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Volumn 47, Issue 5, 2006, Pages 1862-1868

Promotion of corneal epithelial wound healing in vitro and in vivo by annexin A5

Author keywords

[No Author keywords available]

Indexed keywords

LIPOCORTIN 5; ENZYME INHIBITOR; UROKINASE;

EID: 33744732720     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: 10.1167/iovs.05-0591     Document Type: Article
Times cited : (26)

References (56)
  • 1
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins
    • Raynal P, Pollard HB. Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim Biophys Acta. 1994;1197:63-93.
    • (1994) Biochim Biophys Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 2
    • 0004922523 scopus 로고    scopus 로고
    • Calcium-binding proteins: Annexins
    • Carafoli E, Klee CB, eds, New York: Oxford University Press;
    • Liemann S, Benz J, Huber R. Calcium-binding proteins: annexins. In: Carafoli E, Klee CB, eds. Calcium as a Cellular Regulator. New York: Oxford University Press; 1999:100-122.
    • (1999) Calcium as a Cellular Regulator , pp. 100-122
    • Liemann, S.1    Benz, J.2    Huber, R.3
  • 3
    • 0034912352 scopus 로고    scopus 로고
    • Annexins: Key regulators of haemostasis, thrombosis, and apoptosis
    • Reutelingsperger CPM. Annexins: key regulators of haemostasis, thrombosis, and apoptosis. Thromb Haemost. 2001;86:413-419.
    • (2001) Thromb Haemost , vol.86 , pp. 413-419
    • Reutelingsperger, C.P.M.1
  • 4
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Gerke V, Moss SE. Annexins: from structure to function. Physiol Rev. 2002;82:331-371.
    • (2002) Physiol Rev , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 5
    • 18744437417 scopus 로고
    • Structure and expression of cDNA for an inhibitor of blood coagulation isolated from human placenta: A new lipocortin-like protein
    • Iwasaki A, Suda M, Nakao H, et al. Structure and expression of cDNA for an inhibitor of blood coagulation isolated from human placenta: a new lipocortin-like protein. J Biochem (Tokyo). 1987;102:1261-1273.
    • (1987) J Biochem (Tokyo) , vol.102 , pp. 1261-1273
    • Iwasaki, A.1    Suda, M.2    Nakao, H.3
  • 6
    • 0025195030 scopus 로고
    • 2+-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins
    • 2+-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins. Biochem J. 1990;266:195-200.
    • (1990) Biochem J , vol.266 , pp. 195-200
    • Blackwood, R.A.1    Ernst, J.D.2
  • 9
  • 10
    • 0032521601 scopus 로고    scopus 로고
    • Annexin V inhibits protein kinase C activity via a mechanism of phospholipid sequestration
    • Dubois T, Mira JP, Feliers D, Solito E, Russo-Marie F, Oudinet JP. Annexin V inhibits protein kinase C activity via a mechanism of phospholipid sequestration. Biochem J. 1998;330:1277-1282.
    • (1998) Biochem J , vol.330 , pp. 1277-1282
    • Dubois, T.1    Mira, J.P.2    Feliers, D.3    Solito, E.4    Russo-Marie, F.5    Oudinet, J.P.6
  • 11
    • 0025635905 scopus 로고
    • Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes
    • Rojas E, Pollard HB, Haigler HT, Parra C, Burns AL. Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes. J Biol Chem. 1990;265:21207-21215.
    • (1990) J Biol Chem , vol.265 , pp. 21207-21215
    • Rojas, E.1    Pollard, H.B.2    Haigler, H.T.3    Parra, C.4    Burns, A.L.5
  • 12
    • 0027411175 scopus 로고
    • Calcium influx through annexin V ion channels into large unilamellar vesicles measured with fura-2
    • Berendes R, Burger A, Voges D, Demange P, Huber R. Calcium influx through annexin V ion channels into large unilamellar vesicles measured with fura-2. FEBS Lett. 1993;317:131-134.
    • (1993) FEBS Lett , vol.317 , pp. 131-134
    • Berendes, R.1    Burger, A.2    Voges, D.3    Demange, P.4    Huber, R.5
  • 13
    • 0034634693 scopus 로고    scopus 로고
    • The roles of annexins and types II and X collagen in matrix vesicle-mediated mineralization of growth plate cartilage
    • Kirsch T, Harrison G, Golub EE, Nah HD. The roles of annexins and types II and X collagen in matrix vesicle-mediated mineralization of growth plate cartilage. J Biol Chem. 2000;275:35577-35583.
    • (2000) J Biol Chem , vol.275 , pp. 35577-35583
    • Kirsch, T.1    Harrison, G.2    Golub, E.E.3    Nah, H.D.4
  • 14
    • 34248639270 scopus 로고    scopus 로고
    • Annexins and tissue mineralization: Matrix vesicles, ion channel activity of annexins and annexin V/collagen interactions
    • Bandorowicz-Pikula J, ed, New York: Kluwer Academic/Plenum;
    • Kirsch T. Annexins and tissue mineralization: matrix vesicles, ion channel activity of annexins and annexin V/collagen interactions. In: Bandorowicz-Pikula J, ed. Annexins: Biological Importance and Annexin-Related Pathologies. New York: Kluwer Academic/Plenum; 2003:172-181.
    • (2003) Annexins: Biological Importance and Annexin-Related Pathologies , pp. 172-181
    • Kirsch, T.1
  • 16
    • 0028133089 scopus 로고
    • A new function of calphobindin I (annexin V). Promotion of both migration and urokinase-type plasminogen activator activity of normal human keratinocytes
    • Nakao H, Watanabe M, Maki M. A new function of calphobindin I (annexin V). Promotion of both migration and urokinase-type plasminogen activator activity of normal human keratinocytes. Eur J Biochem. 1994;223:901-908.
    • (1994) Eur J Biochem , vol.223 , pp. 901-908
    • Nakao, H.1    Watanabe, M.2    Maki, M.3
  • 17
    • 0037370196 scopus 로고    scopus 로고
    • Cell-matrix and cell-cell interactions during corneal epithelial wound healing
    • Suzuki K, Saito J, Yanai R, et al. Cell-matrix and cell-cell interactions during corneal epithelial wound healing. Prog Retin Eye Res. 2003;22:113-133.
    • (2003) Prog Retin Eye Res , vol.22 , pp. 113-133
    • Suzuki, K.1    Saito, J.2    Yanai, R.3
  • 18
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger DA, Horwitz AF. Cell migration: a physically integrated molecular process. Cell. 1996;84:359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 19
    • 0031964022 scopus 로고    scopus 로고
    • Cell migration: Regulation of force on extracellular-matrix-integrin complexes
    • Sheetz MP, Felsenfeld DP, Galbraith CG. Cell migration: regulation of force on extracellular-matrix-integrin complexes. Trends Cell Biol. 1998;8:51-54.
    • (1998) Trends Cell Biol , vol.8 , pp. 51-54
    • Sheetz, M.P.1    Felsenfeld, D.P.2    Galbraith, C.G.3
  • 20
    • 0024426006 scopus 로고
    • The pathogenesis of corneal epithelial defects
    • Berman M. The pathogenesis of corneal epithelial defects. Acta Ophthalmol. 1989;192:55-64.
    • (1989) Acta Ophthalmol , vol.192 , pp. 55-64
    • Berman, M.1
  • 22
    • 0023229547 scopus 로고
    • Human urokinase-type plasminogen activator stimulates chemotaxis of human neutrophils
    • Gudewicz PW, Gilboa N. Human urokinase-type plasminogen activator stimulates chemotaxis of human neutrophils. Biochem Biophys Res Commun. 1987;147:1176-1181.
    • (1987) Biochem Biophys Res Commun , vol.147 , pp. 1176-1181
    • Gudewicz, P.W.1    Gilboa, N.2
  • 23
    • 0027219030 scopus 로고
    • Urokinase-urokinase receptor interaction: Non-mitogenic signal transduction in human epidermal cells
    • Del Rosso M, Anichini E, Pedersen N, et al. Urokinase-urokinase receptor interaction: non-mitogenic signal transduction in human epidermal cells. Biochem Biophys Res Commun. 1993;190:347-352.
    • (1993) Biochem Biophys Res Commun , vol.190 , pp. 347-352
    • Del Rosso, M.1    Anichini, E.2    Pedersen, N.3
  • 24
    • 0029799088 scopus 로고    scopus 로고
    • Contrasting effects of plasminogen activators, urokinase receptor, and LDL receptor-related protein on smooth muscle cell migration and invasion
    • Okada SS, Grobmyer SR, Barnathan ES. Contrasting effects of plasminogen activators, urokinase receptor, and LDL receptor-related protein on smooth muscle cell migration and invasion. Arterioscler Thromb Vasc Biol. 1996;16:1269-1276.
    • (1996) Arterioscler Thromb Vasc Biol , vol.16 , pp. 1269-1276
    • Okada, S.S.1    Grobmyer, S.R.2    Barnathan, E.S.3
  • 25
    • 0029923744 scopus 로고    scopus 로고
    • Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect
    • Resnati M, Guttinger M, Valcamonica S, Sidenius N, Blasi F, Fazioli F. Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect. EMBO J. 1996;15:1572-1582.
    • (1996) EMBO J , vol.15 , pp. 1572-1582
    • Resnati, M.1    Guttinger, M.2    Valcamonica, S.3    Sidenius, N.4    Blasi, F.5    Fazioli, F.6
  • 26
    • 0032748523 scopus 로고    scopus 로고
    • Proteolysis, cell adhesion, chemotaxis, and invasiveness are regulated by the u-PA-u-PAR-PAI-1 system
    • Blasi F. Proteolysis, cell adhesion, chemotaxis, and invasiveness are regulated by the u-PA-u-PAR-PAI-1 system. Thromb Haemost. 1999;82:298-304.
    • (1999) Thromb Haemost , vol.82 , pp. 298-304
    • Blasi, F.1
  • 27
    • 0027480649 scopus 로고
    • Role of urokinase type plasminogen activator (u-PA) in corneal epithelial migration
    • Morimoto K, Mishima H, Nishida T, Otori T. Role of urokinase type plasminogen activator (u-PA) in corneal epithelial migration. Thromb Haemost. 1993;69:387-391.
    • (1993) Thromb Haemost , vol.69 , pp. 387-391
    • Morimoto, K.1    Mishima, H.2    Nishida, T.3    Otori, T.4
  • 28
    • 0042844825 scopus 로고    scopus 로고
    • Up-regulation of urokinase-type plasminogen activator in corneal epithelial cells induced by wounding
    • Watanabe M, Yano W, Kondo S, et al. Up-regulation of urokinase-type plasminogen activator in corneal epithelial cells induced by wounding. Invest Ophthalmol Vis Sci. 2003;44:3332-3338.
    • (2003) Invest Ophthalmol Vis Sci , vol.44 , pp. 3332-3338
    • Watanabe, M.1    Yano, W.2    Kondo, S.3
  • 29
    • 0019941062 scopus 로고
    • A technique for obtaining sheets of intact rabbit corneal epithelium
    • Gipson IK, Grill SM. A technique for obtaining sheets of intact rabbit corneal epithelium. Invest Ophthalmol Vis Sci. 1982;23:269-273.
    • (1982) Invest Ophthalmol Vis Sci , vol.23 , pp. 269-273
    • Gipson, I.K.1    Grill, S.M.2
  • 30
    • 0023950512 scopus 로고
    • Chemotactic and haptotactic activities of fibronectin for cultured rabbit corneal epithelial cells
    • Watanabe K, Nakagawa S, Nishida T. Chemotactic and haptotactic activities of fibronectin for cultured rabbit corneal epithelial cells. Invest Ophthalmol Vis Sci. 1988;29:572-577.
    • (1988) Invest Ophthalmol Vis Sci , vol.29 , pp. 572-577
    • Watanabe, K.1    Nakagawa, S.2    Nishida, T.3
  • 31
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • Heussen C, Dowdle EB. Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal Biochem. 1980;102:196-202.
    • (1980) Anal Biochem , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 32
    • 0025368805 scopus 로고
    • Urokinase-type plasminogen activator in rabbit tears. Comparison with human tears
    • Tozser J, Berta A. Urokinase-type plasminogen activator in rabbit tears. Comparison with human tears. Exp Eye Res. 1990;51:33-37.
    • (1990) Exp Eye Res , vol.51 , pp. 33-37
    • Tozser, J.1    Berta, A.2
  • 35
    • 0021332294 scopus 로고
    • Comparison of the effects of EGF, pFGF and EDGF on corneal epithelium wound healing
    • Petroutsos G, Courty J, Guimaraes R, et al. Comparison of the effects of EGF, pFGF and EDGF on corneal epithelium wound healing. Curr Eye Res. 1984;3:593-598.
    • (1984) Curr Eye Res , vol.3 , pp. 593-598
    • Petroutsos, G.1    Courty, J.2    Guimaraes, R.3
  • 36
  • 37
  • 38
    • 0028236005 scopus 로고
    • Effect of topical beta blockers on corneal epithelial wound healing in the rabbit
    • Reidy JJ, Zarzour J, Thompson HW, Beuerman RW. Effect of topical beta blockers on corneal epithelial wound healing in the rabbit. Br J Ophthalmol. 1994;78:377-380.
    • (1994) Br J Ophthalmol , vol.78 , pp. 377-380
    • Reidy, J.J.1    Zarzour, J.2    Thompson, H.W.3    Beuerman, R.W.4
  • 39
    • 0033991556 scopus 로고    scopus 로고
    • Growth factors: Importance in wound healing and maintenance of transparency of the cornea
    • Imanishi J, Kamiyama K, Iguchi I, et al. Growth factors: importance in wound healing and maintenance of transparency of the cornea. Prog Retin Eye Res. 2000;19:113-129.
    • (2000) Prog Retin Eye Res , vol.19 , pp. 113-129
    • Imanishi, J.1    Kamiyama, K.2    Iguchi, I.3
  • 40
    • 0030957841 scopus 로고    scopus 로고
    • Effects of mucin ophthalmic solution on epithelial wound healing in rabbit cornea
    • Sigemitsu T, Shimizu Y, Majima Y. Effects of mucin ophthalmic solution on epithelial wound healing in rabbit cornea. Ophthalmic Res. 1997;29:61-66.
    • (1997) Ophthalmic Res , vol.29 , pp. 61-66
    • Sigemitsu, T.1    Shimizu, Y.2    Majima, Y.3
  • 41
    • 0026728743 scopus 로고
    • Recombinant human basic fibroblast growth factor (Rh-bFGF) in three different wound models in rabbits: Corneal wound healing effect and pharmacology
    • Rieck P, Assouline M, Savoldelli M, et al. Recombinant human basic fibroblast growth factor (Rh-bFGF) in three different wound models in rabbits: corneal wound healing effect and pharmacology. Exp Eye Res. 1992;54:987-998.
    • (1992) Exp Eye Res , vol.54 , pp. 987-998
    • Rieck, P.1    Assouline, M.2    Savoldelli, M.3
  • 42
    • 0028567793 scopus 로고
    • Effect of epidermal growth factor, hepatocyte growth factor, and keratinocyte growth factor on proliferation, motility and differentiation of human corneal epithelial cells
    • Wilson SE, He YG, Weng J, Zieske JD, Jester JV, Schultz GS. Effect of epidermal growth factor, hepatocyte growth factor, and keratinocyte growth factor on proliferation, motility and differentiation of human corneal epithelial cells. Exp Eye Res. 1994;59:665-678.
    • (1994) Exp Eye Res , vol.59 , pp. 665-678
    • Wilson, S.E.1    He, Y.G.2    Weng, J.3    Zieske, J.D.4    Jester, J.V.5    Schultz, G.S.6
  • 43
    • 0030926967 scopus 로고    scopus 로고
    • Epidermal growth factor stimulation of phosphatidylinositol 3-kinase during wound closure in rabbit corneal epithelial cells
    • Zhang Y, Akhtar RA. Epidermal growth factor stimulation of phosphatidylinositol 3-kinase during wound closure in rabbit corneal epithelial cells. Invest Ophthalmol Vis Sci. 1997;38:1139-1148.
    • (1997) Invest Ophthalmol Vis Sci , vol.38 , pp. 1139-1148
    • Zhang, Y.1    Akhtar, R.A.2
  • 44
    • 0023146946 scopus 로고
    • Migrating keratinocytes express urokinase-type plasminogen activator
    • Morioka S, Lazarus GS, Baird JL, Jensen PJ. Migrating keratinocytes express urokinase-type plasminogen activator. J Invest Dermatol. 1987;88:418-423.
    • (1987) J Invest Dermatol , vol.88 , pp. 418-423
    • Morioka, S.1    Lazarus, G.S.2    Baird, J.L.3    Jensen, P.J.4
  • 45
    • 0034705424 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator stimulates the Ras/extracellular signal-regulated kinase (ERK) signaling pathway and MCF-7 cell migration by a mechanism that requires focal adhesion kinase, Src, and Shc: Rapid dissociation of GRB2/Sps-Shc complex is associated with the transient phosphorylation of ERK in urokinase-treated cells
    • Nguyen DH, Webb DJ, Catling AD, et al. Urokinase-type plasminogen activator stimulates the Ras/extracellular signal-regulated kinase (ERK) signaling pathway and MCF-7 cell migration by a mechanism that requires focal adhesion kinase, Src, and Shc: rapid dissociation of GRB2/Sps-Shc complex is associated with the transient phosphorylation of ERK in urokinase-treated cells. J Biol Chem. 2000;275:19382-19388.
    • (2000) J Biol Chem , vol.275 , pp. 19382-19388
    • Nguyen, D.H.1    Webb, D.J.2    Catling, A.D.3
  • 46
    • 0037023720 scopus 로고    scopus 로고
    • Cooperativity between the Ras-ERK and Rho-Rho kinase pathways in urokinasetype plasminogen activator-stimulated cell migration
    • Jo M, Thomas KS, Somlyo AV, Somlyo AP, Gonias SL. Cooperativity between the Ras-ERK and Rho-Rho kinase pathways in urokinasetype plasminogen activator-stimulated cell migration. J Biol Chem. 2002;277:12479-12485.
    • (2002) J Biol Chem , vol.277 , pp. 12479-12485
    • Jo, M.1    Thomas, K.S.2    Somlyo, A.V.3    Somlyo, A.P.4    Gonias, S.L.5
  • 47
    • 0025125427 scopus 로고
    • An enzyme-linked immunosorbent assay system for quantitative determination of calphobindin I, a new placental anticoagulant protein, and its application to various specimens
    • Nakao H, Nagoya T, Iwasaki A, et al. An enzyme-linked immunosorbent assay system for quantitative determination of calphobindin I, a new placental anticoagulant protein, and its application to various specimens. Chem Pharm Bull. 1990;38:1957-1960.
    • (1990) Chem Pharm Bull , vol.38 , pp. 1957-1960
    • Nakao, H.1    Nagoya, T.2    Iwasaki, A.3
  • 48
    • 0037372244 scopus 로고    scopus 로고
    • Evidence for a role of the adenosine 5́-triphosphate-binding cassette transporter A1 in the externalization of annexin I from pituitary folliculo-stellate cells
    • Chapman LP, Epton MJ, Buckingham JC, Morris JF, Christian HC. Evidence for a role of the adenosine 5́-triphosphate-binding cassette transporter A1 in the externalization of annexin I from pituitary folliculo-stellate cells. Endocrinology. 2003;144:1062-1073.
    • (2003) Endocrinology , vol.144 , pp. 1062-1073
    • Chapman, L.P.1    Epton, M.J.2    Buckingham, J.C.3    Morris, J.F.4    Christian, H.C.5
  • 49
    • 0037821650 scopus 로고    scopus 로고
    • Thrombin induces endothelial cell-surface exposure of the plasminogen receptor annexin 2
    • Peterson EA, Sutherland MR, Nesheim ME, Pryzdial EL. Thrombin induces endothelial cell-surface exposure of the plasminogen receptor annexin 2. J Cell Sci. 2003;116:2399-2408.
    • (2003) J Cell Sci , vol.116 , pp. 2399-2408
    • Peterson, E.A.1    Sutherland, M.R.2    Nesheim, M.E.3    Pryzdial, E.L.4
  • 50
    • 0347481133 scopus 로고    scopus 로고
    • Nonclassical secretion of annexin A2 to the lumenal side of the enterocyte brush border membrane
    • Danielsen EM, van Deurs B, Hansen GH. "Nonclassical" secretion of annexin A2 to the lumenal side of the enterocyte brush border membrane. Biochemistry. 2003;42:14670-14676.
    • (2003) Biochemistry , vol.42 , pp. 14670-14676
    • Danielsen, E.M.1    van Deurs, B.2    Hansen, G.H.3
  • 51
    • 3242877433 scopus 로고    scopus 로고
    • Annexins: Unique membrane binding proteins with diverse functions
    • Rescher U, Gerke V. Annexins: unique membrane binding proteins with diverse functions. J Cell Sci. 2004;117:2631-2639.
    • (2004) J Cell Sci , vol.117 , pp. 2631-2639
    • Rescher, U.1    Gerke, V.2
  • 52
    • 0029043888 scopus 로고
    • A novel assay for apoptosis: Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V
    • Vermes I, Haanen C, Steffens-Nakken H, Reutelingsperger C. A novel assay for apoptosis: flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V. J Immunol Methods. 1995;184:39-51.
    • (1995) J Immunol Methods , vol.184 , pp. 39-51
    • Vermes, I.1    Haanen, C.2    Steffens-Nakken, H.3    Reutelingsperger, C.4
  • 54
    • 0034142375 scopus 로고    scopus 로고
    • Annexin V binds to viable B cells and colocalizes with a marker of lipid rafts upon B cell receptor activation
    • Dillon SR, Mancini M, Rosen A, Schlissel MS. Annexin V binds to viable B cells and colocalizes with a marker of lipid rafts upon B cell receptor activation. J Immunol. 2000;164:1322-1332.
    • (2000) J Immunol , vol.164 , pp. 1322-1332
    • Dillon, S.R.1    Mancini, M.2    Rosen, A.3    Schlissel, M.S.4
  • 56
    • 3142757912 scopus 로고    scopus 로고
    • Secretion of intracellular IL-1 receptor antagonist (type 1) is dependent on P2X7 receptor activation
    • Wilson HL, Francis SE, Dower SK, Crossman DC. Secretion of intracellular IL-1 receptor antagonist (type 1) is dependent on P2X7 receptor activation. J Immunol. 2004;173:1202-1208.
    • (2004) J Immunol , vol.173 , pp. 1202-1208
    • Wilson, H.L.1    Francis, S.E.2    Dower, S.K.3    Crossman, D.C.4


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