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Volumn 1833, Issue 6, 2013, Pages 1304-1315

Molecular mechanism of transglutaminase-2 in corneal epithelial migration and adhesion

Author keywords

Adhesion; Cornea; Epithelium; Migration; Transglutaminase; Wound healing

Indexed keywords

BETA3 INTEGRIN; FOCAL ADHESION KINASE; PAXILLIN; PROTEIN CDC42; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; RAC PROTEIN; SHORT HAIRPIN RNA; VINCULIN;

EID: 84875678759     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.02.030     Document Type: Article
Times cited : (23)

References (40)
  • 1
    • 32844467408 scopus 로고    scopus 로고
    • Tissue transglutaminase: from biological glue to cell survival cues
    • Mehta K., Fok J.Y., Mangala L.S. Tissue transglutaminase: from biological glue to cell survival cues. Front. Biosci. 2006, 11:173-185.
    • (2006) Front. Biosci. , vol.11 , pp. 173-185
    • Mehta, K.1    Fok, J.Y.2    Mangala, L.S.3
  • 2
    • 38649141890 scopus 로고    scopus 로고
    • Cross-linking transglutaminases with G protein-coupled receptor signaling
    • Iismaa S.E., Begg G.E., Graham R.M. Cross-linking transglutaminases with G protein-coupled receptor signaling. Sci. STKE 2006, 2006:pe34.
    • (2006) Sci. STKE , vol.2006
    • Iismaa, S.E.1    Begg, G.E.2    Graham, R.M.3
  • 3
    • 67651071286 scopus 로고    scopus 로고
    • Transglutaminases and disease: lessons from genetically engineered mouse models and inherited disorders
    • Iismaa S.E., Mearns B.M., Lorand L., Graham R.M. Transglutaminases and disease: lessons from genetically engineered mouse models and inherited disorders. Physiol. Rev. 2009, 89:991-1023.
    • (2009) Physiol. Rev. , vol.89 , pp. 991-1023
    • Iismaa, S.E.1    Mearns, B.M.2    Lorand, L.3    Graham, R.M.4
  • 4
    • 0032728955 scopus 로고    scopus 로고
    • Regulation of cell surface tissue transglutaminase: effects on matrix storage of latent transforming growth factor-beta binding protein-1
    • Verderio E., Gaudry C., Gross S., Smith C., Downes S., Griffin M. Regulation of cell surface tissue transglutaminase: effects on matrix storage of latent transforming growth factor-beta binding protein-1. J. Histochem. Cytochem. 1999, 47:1417-1432.
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 1417-1432
    • Verderio, E.1    Gaudry, C.2    Gross, S.3    Smith, C.4    Downes, S.5    Griffin, M.6
  • 5
    • 0034695929 scopus 로고    scopus 로고
    • Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin
    • Akimov S.S., Krylov D., Fleischman L.F., Belkin A.M. Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin. J. Cell Biol. 2000, 148:825-838.
    • (2000) J. Cell Biol. , vol.148 , pp. 825-838
    • Akimov, S.S.1    Krylov, D.2    Fleischman, L.F.3    Belkin, A.M.4
  • 6
  • 7
    • 18244399091 scopus 로고    scopus 로고
    • Transglutaminase-mediated oligomerization of the fibrin(ogen) alphaC domains promotes integrin-dependent cell adhesion and signaling
    • Belkin A.M., Tsurupa G., Zemskov E., Veklich Y., Weisel J.W., Medved L. Transglutaminase-mediated oligomerization of the fibrin(ogen) alphaC domains promotes integrin-dependent cell adhesion and signaling. Blood 2005, 105:3561-3568.
    • (2005) Blood , vol.105 , pp. 3561-3568
    • Belkin, A.M.1    Tsurupa, G.2    Zemskov, E.3    Veklich, Y.4    Weisel, J.W.5    Medved, L.6
  • 8
    • 0035469864 scopus 로고    scopus 로고
    • Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin
    • Akimov S.S., Belkin A.M. Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin. Blood 2001, 98:1567-1576.
    • (2001) Blood , vol.98 , pp. 1567-1576
    • Akimov, S.S.1    Belkin, A.M.2
  • 9
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: crosslinking enzymes with pleiotropic functions
    • Lorand L., Graham R.M. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat. Rev. Mol. Cell Biol. 2003, 4:140-156.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 10
    • 0142242157 scopus 로고    scopus 로고
    • A novel RGD-independent cell adhesion pathway mediated by fibronectin-bound tissue transglutaminase rescues cells from anoikis
    • Verderio E.A., Telci D., Okoye A., Melino G., Griffin M. A novel RGD-independent cell adhesion pathway mediated by fibronectin-bound tissue transglutaminase rescues cells from anoikis. J. Biol. Chem. 2003, 278:42604-42614.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42604-42614
    • Verderio, E.A.1    Telci, D.2    Okoye, A.3    Melino, G.4    Griffin, M.5
  • 12
    • 0037252190 scopus 로고    scopus 로고
    • Novel transglutaminase inhibitors reverse the inflammation of allergic conjunctivitis
    • Sohn J., Kim T.I., Yoon Y.H., Kim J.Y., Kim S.Y. Novel transglutaminase inhibitors reverse the inflammation of allergic conjunctivitis. J. Clin. Invest. 2003, 111:121-128.
    • (2003) J. Clin. Invest. , vol.111 , pp. 121-128
    • Sohn, J.1    Kim, T.I.2    Yoon, Y.H.3    Kim, J.Y.4    Kim, S.Y.5
  • 13
    • 0032086817 scopus 로고    scopus 로고
    • Glutathione transferase (class pi) and tissue transglutaminase (Tgase C) expression in pterygia
    • Kim Y.J., Park E.S., Song K.Y., Park S.C., Kim J.C. Glutathione transferase (class pi) and tissue transglutaminase (Tgase C) expression in pterygia. Korean J. Ophthalmol. 1998, 12:6-13.
    • (1998) Korean J. Ophthalmol. , vol.12 , pp. 6-13
    • Kim, Y.J.1    Park, E.S.2    Song, K.Y.3    Park, S.C.4    Kim, J.C.5
  • 14
    • 0742321779 scopus 로고    scopus 로고
    • Expression and distribution of tissue transglutaminase in normal and injured rat cornea
    • Zhang W., Shiraishi A., Suzuki A., Zheng X., Kodama T., Ohashi Y. Expression and distribution of tissue transglutaminase in normal and injured rat cornea. Curr. Eye Res. 2004, 28:37-45.
    • (2004) Curr. Eye Res. , vol.28 , pp. 37-45
    • Zhang, W.1    Shiraishi, A.2    Suzuki, A.3    Zheng, X.4    Kodama, T.5    Ohashi, Y.6
  • 15
    • 4143089161 scopus 로고    scopus 로고
    • Tissue transglutaminase in normal and abnormal wound healing: review article
    • Verderio E.A., Johnson T., Griffin M. Tissue transglutaminase in normal and abnormal wound healing: review article. Amino Acids 2004, 26:387-404.
    • (2004) Amino Acids , vol.26 , pp. 387-404
    • Verderio, E.A.1    Johnson, T.2    Griffin, M.3
  • 16
    • 39549104795 scopus 로고    scopus 로고
    • Role of JNK-dependent serine phosphorylation of paxillin in migration of corneal epithelial cells during wound closure
    • Kimura K., Teranishi S., Yamauchi J., Nishida T. Role of JNK-dependent serine phosphorylation of paxillin in migration of corneal epithelial cells during wound closure. Invest. Ophthalmol. Vis. Sci. 2008, 49:125-132.
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , pp. 125-132
    • Kimura, K.1    Teranishi, S.2    Yamauchi, J.3    Nishida, T.4
  • 17
    • 33745373374 scopus 로고    scopus 로고
    • Cell surface transglutaminase promotes RhoA activation via integrin clustering and suppression of the Src-p190RhoGAP signaling pathway
    • Janiak A., Zemskov E.A., Belkin A.M. Cell surface transglutaminase promotes RhoA activation via integrin clustering and suppression of the Src-p190RhoGAP signaling pathway. Mol. Biol. Cell 2006, 17:1606-1619.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1606-1619
    • Janiak, A.1    Zemskov, E.A.2    Belkin, A.M.3
  • 20
    • 78650642603 scopus 로고    scopus 로고
    • Hyperosmolarity mediated mitochondrial dysfunction requires transglutaminase-2 in human corneal epithelial cells
    • Png E., Samivelu G.K., Yeo S.H., Chew J., Chaurasia S.S., Tong L. Hyperosmolarity mediated mitochondrial dysfunction requires transglutaminase-2 in human corneal epithelial cells. J. Cell. Physiol. 2010, 226:693-699.
    • (2010) J. Cell. Physiol. , vol.226 , pp. 693-699
    • Png, E.1    Samivelu, G.K.2    Yeo, S.H.3    Chew, J.4    Chaurasia, S.S.5    Tong, L.6
  • 22
    • 61849171644 scopus 로고    scopus 로고
    • Calcium-binding S100 protein expression in pterygium
    • Riau A.K., Wong T.T., Beuerman R.W., Tong L. Calcium-binding S100 protein expression in pterygium. Mol. Vis. 2009, 15:335-342.
    • (2009) Mol. Vis. , vol.15 , pp. 335-342
    • Riau, A.K.1    Wong, T.T.2    Beuerman, R.W.3    Tong, L.4
  • 23
    • 33646870587 scopus 로고    scopus 로고
    • Corneal integrins and their functions
    • Stepp M.A. Corneal integrins and their functions. Exp. Eye Res. 2006, 83:3-15.
    • (2006) Exp. Eye Res. , vol.83 , pp. 3-15
    • Stepp, M.A.1
  • 24
    • 42049092972 scopus 로고    scopus 로고
    • Regulation of actin assembly associated with protrusion and adhesion in cell migration
    • Le Clainche C., Carlier M.F. Regulation of actin assembly associated with protrusion and adhesion in cell migration. Physiol. Rev. 2008, 88:489-513.
    • (2008) Physiol. Rev. , vol.88 , pp. 489-513
    • Le Clainche, C.1    Carlier, M.F.2
  • 25
    • 1542742158 scopus 로고    scopus 로고
    • TGF-beta2-induced cell surface tissue transglutaminase increases adhesion and migration of RPE cells on fibronectin through the gelatin-binding domain
    • Priglinger S.G., Alge C.S., Neubauer A.S., Kristin N., Hirneiss C., Eibl K., Kampik A., Welge-Lussen U. TGF-beta2-induced cell surface tissue transglutaminase increases adhesion and migration of RPE cells on fibronectin through the gelatin-binding domain. Invest. Ophthalmol. Vis. Sci. 2004, 45:955-963.
    • (2004) Invest. Ophthalmol. Vis. Sci. , vol.45 , pp. 955-963
    • Priglinger, S.G.1    Alge, C.S.2    Neubauer, A.S.3    Kristin, N.4    Hirneiss, C.5    Eibl, K.6    Kampik, A.7    Welge-Lussen, U.8
  • 26
    • 0010115712 scopus 로고    scopus 로고
    • Reduced expression of tissue transglutaminase in a human endothelial cell line leads to changes in cell spreading, cell adhesion and reduced polymerisation of fibronectin
    • Jones R.A., Nicholas B., Mian S., Davies P.J., Griffin M. Reduced expression of tissue transglutaminase in a human endothelial cell line leads to changes in cell spreading, cell adhesion and reduced polymerisation of fibronectin. J. Cell Sci. 1997, 110(Pt 19):2461-2472.
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 19 , pp. 2461-2472
    • Jones, R.A.1    Nicholas, B.2    Mian, S.3    Davies, P.J.4    Griffin, M.5
  • 27
    • 62949131510 scopus 로고    scopus 로고
    • Enhanced osteoblast adhesion on transglutaminase 2-crosslinked fibronectin
    • Forsprecher J., Wang Z., Nelea V., Kaartinen M.T. Enhanced osteoblast adhesion on transglutaminase 2-crosslinked fibronectin. Amino Acids 2009, 36:747-753.
    • (2009) Amino Acids , vol.36 , pp. 747-753
    • Forsprecher, J.1    Wang, Z.2    Nelea, V.3    Kaartinen, M.T.4
  • 28
    • 26844581609 scopus 로고    scopus 로고
    • Tissue transglutaminase-induced alterations in extracellular matrix inhibit tumor invasion
    • Mangala L.S., Arun B., Sahin A.A., Mehta K. Tissue transglutaminase-induced alterations in extracellular matrix inhibit tumor invasion. Mol. Cancer 2005, 4:33.
    • (2005) Mol. Cancer , vol.4 , pp. 33
    • Mangala, L.S.1    Arun, B.2    Sahin, A.A.3    Mehta, K.4
  • 30
  • 31
    • 34147140579 scopus 로고    scopus 로고
    • Structure-function analysis reveals discrete beta3 integrin inside-out and outside-in signaling pathways in platelets
    • Zou Z., Chen H., Schmaier A.A., Hynes R.O., Kahn M.L. Structure-function analysis reveals discrete beta3 integrin inside-out and outside-in signaling pathways in platelets. Blood 2007, 109:3284-3290.
    • (2007) Blood , vol.109 , pp. 3284-3290
    • Zou, Z.1    Chen, H.2    Schmaier, A.A.3    Hynes, R.O.4    Kahn, M.L.5
  • 32
    • 0029916875 scopus 로고    scopus 로고
    • Outside-in integrin signal transduction. Alpha IIb beta 3-(GP IIb IIIa) tyrosine phosphorylation induced by platelet aggregation
    • Law D.A., Nannizzi-Alaimo L., Phillips D.R. Outside-in integrin signal transduction. Alpha IIb beta 3-(GP IIb IIIa) tyrosine phosphorylation induced by platelet aggregation. J. Biol. Chem. 1996, 271:10811-10815.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10811-10815
    • Law, D.A.1    Nannizzi-Alaimo, L.2    Phillips, D.R.3
  • 33
    • 0030612268 scopus 로고    scopus 로고
    • Requirement of integrin beta3 tyrosine 747 for beta3 tyrosine phosphorylation and regulation of alphavbeta3 avidity
    • Blystone S.D., Williams M.P., Slater S.E., Brown E.J. Requirement of integrin beta3 tyrosine 747 for beta3 tyrosine phosphorylation and regulation of alphavbeta3 avidity. J. Biol. Chem. 1997, 272:28757-28761.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28757-28761
    • Blystone, S.D.1    Williams, M.P.2    Slater, S.E.3    Brown, E.J.4
  • 35
    • 33748994545 scopus 로고    scopus 로고
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • Ridley A.J. Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking. Trends Cell Biol. 2006, 16:522-529.
    • (2006) Trends Cell Biol. , vol.16 , pp. 522-529
    • Ridley, A.J.1
  • 36
    • 1542373753 scopus 로고    scopus 로고
    • Coactivation of Rac1 and Cdc42 at lamellipodia and membrane ruffles induced by epidermal growth factor
    • Kurokawa K., Itoh R.E., Yoshizaki H., Nakamura Y.O., Matsuda M. Coactivation of Rac1 and Cdc42 at lamellipodia and membrane ruffles induced by epidermal growth factor. Mol. Biol. Cell 2004, 15:1003-1010.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1003-1010
    • Kurokawa, K.1    Itoh, R.E.2    Yoshizaki, H.3    Nakamura, Y.O.4    Matsuda, M.5
  • 37
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes C.D., Hall A. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 1995, 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 38
    • 0033024366 scopus 로고    scopus 로고
    • Keratocyte and fibroblast phenotypes in the repairing cornea
    • Fini M.E. Keratocyte and fibroblast phenotypes in the repairing cornea. Prog. Retin. Eye Res. 1999, 18:529-551.
    • (1999) Prog. Retin. Eye Res. , vol.18 , pp. 529-551
    • Fini, M.E.1
  • 39
    • 0041326360 scopus 로고    scopus 로고
    • Corneal cells: chatty in development, homeostasis, wound healing, and disease
    • Wilson S.E., Netto M., Ambrosio R. Corneal cells: chatty in development, homeostasis, wound healing, and disease. Am. J. Ophthalmol. 2003, 136:530-536.
    • (2003) Am. J. Ophthalmol. , vol.136 , pp. 530-536
    • Wilson, S.E.1    Netto, M.2    Ambrosio, R.3
  • 40
    • 0030793696 scopus 로고    scopus 로고
    • Adhesion of fibroblasts to fibronectin stimulates both serine and tyrosine phosphorylation of paxillin
    • Bellis S.L., Perrotta J.A., Curtis M.S., Turner C.E. Adhesion of fibroblasts to fibronectin stimulates both serine and tyrosine phosphorylation of paxillin. Biochem. J. 1997, 325(Pt 2):375-381.
    • (1997) Biochem. J. , vol.325 , Issue.PART 2 , pp. 375-381
    • Bellis, S.L.1    Perrotta, J.A.2    Curtis, M.S.3    Turner, C.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.