Biol. 2006 ; 16: 376-383 (Pubitemid 44062316)
    • (2006) Trends in Cell Biology , vol.16 , Issue.7 , pp. 376-383
    • Litjens, S.H.M.1    De Pereda, J.M.2    Sonnenberg, A.3
  • 76
    • 0033491886 scopus 로고    scopus 로고
    • The tenascin-C knockout revisited
    • Mackie EJ, Tucker RP. The tenascin-C knockout revisited. J Cell Sci. 1999 ; 112 (Pt 22). 3847-3853 (Pubitemid 30119755)
    • (1999) Journal of Cell Science , vol.112 , Issue.22 , pp. 3847-3853
    • Mackie, E.J.1    Tucker, R.P.2
  • 77
    • 61949421021 scopus 로고    scopus 로고
    • Integrin ?3ß1 inhibits directional migration and wound re-epithelialization in the skin
    • Margadant C, Raymond K, Kreft M, Sachs N, Janssen H, Sonnenberg A. Integrin ?3ß1 inhibits directional migration and wound re-epithelialization in the skin. J Cell Sci. 2009 ; 122 (Pt 2). 278-288
    • (2009) J Cell Sci , vol.122 , Issue.PART 2 , pp. 278-288
    • Margadant, C.1    Raymond, K.2    Kreft, M.3    Sachs, N.4    Janssen, H.5    Sonnenberg, A.6
  • 78
    • 63249111302 scopus 로고    scopus 로고
    • Peri-implant diseases may be associated with increased time loading and generalized periodontal bone loss: Preliminary results
    • Máximo MB, de Mendonça AC, Alves JF, Cortelli SC, Peruzzo DC, Duarte PM. Peri-implant diseases may be associated with increased time loading and generalized periodontal bone loss: preliminary results. J Oral Implantol. 2008 ; 34: 268-273
    • (2008) J Oral Implantol , vol.34 , pp. 268-273
    • Máximo, M.B.1    De Mendonça, A.C.2    Alves, J.F.3    Cortelli, S.C.4    Peruzzo, D.C.5    Duarte, P.M.6
  • 79
    • 70349312643 scopus 로고    scopus 로고
    • The Kindlin protein family: New members to the club of focal adhesion proteins
    • Meves A, Stremmel C, Gottschalk K, Fässler R. The Kindlin protein family: new members to the club of focal adhesion proteins. Trends Cell Biol. 2009 ; 19: 504-513
    • (2009) Trends Cell Biol , vol.19 , pp. 504-513
    • Meves, A.1    Stremmel, C.2    Gottschalk, K.3    Fässler, R.4
  • 80
    • 69449085135 scopus 로고    scopus 로고
    • 3ß1 integrin in epidermis promotes wound angiogenesis and keratinocyte-to-endothelial-cell crosstalk through the induction of MRP3
    • Mitchell K, Szekeres C, Milano V, Svenson KB, Nilsen-Hamilton M, Kreidberg JA, et al. 3ß1 integrin in epidermis promotes wound angiogenesis and keratinocyte-to-endothelial-cell crosstalk through the induction of MRP3. J Cell Sci. 2009 ; 122 (Pt 11). 1778-1787
    • (2009) J Cell Sci , vol.122 , Issue.PART 11 , pp. 1778-1787
    • Mitchell, K.1    Szekeres, C.2    Milano, V.3    Svenson, K.B.4    Nilsen-Hamilton, M.5    Kreidberg, J.A.6
  • 82
    • 0032528060 scopus 로고    scopus 로고
    • Cell cycle and adhesion defects in mice carrying a targeted deletion of the integrin β4 cytoplasmic domain
    • DOI 10.1093/emboj/17.14.3940
    • Murgia C, Blaikie P, Kim N, Dans M, Petrie HT, Giancotti FG. Cell cycle and adhesion defects in mice carrying a targeted deletion of the integrin ß4 cytoplasmic domain. EMBO J. 1998 ; 17: 3940-3951 (Pubitemid 28333980)
    • (1998) EMBO Journal , vol.17 , Issue.14 , pp. 3940-3951
    • Murgia, C.1    Blaikie, P.2    Kim, N.3    Dans, M.4    Petrie, H.T.5    Giancotti, F.G.6
  • 83
    • 0038825157 scopus 로고    scopus 로고
    • Regulated splicing of the fibronectin EDA exon is essential for proper skin wound healing and normal lifespan
    • DOI 10.1083/jcb.200212079
    • Muro AF, Chauhan AK, Gajovic S, Iaconcig A, Porro F, Stanta G, et al. Regulated splicing of the fibronectin EDA exon is essential for proper skin wound healing and normal lifespan. J Cell Biol. 2003 ; 162: 149-160 (Pubitemid 36859542)
    • (2003) Journal of Cell Biology , vol.162 , Issue.1 , pp. 149-160
    • Muro, A.F.1    Chauhan, A.K.2    Gajovic, S.3    Iaconcig, A.4    Porro, F.5    Stanta, G.6    Baralle, F.E.7
  • 84
    • 27744445885 scopus 로고    scopus 로고
    • Factors affecting soft tissue around dental implants: A review of the literature
    • DOI 10.1016/j.prosdent.2005.08.021, PII S0022391305004622
    • Myshin HL, Wiens JP. Factors affecting soft tissue around dental implants: a review of the literature. J Prosthet Dent. 2005 ; 94: 440-444 (Pubitemid 41586456)
    • (2005) Journal of Prosthetic Dentistry , vol.94 , Issue.5 , pp. 440-444
    • Myshin, H.L.1    Wiens, J.P.2
  • 85
    • 21744455891 scopus 로고    scopus 로고
    • Targeted deletion of the integrin β4 signaling domain suppresses laminin-5-dependent nuclear entry of mitogen-activated protein kinases and NF-κB, causing defects in epidermal growth and migration
    • DOI 10.1128/MCB.25.14.6090-6102.2005
    • Nikolopoulos SN, Blaikie P, Yoshioka T, Guo W, Puri C, Tacchetti C, et al. Targeted deletion of the integrin ß4 signaling domain suppresses laminin-5-dependent nuclear entry of mitogen-activated protein kinases and NF-?B, causing defects in epidermal growth and migration. Mol Cell Biol. 2005 ; 25: 6090-6102 (Pubitemid 40946560)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.14 , pp. 6090-6102
    • Nikolopoulos, S.N.1    Blaikie, P.2    Yoshioka, T.3    Guo, W.4    Puri, C.5    Tacchetti, C.6    Giancotti, F.G.7
  • 86
    • 0035544175 scopus 로고    scopus 로고
    • The junctional epithelium around murine teeth differs from gingival epithelium in its basement membrane composition
    • Oksonen J, Sorokin LM, Virtanen , Hormia M. The junctional epithelium around murine teeth differs from gingival epithelium in its basement membrane composition. J Dent Res. 2001 ; 80: 2093-2097
    • (2001) J Dent Res , vol.80 , pp. 2093-2097
    • Oksonen, J.1    Sorokin, L.M.2    Virtanen3    Hormia, M.4
  • 87
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • DOI 10.1242/jcs.00059
    • Pankov R, Yamada KM. Fibronectin at a glance. J Cell Sci. 2002 ; 115 (Pt 20). 3861-3863 (Pubitemid 35256486)
    • (2002) Journal of Cell Science , vol.115 , Issue.20 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 88
  • 89
    • 0030949650 scopus 로고    scopus 로고
    • The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix
    • DOI 10.1083/jcb.137.6.1445
    • Pilcher BK, Dumin JA, Sudbeck BD, Krane SM, Welgus HG, Parks WC. The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix. J Cell Biol. 1997 ; 137: 1445-1457 (Pubitemid 27265954)
    • (1997) Journal of Cell Biology , vol.137 , Issue.6 , pp. 1445-1457
    • Pilcher, B.K.1    Dumin, J.A.2    Sudbeck, B.D.3    Krane, S.M.4    Welgus, H.G.5    Parks, W.C.6
  • 91
    • 0034604845 scopus 로고    scopus 로고
    • Conditional ablation of ß1 integrin in skin. Severe defects in epidermal proliferation, basement membrane formation, and hair follicle invagination
    • Raghavan S, Bauer C, Mundschau G, Li Q, Fuchs E. Conditional ablation of ß1 integrin in skin. Severe defects in epidermal proliferation, basement membrane formation, and hair follicle invagination. J Cell Biol. 2000 ; 150: 1149-1160
    • (2000) J Cell Biol , vol.150 , pp. 1149-1160
    • Raghavan, S.1    Bauer, C.2    Mundschau, G.3    Li, Q.4    Fuchs, E.5
  • 94
    • 0033012926 scopus 로고    scopus 로고
    • Transforming growth factor-β1 up-regulates p15, p21 and p27 and blocks cell cycling in G1 in human prostate epithelium
    • DOI 10.1677/joe.0.1600257
    • Robson CN, Gnanapragasam V, Byrne RL, Collins AT, Neal DE. Transforming growth factor-ß1 up-regulates p15, p21 and p27 and blocks cell cycling in G1 in human prostate epithelium. J Endocrinol. 1999 ; 160: 257-266 (Pubitemid 29074696)
    • (1999) Journal of Endocrinology , vol.160 , Issue.2 , pp. 257-266
    • Robson, C.N.1    Gnanapragasam, V.2    Byrne, R.L.3    Collins, A.T.4    Neal, D.E.5
  • 95
    • 33748310729 scopus 로고    scopus 로고
    • The effect of material characteristics, of surface topography and of implant components and connections on soft tissue integration: A literature review
    • DOI 10.1111/j.1600-0501.2006.01367.x
    • Rompen E, Domken O, Degidi M, Pontes AE, Piattelli A. The effect of material characteristics, of surface topography and of implant components and connections on soft tissue integration: a literature review. Clin Oral Implants Res. 2006 ; 17 (Suppl 2). 55-67 (Pubitemid 44327698)
    • (2006) Clinical Oral Implants Research , vol.17 , Issue.SUPPL. 2 , pp. 55-67
    • Rompen, E.1    Domken, O.2    Degidi, M.3    Pontes, A.E.P.4    Piattelli, A.5
  • 96
    • 33645111120 scopus 로고    scopus 로고
    • Nine- to fourteen-year follow-up of implant treatment. Part II: Presence of peri-implant lesions
    • DOI 10.1111/j.1600-051X.2006.00906.x
    • Roos-Jansåker AM, Lindahl C, Renvert H, Renvert S. Nine- to fourteen-year follow-up of implant treatment. Part II: presence of peri-implant lesions. J Clin Periodontol. 2006 ; 33: 290-295 (Pubitemid 43439346)
    • (2006) Journal of Clinical Periodontology , vol.33 , Issue.4 , pp. 290-295
    • Roos-Jansaker, A.-M.1    Lindahl, C.2    Renvert, H.3    Renvert, S.4
  • 99
    • 0026198746 scopus 로고
    • Synthesis of type VIII collagen by epithelial cells of human gingiva
    • Salonen J, Oda D, Funk SE, Sage H. Synthesis of type VIII collagen by epithelial cells of human gingiva. J Periodontal Res. 1991 ; 26: 355-360
    • (1991) J Periodontal Res , vol.26 , pp. 355-360
    • Salonen, J.1    Oda, D.2    Funk, S.E.3    Sage, H.4
  • 100
    • 0026799402 scopus 로고
    • Targeted disruption of the mouse transforming growth factor-ß1 gene results in multifocal inflammatory disease
    • Shull MM, Ormsby I, Kier AB, Pawlowski S, Diebold RJ, Yin M, et al. Targeted disruption of the mouse transforming growth factor-ß1 gene results in multifocal inflammatory disease. Nature. 1992 ; 359: 693-699
    • (1992) Nature , vol.359 , pp. 693-699
    • Shull, M.M.1    Ormsby, I.2    Kier, A.B.3    Pawlowski, S.4    Diebold, R.J.5    Yin, M.6
  • 101
    • 77956289251 scopus 로고    scopus 로고
    • Roles of epithelial cell-derived periostin in TGF-beta activation, collagen production, and collagen gel elasticity in asthma
    • Sidhu SS, Yuan S, Innes AL, Kerr S, Woodruff PG, Hou L, et al. Roles of epithelial cell-derived periostin in TGF-beta activation, collagen production, and collagen gel elasticity in asthma. Proc Natl Acad Sci U S A. 2010 ; 107: 14170-14175
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 14170-14175
    • Sidhu, S.S.1    Yuan, S.2    Innes, A.L.3    Kerr, S.4    Woodruff, P.G.5    Hou, L.6
  • 102
    • 9744274523 scopus 로고    scopus 로고
    • The spatial and temporal expression patterns of integrin α9β1 and one of its ligands, the EIIIA segment of fibronectin, in cutaneous wound healing
    • DOI 10.1111/j.0022-202X.2004.23485.x
    • Singh P, Reimer CL, Peters JH, Stepp MA, Hynes RO, Van De Water L. The spatial and temporal expression patterns of integrin ?9ß1 and one of its ligands, the EIIIA segment of fibronectin, in cutaneous wound healing. J Invest Dermatol. 2004 ; 123: 1176-1181 (Pubitemid 39586843)
    • (2004) Journal of Investigative Dermatology , vol.123 , Issue.6 , pp. 1176-1181
    • Singh, P.1    Reimer, C.L.2    Peters, J.H.3    Stepp, M.A.4    Hynes, R.O.5    Van De Water, L.6
  • 103
    • 58149332702 scopus 로고    scopus 로고
    • Loss of integrin 9ß1 results in defects in proliferation, causing poor re-epithelialization during cutaneous wound healing
    • Singh P, Chen C, Pal-Ghosh S, Stepp MA, Sheppard D, Van De Water L. Loss of integrin 9ß1 results in defects in proliferation, causing poor re-epithelialization during cutaneous wound healing. J Invest Dermatol. 2009 ; 129: 217-228
    • (2009) J Invest Dermatol , vol.129 , pp. 217-228
    • Singh, P.1    Chen, C.2    Pal-Ghosh, S.3    Stepp, M.A.4    Sheppard, D.5    Van De Water, L.6
  • 104
    • 0031845096 scopus 로고    scopus 로고
    • Dynamics of basement membrane formation by keratinocyte-fibroblast interactions in organotypic skin culture
    • DOI 10.1006/excr.1997.3910
    • Smola H, Stark HJ, Thiekötter G, Mirancea N, Krieg T, Fusenig NE. Dynamics of basement membrane formation by keratinocyte-fibroblast interactions in organotypic skin culture. Exp Cell Res. 1998 ; 239: 399-410 (Pubitemid 28366640)
    • (1998) Experimental Cell Research , vol.239 , Issue.2 , pp. 399-410
    • Smola, H.1    Stark, H.-J.2    Thiekotter, G.3    Mirancea, N.4    Krieg, T.5    Fusenig, N.E.6
  • 105
    • 0027976521 scopus 로고
    • Latent transforming growth factor-β1 associates to fibroblast extracellular matrix via latent TGF-β binding protein
    • Taipale J, Miyazono K, Heldin CH, Keski-Oja J. Latent transforming growth factor-ß1 associates to fibroblast extracellular matrix via latent TGF-ß binding protein. J Cell Biol. 1994 ; 12: 171-181 (Pubitemid 24054619)
    • (1994) Journal of Cell Biology , vol.124 , Issue.1-2 , pp. 171-181
    • Taipale, J.1    Miyazono, K.2    Heldin, C.-H.3    Keski-Oja, J.4
  • 106
    • 33645299331 scopus 로고    scopus 로고
    • Vß6 integrin in wound healing and cancer of the oral cavity
    • Thomas GJ, Nyström ML, Marshall JF. vß6 integrin in wound healing and cancer of the oral cavity. J Oral Pathol Med. 2006 ; 35: 1-10
    • (2006) J Oral Pathol Med , vol.35 , pp. 1-10
    • Thomas, G.J.1    Nyström, M.L.2    Marshall, J.F.3
  • 108
    • 0037315708 scopus 로고    scopus 로고
    • Resolution of inflammation: A new paradigm for the pathogenesis of periodontal diseases
    • Van Dyke TE, Serhan CN. Resolution of inflammation: a new paradigm for the pathogenesis of periodontal diseases. J Dent Res. 2003 ; 82: 82-90 (Pubitemid 41764116)
    • (2003) Journal of Dental Research , vol.82 , Issue.2 , pp. 82-90
    • Van Dyke, T.E.1    Serhan, C.N.2
  • 109
    • 0036549082 scopus 로고    scopus 로고
    • Control of connective tissue gene expression by TGFß: Role of Smad proteins in fibrosis
    • Verrecchia F, Mauviel A. Control of connective tissue gene expression by TGFß: role of Smad proteins in fibrosis. Curr Rheumatol Rep. 2002 ; 4: 143-149
    • (2002) Curr Rheumatol Rep , vol.4 , pp. 143-149
    • Verrecchia, F.1    Mauviel, A.2
  • 110
    • 3042703866 scopus 로고    scopus 로고
    • TGF-β: The perpetrator of immune suppression by regulatory T cells and suicidal T cells
    • DOI 10.1189/jlb.1103539
    • Wahl SM, Swisher J, McCartney-Francis N, Chen W. TGF-ß: the perpetrator of immune suppression by regulatory T cells and suicidal T cells. J Leukoc Biol. 2004 ; 76: 15-24 (Pubitemid 38857166)
    • (2004) Journal of Leukocyte Biology , vol.76 , Issue.1 , pp. 15-24
    • Wahl, S.M.1    Swisher, J.2    McCartney-Francis, N.3    Chen, W.4
  • 112
    • 44349152315 scopus 로고    scopus 로고
    • Kindler syndrome and periodontal disease: Review of the literature and 12-year follow-up of treatment outcome
    • Wiebe CB, Petricca G, Häkkinen L, Jiang G, Wu C, Larjava H. Kindler syndrome and periodontal disease: review of the literature and 12-year follow-up of treatment outcome. J Periodontol. 2008 ; 79: 961-966
    • (2008) J Periodontol , vol.79 , pp. 961-966
    • Wiebe, C.B.1    Petricca, G.2    Häkkinen, L.3    Jiang, G.4    Wu, C.5    Larjava, H.6
  • 113
    • 34548477663 scopus 로고    scopus 로고
    • Serine phosphorylation of the integrin β4 subunit is necessary for epidermal growth factor receptor-induced hemidesmosome disruption
    • DOI 10.1091/mbc.E07-04-0306
    • Wilhelmsen K, Litjens SH, Kuikman I, Margadant C, van Rheenen J, Sonnenberg A. Serine phosphorylation of the integrin ß4 subunit is necessary for epidermal growth factor receptor induced hemidesmosome disruption. Mol Biol Cell. 2007 ; 18: 3512-3522 (Pubitemid 47378689)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.9 , pp. 3512-3522
    • Wilhelmsen, K.1    Litjens, S.H.M.2    Kuikman, I.3    Margadant, C.4    Van Rheenen, J.5    Sonnenberg, A.6
  • 114
    • 70349159900 scopus 로고    scopus 로고
    • Wound healing in oral mucosa results in reduced scar formation as compared with skin: Evidence from the red Duroc pig model and humans
    • Wong JW, Gallant-Behm C, Wiebe C, Mak K, Hart DA, Larjava H, et al. Wound healing in oral mucosa results in reduced scar formation as compared with skin: evidence from the red Duroc pig model and humans. Wound Repair Regen. 2009 ; 17: 717-729
    • (2009) Wound Repair Regen , vol.17 , pp. 717-729
    • Wong, J.W.1    Gallant-Behm, C.2    Wiebe, C.3    Mak, K.4    Hart, D.A.5    Larjava, H.6
  • 115
    • 65949105729 scopus 로고    scopus 로고
    • Mice lacking ß6 integrin in skin show accelerated wound repair in dexamethasone impaired wound healing model
    • Xie Y, Gao K, Häkkinen L, Larjava H. Mice lacking ß6 integrin in skin show accelerated wound repair in dexamethasone impaired wound healing model. Wound Repair Regen. 2009 ; 17: 326-339
    • (2009) Wound Repair Regen , vol.17 , pp. 326-339
    • Xie, Y.1    Gao, K.2    Häkkinen, L.3    Larjava, H.4
  • 116
    • 0344026029 scopus 로고    scopus 로고
    • Active transforming growth factor-β in wound repair: Determination using a new assay
    • Yang L, Qiu CX, Ludlow A, Ferguson MW, Brunner G. Active transforming growth factor-ß in wound repair: determination using a new assay. Am J Pathol. 1999 ; 154: 105-111 (Pubitemid 29031617)
    • (1999) American Journal of Pathology , vol.154 , Issue.1 , pp. 105-111
    • Yang, L.1    Qui, C.X.2    Ludlow, A.3    Ferguson, M.W.J.4    Brunner, G.5
  • 117
    • 33947265169 scopus 로고    scopus 로고
    • Absence of integrin-mediated TGFβ1 activation in vivo recapitulates the phenotype of TGFβ1-null mice
    • DOI 10.1083/jcb.200611044
    • Yang Z, Mu Z, Dabovic B, Jurukovski V, Yu D, Sung J, et al. Absence of integrin-mediated TGFß1 activation in vivo recapitulates the phenotype of TGFß1-null mice. J Cell Biol. 2007 ; 176: 787-793 (Pubitemid 46425539)
    • (2007) Journal of Cell Biology , vol.176 , Issue.6 , pp. 787-793
    • Yang, Z.1    Mu, Z.2    Dabovic, B.3    Jurukovski, V.4    Yu, D.5    Sung, J.6    Xiong, X.7    Munger, J.S.8
  • 118
    • 0028171068 scopus 로고
    • The integrin 9ß1 mediates cell attachment to a non-RGD site in the third fibronectin type III repeat of tenascin
    • Yokosaki Y, Palmer EL, Prieto AL, Crossin KL, Bourdon MA, Pytela R, et al. The integrin 9ß1 mediates cell attachment to a non-RGD site in the third fibronectin type III repeat of tenascin. J Biol Chem. 1994 ; 269: 26691-26696
    • (1994) J Biol Chem , vol.269 , pp. 26691-26696
    • Yokosaki, Y.1    Palmer, E.L.2    Prieto, A.L.3    Crossin, K.L.4    Bourdon, M.A.5    Pytela, R.6
  • 119
    • 0030587422 scopus 로고    scopus 로고
    • Laminin 5 deposition promotes keratinocyte motility
    • DOI 10.1006/excr.1996.0280
    • Zhang K, Kramer RH. Laminin 5 deposition promotes keratinocyte motility. Exp Cell Res. 1996 ; 227: 309-322 (Pubitemid 26320173)
    • (1996) Experimental Cell Research , vol.227 , Issue.2 , pp. 309-322
    • Zhang, K.1    Kramer, R.H.2
  • 120
    • 0027175838 scopus 로고
    • The αvβ1 integrin functions as a fibronectin receptor but does not support fibronectin matrix assembly and cell migration on fibronectin
    • Zhang Z, Morla AO, Vuori K, Bauer JS, Juliano RL, Ruoslahti E. The ?vß1 integrin functions as a fibronectin receptor but does not support fibronectin matrix assembly and cell migration on fibronectin. J Cell Biol. 1993 ; 122: 235-242 (Pubitemid 23188814)
    • (1993) Journal of Cell Biology , vol.122 , Issue.1 , pp. 235-242
    • Zhang, Z.1    Morla, A.O.2    Vuori, K.3    Bauer, J.S.4    Juliano, R.L.5    Ruoslahti, E.6


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