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Volumn 289, Issue 19, 2014, Pages 13419-13433

Fibulin 2, a tyrosine O-sulfated protein, is up-regulated following retinal detachment

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; EYE PROTECTION;

EID: 84900437907     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.562157     Document Type: Article
Times cited : (11)

References (79)
  • 2
    • 84859994414 scopus 로고    scopus 로고
    • Comparative analysis of the basement membrane composition of the human limbus epithelium and amniotic membrane epithelium
    • Dietrich-Ntoukas, T., Hofmann-Rummelt, C., Kruse, F. E., and Schlötzer-Schrehardt, U. (2012) Comparative analysis of the basement membrane composition of the human limbus epithelium and amniotic membrane epithelium. Cornea 31, 564-569
    • (2012) Cornea , vol.31 , pp. 564-569
    • Dietrich-Ntoukas, T.1    Hofmann-Rummelt, C.2    Kruse, F.E.3    Schlötzer- Schrehardt, U.4
  • 3
    • 0031956936 scopus 로고    scopus 로고
    • Developmental changes in the basement membrane of the normal and hypothyroid postnatal rat testis: Segmental localization of fibulin-2 and fibronectin
    • Loveland, K., Schlatt, S., Sasaki, T., Chu, M. L., Timpl, R., and Dziadek, M. (1998) Developmental changes in the basement membrane of the normal and hypothyroid postnatal rat testis: segmental localization of fibulin-2 and fibronectin. Biol. Reprod. 58, 1123-1130
    • (1998) Biol. Reprod. , vol.58 , pp. 1123-1130
    • Loveland, K.1    Schlatt, S.2    Sasaki, T.3    Chu, M.L.4    Timpl, R.5    Dziadek, M.6
  • 4
    • 0029932657 scopus 로고    scopus 로고
    • The extracellular matrix proteins fibulin-1 and fibulin-2 in the early human embryo
    • Miosge, N., Götz, W., Sasaki, T., Chu, M. L., Timpl, R., and Herken, R. (1996) The extracellular matrix proteins fibulin-1 and fibulin-2 in the early human embryo. Histochem. J. 28, 109-116
    • (1996) Histochem. J. , vol.28 , pp. 109-116
    • Miosge, N.1    Götz, W.2    Sasaki, T.3    Chu, M.L.4    Timpl, R.5    Herken, R.6
  • 5
    • 0034798690 scopus 로고    scopus 로고
    • Increased deposition of fibulin-2 in solar elastosis and its colocalization with elastic fibres
    • Hunzelmann, N., Nischt, R., Brenneisen, P., Eickert, A., and Krieg, T. (2001) Increased deposition of fibulin-2 in solar elastosis and its colocalization with elastic fibres. Br. J. Dermatol. 145, 217-222
    • (2001) Br. J. Dermatol. , vol.145 , pp. 217-222
    • Hunzelmann, N.1    Nischt, R.2    Brenneisen, P.3    Eickert, A.4    Krieg, T.5
  • 6
    • 72449168333 scopus 로고    scopus 로고
    • Fibulin-5, an integrin-binding matricellular protein: Its function in development and disease
    • Yanagisawa, H., Schluterman, M. K., and Brekken, R. A. (2009) Fibulin-5, an integrin-binding matricellular protein: its function in development and disease. J. Cell Commun. Signal. 3, 337-347
    • (2009) J. Cell Commun. Signal. , vol.3 , pp. 337-347
    • Yanagisawa, H.1    Schluterman, M.K.2    Brekken, R.A.3
  • 7
    • 69949132246 scopus 로고    scopus 로고
    • Fibulins: Multiple roles in matrix structures and tissue functions
    • De Vega, S., Iwamoto, T., and Yamada, Y. (2009) Fibulins: multiple roles in matrix structures and tissue functions. Cell. Mol. Life Sci. 66, 1890-1902
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1890-1902
    • De Vega, S.1    Iwamoto, T.2    Yamada, Y.3
  • 15
    • 80052827057 scopus 로고    scopus 로고
    • KSHV regulation of fibulin-2 in Kaposi's sarcoma: Implications for tumorigenesis
    • Alcendor, D. J., Knobel, S., Desai, P., Zhu, W. Q., and Hayward, G. S. (2011) KSHV regulation of fibulin-2 in Kaposi's sarcoma: implications for tumorigenesis. Am. J. Pathol. 179, 1443-1454
    • (2011) Am. J. Pathol. , vol.179 , pp. 1443-1454
    • Alcendor, D.J.1    Knobel, S.2    Desai, P.3    Zhu, W.Q.4    Hayward, G.S.5
  • 16
    • 34250815728 scopus 로고    scopus 로고
    • Loss of fibulin-2 expression is associated with breast cancer progression
    • Yi, C. H., Smith, D. J., West, W. W., and Hollingsworth, M. A. (2007) Loss of fibulin-2 expression is associated with breast cancer progression. Am. J. Pathol. 170, 1535-1545
    • (2007) Am. J. Pathol. , vol.170 , pp. 1535-1545
    • Yi, C.H.1    Smith, D.J.2    West, W.W.3    Hollingsworth, M.A.4
  • 20
    • 34047195173 scopus 로고    scopus 로고
    • Case-control genetic association study of fibulin-6 (FBLN6 or HMCN1) variants in age-related macular degeneration (AMD)
    • Fisher, S. A., Rivera, A., Fritsche, L. G., Keilhauer, C. N., Lichtner, P., Meitinger, T., Rudolph, G., and Weber, B. H. (2007) Case-control genetic association study of fibulin-6 (FBLN6 or HMCN1) variants in age-related macular degeneration (AMD). Hum. Mutat. 28, 406-413
    • (2007) Hum. Mutat. , vol.28 , pp. 406-413
    • Fisher, S.A.1    Rivera, A.2    Fritsche, L.G.3    Keilhauer, C.N.4    Lichtner, P.5    Meitinger, T.6    Rudolph, G.7    Weber, B.H.8
  • 22
    • 34548070301 scopus 로고    scopus 로고
    • Global changes in optic nerve head gene expression after exposure to elevated intraocular pressure in a rat glaucoma model
    • Johnson, E. C., Jia, L., Cepurna, W. O., Doser, T. A., and Morrison, J. C. (2007) Global changes in optic nerve head gene expression after exposure to elevated intraocular pressure in a rat glaucoma model. Invest. Ophthalmol. Vis. Sci. 48, 3161-3177
    • (2007) Invest. Ophthalmol. Vis. Sci. , vol.48 , pp. 3161-3177
    • Johnson, E.C.1    Jia, L.2    Cepurna, W.O.3    Doser, T.A.4    Morrison, J.C.5
  • 23
    • 0027380642 scopus 로고
    • Structure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium binding
    • Pan, T. C., Sasaki, T., Zhang, R. Z., Fässler, R., Timpl, R., and Chu, M. L. (1993) Structure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium binding. J. Cell Biol. 123, 1269-1277
    • (1993) J. Cell Biol. , vol.123 , pp. 1269-1277
    • Pan, T.C.1    Sasaki, T.2    Zhang, R.Z.3    Fässler, R.4    Timpl, R.5    Chu, M.L.6
  • 24
    • 33845998556 scopus 로고    scopus 로고
    • Detection and purification of tyrosine-sulfated proteins using a novel anti-sulfotyrosine monoclonal antibody
    • Hoffhines, A. J., Damoc, E., Bridges, K. G., Leary, J. A., and Moore, K. L. (2006) Detection and purification of tyrosine-sulfated proteins using a novel anti-sulfotyrosine monoclonal antibody. J. Biol. Chem. 281, 37877-37887
    • (2006) J. Biol. Chem. , vol.281 , pp. 37877-37887
    • Hoffhines, A.J.1    Damoc, E.2    Bridges, K.G.3    Leary, J.A.4    Moore, K.L.5
  • 25
    • 59149084410 scopus 로고    scopus 로고
    • Tyrosylprotein sulfotransferase-2 expression is required for sulfation of RNase 9 and Mfge8 in vivo
    • Hoffhines, A. J., Jen, C. H., Leary, J. A., and Moore, K. L. (2009) Tyrosylprotein sulfotransferase-2 expression is required for sulfation of RNase 9 and Mfge8 in vivo. J. Biol. Chem. 284, 3096-3105
    • (2009) J. Biol. Chem. , vol.284 , pp. 3096-3105
    • Hoffhines, A.J.1    Jen, C.H.2    Leary, J.A.3    Moore, K.L.4
  • 26
    • 1542742250 scopus 로고    scopus 로고
    • Expression of cone-photoreceptor-specific antigens in a cell line derived from retinal tumors in transgenic mice
    • Tan, E., Ding, X. Q., Saadi, A., Agarwal, N., Naash, M. I., and Al-Ubaidi, M. R. (2004) Expression of cone-photoreceptor-specific antigens in a cell line derived from retinal tumors in transgenic mice. Invest. Ophthalmol. Vis. Sci. 45, 764-768
    • (2004) Invest. Ophthalmol. Vis. Sci. , vol.45 , pp. 764-768
    • Tan, E.1    Ding, X.Q.2    Saadi, A.3    Agarwal, N.4    Naash, M.I.5    Al-Ubaidi, M.R.6
  • 27
    • 0029872876 scopus 로고    scopus 로고
    • ARPE-19, a human retinal pigment epithelial cell line with differentiated properties
    • Dunn, K. C., Aotaki-Keen, A. E., Putkey, F. R., and Hjelmeland, L. M. (1996) ARPE-19, a human retinal pigment epithelial cell line with differentiated properties. Exp. Eye Res. 62, 155-169
    • (1996) Exp. Eye Res. , vol.62 , pp. 155-169
    • Dunn, K.C.1    Aotaki-Keen, A.E.2    Putkey, F.R.3    Hjelmeland, L.M.4
  • 28
    • 0036618178 scopus 로고    scopus 로고
    • Preferential transformation of human neuronal cells by human adenoviruses and the origin of HEK293 cells
    • Shaw, G., Morse, S., Ararat, M., and Graham, F. L. (2002) Preferential transformation of human neuronal cells by human adenoviruses and the origin of HEK293 cells. FASEB J. 16, 869-871
    • (2002) FASEB J. , vol.16 , pp. 869-871
    • Shaw, G.1    Morse, S.2    Ararat, M.3    Graham, F.L.4
  • 29
    • 0023711798 scopus 로고
    • Calcium phosphate-mediated gene transfer: A highly efficient transfection system for stably transforming cells with plasmid DNA
    • Chen, C. A., and Okayama, H. (1988) Calcium phosphate-mediated gene transfer: a highly efficient transfection system for stably transforming cells with plasmid DNA. BioTechniques 6, 632-638
    • (1988) BioTechniques , vol.6 , pp. 632-638
    • Chen, C.A.1    Okayama, H.2
  • 30
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C., and Okayama, H. (1987) High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7, 2745-2752
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 32
    • 0030447865 scopus 로고    scopus 로고
    • Expression of fibulin-2 by fibroblasts and deposition with fibronectin into a fibrillar matrix
    • Sasaki, T., Wiedemann, H., Matzner, M., Chu, M. L., and Timpl, R. (1996) Expression of fibulin-2 by fibroblasts and deposition with fibronectin into a fibrillar matrix. J. Cell Sci. 109, 2895-2904
    • (1996) J. Cell Sci. , vol.109 , pp. 2895-2904
    • Sasaki, T.1    Wiedemann, H.2    Matzner, M.3    Chu, M.L.4    Timpl, R.5
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 34848820048 scopus 로고    scopus 로고
    • Formation and progression of sub-retinal pigment epithelium deposits in Efemp1 mutation knock-in mice: A model for the early pathogenic course of macular degeneration
    • Marmorstein, L. Y., McLaughlin, P. J., Peachey, N. S., Sasaki, T., and Marmorstein, A. D. (2007) Formation and progression of sub-retinal pigment epithelium deposits in Efemp1 mutation knock-in mice: a model for the early pathogenic course of macular degeneration. Hum. Mol. Genet. 16, 2423-2432
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 2423-2432
    • Marmorstein, L.Y.1    McLaughlin, P.J.2    Peachey, N.S.3    Sasaki, T.4    Marmorstein, A.D.5
  • 37
    • 39649109883 scopus 로고    scopus 로고
    • Early postnatal pulmonary failure and primary hypothyroidism in mice with combined TPST-1 and TPST-2 deficiency
    • Westmuckett, A. D., Hoffhines, A. J., Borghei, A., and Moore, K. L. (2008) Early postnatal pulmonary failure and primary hypothyroidism in mice with combined TPST-1 and TPST-2 deficiency. Gen. Comp. Endocrinol. 156, 145-153
    • (2008) Gen. Comp. Endocrinol. , vol.156 , pp. 145-153
    • Westmuckett, A.D.1    Hoffhines, A.J.2    Borghei, A.3    Moore, K.L.4
  • 38
    • 0141430039 scopus 로고    scopus 로고
    • P2Y (2) receptor agonist INS37217 enhances functional recovery after detachment caused by subretinal injection in normal and rds mice
    • Nour, M., Quiambao, A. B., Peterson, W. M., Al-Ubaidi, M. R., and Naash, M. I. (2003) P2Y (2) receptor agonist INS37217 enhances functional recovery after detachment caused by subretinal injection in normal and rds mice. Invest. Ophthalmol. Vis. Sci. 44, 4505-4514
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 4505-4514
    • Nour, M.1    Quiambao, A.B.2    Peterson, W.M.3    Al-Ubaidi, M.R.4    Naash, M.I.5
  • 39
    • 0027074996 scopus 로고
    • Bilateral retinal and brain tumors in transgenic mice expressing simian virus 40 large T antigen under control of the human interphotoreceptor retinoid-binding protein promoter
    • Al-Ubaidi, M. R., Font, R. L., Quiambao, A. B., Keener, M. J., Liou, G. I., Overbeek, P. A., and Baehr, W. (1992) Bilateral retinal and brain tumors in transgenic mice expressing simian virus 40 large T antigen under control of the human interphotoreceptor retinoid-binding protein promoter. J. Cell Biol. 119, 1681-1687
    • (1992) J. Cell Biol. , vol.119 , pp. 1681-1687
    • Al-Ubaidi, M.R.1    Font, R.L.2    Quiambao, A.B.3    Keener, M.J.4    Liou, G.I.5    Overbeek, P.A.6    Baehr, W.7
  • 40
    • 0036088377 scopus 로고    scopus 로고
    • The Sulfinator: Predicting tyrosine sulfation sites in protein sequences
    • Monigatti, F., Gasteiger, E., Bairoch, A., and Jung, E. (2002) The Sulfinator: predicting tyrosine sulfation sites in protein sequences. Bioinformatics 18, 769-770
    • (2002) Bioinformatics , vol.18 , pp. 769-770
    • Monigatti, F.1    Gasteiger, E.2    Bairoch, A.3    Jung, E.4
  • 41
    • 84856204941 scopus 로고    scopus 로고
    • Modifications of glycans: Biological significance and therapeutic opportunities
    • Muthana, S. M., Campbell, C. T., and Gildersleeve, J. C. (2012) Modifications of glycans: biological significance and therapeutic opportunities. ACS Chem. Biol. 7, 31-43
    • (2012) ACS Chem. Biol. , vol.7 , pp. 31-43
    • Muthana, S.M.1    Campbell, C.T.2    Gildersleeve, J.C.3
  • 42
    • 0021118791 scopus 로고
    • Determination and occurrence of tyrosine O-sulfate in proteins
    • Huttner, W. B. (1984) Determination and occurrence of tyrosine O-sulfate in proteins. Methods Enzymol. 107, 200-223
    • (1984) Methods Enzymol. , vol.107 , pp. 200-223
    • Huttner, W.B.1
  • 43
    • 0041589205 scopus 로고    scopus 로고
    • The biology and enzymology of protein tyrosine Osulfation
    • Moore, K. L. (2003) The biology and enzymology of protein tyrosine Osulfation. J. Biol. Chem. 278, 24243-24246
    • (2003) J. Biol. Chem. , vol.278 , pp. 24243-24246
    • Moore, K.L.1
  • 44
    • 31344444357 scopus 로고    scopus 로고
    • Fibulin-2 is present in murine vascular lesions and is important for smooth muscle cell migration
    • Ström, A., Olin, A. I., Aspberg, A., and Hultgårdh-Nilsson, A. (2006) Fibulin-2 is present in murine vascular lesions and is important for smooth muscle cell migration. Cardiovasc. Res. 69, 755-763
    • (2006) Cardiovasc. Res. , vol.69 , pp. 755-763
    • Ström, A.1    Olin, A.I.2    Aspberg, A.3    Hultgårdh-Nilsson, A.4
  • 45
    • 0036142782 scopus 로고    scopus 로고
    • The α (1) β (1) and α (2) β (1) integrins provide critical support for vascular endothelial growth factor signaling, endothelial cell migration, and tumor angiogenesis
    • Senger, D. R., Perruzzi, C. A., Streit, M., Koteliansky, V. E., De Fougerolles, A. R., and Detmar, M. (2002) The α (1) β (1) and α (2) β (1) integrins provide critical support for vascular endothelial growth factor signaling, endothelial cell migration, and tumor angiogenesis. Am. J. Pathol. 160, 195-204
    • (2002) Am. J. Pathol. , vol.160 , pp. 195-204
    • Senger, D.R.1    Perruzzi, C.A.2    Streit, M.3    Koteliansky, V.E.4    De Fougerolles, A.R.5    Detmar, M.6
  • 48
    • 0029087888 scopus 로고
    • Integrin-binding and cell-Adhesion studies of fibulins reveal a particular affinity for αIIbβ3
    • Pfaff, M., Sasaki, T., Tangemann, K., Chu, M. L., and Timpl, R. (1995) Integrin-binding and cell-Adhesion studies of fibulins reveal a particular affinity for αIIbβ3. Exp. Cell Res. 219, 87-92
    • (1995) Exp. Cell Res. , vol.219 , pp. 87-92
    • Pfaff, M.1    Sasaki, T.2    Tangemann, K.3    Chu, M.L.4    Timpl, R.5
  • 49
    • 0036956659 scopus 로고    scopus 로고
    • Long-term effects of shortterm retinal bleb detachments in rabbits
    • Ivert, L., Kjeldbye, H., and Gouras, P. (2002) Long-term effects of shortterm retinal bleb detachments in rabbits. Graefes Arch. Clin. Exp. Ophthalmol. 240, 232-237
    • (2002) Graefes Arch. Clin. Exp. Ophthalmol. , vol.240 , pp. 232-237
    • Ivert, L.1    Kjeldbye, H.2    Gouras, P.3
  • 50
    • 0024535753 scopus 로고
    • Subretinal fluid stimulation of retinal pigment epithelial cell migration and proliferation is dependent on certain features of the detachment or its treatment
    • Hackett, S. F., Conway, B. P., and Campochiaro, P. A. (1989) Subretinal fluid stimulation of retinal pigment epithelial cell migration and proliferation is dependent on certain features of the detachment or its treatment. Arch. Ophthalmol. 107, 391-394
    • (1989) Arch. Ophthalmol. , vol.107 , pp. 391-394
    • Hackett, S.F.1    Conway, B.P.2    Campochiaro, P.A.3
  • 51
    • 84857796528 scopus 로고    scopus 로고
    • Protein markers and differentiation in culture for Schlemm's canal endothelial cells
    • Perkumas, K. M., and Stamer, W. D. (2012) Protein markers and differentiation in culture for Schlemm's canal endothelial cells. Exp. Eye Res. 96, 82-87
    • (2012) Exp. Eye Res. , vol.96 , pp. 82-87
    • Perkumas, K.M.1    Stamer, W.D.2
  • 52
  • 54
    • 77956038457 scopus 로고    scopus 로고
    • Tyrosylprotein sulfotransferase regulates collagen secretion in Caenorhabditis elegans
    • Kim, T. H., Kim Do, H., Nam, H. W., Park, S. Y., Shim, J., and Cho, J. W. (2010) Tyrosylprotein sulfotransferase regulates collagen secretion in Caenorhabditis elegans. Mol. Cells 29, 413-418
    • (2010) Mol. Cells , vol.29 , pp. 413-418
    • Kim, T.H.1    Kim Do, H.2    Nam, H.W.3    Park, S.Y.4    Shim, J.5    Cho, J.W.6
  • 55
    • 0023685933 scopus 로고
    • Inhibition of tyrosine sulfation in the trans-Golgi retards the transport of a constitutively secreted protein to the cell surface
    • Friederich, E., Fritz, H. J., and Huttner, W. B. (1988) Inhibition of tyrosine sulfation in the trans-Golgi retards the transport of a constitutively secreted protein to the cell surface. J. Cell Biol. 107, 1655-1667
    • (1988) J. Cell Biol. , vol.107 , pp. 1655-1667
    • Friederich, E.1    Fritz, H.J.2    Huttner, W.B.3
  • 56
    • 0017831892 scopus 로고
    • Glycosaminoglycans and their binding to biological macromolecules
    • Lindahl, U., and Höök, M. (1978) Glycosaminoglycans and their binding to biological macromolecules. Annu. Rev. Biochem. 47, 385-417
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 385-417
    • Lindahl, U.1    Höök, M.2
  • 58
    • 33745439051 scopus 로고    scopus 로고
    • Heparin/heparan sulphate binding in the TGF-β cytokine superfamily
    • Rider, C. C. (2006) Heparin/heparan sulphate binding in the TGF-β cytokine superfamily. Biochem. Soc. Trans. 34, 458-460
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 458-460
    • Rider, C.C.1
  • 59
    • 84877025513 scopus 로고    scopus 로고
    • The effect of desulfation of chondroitin sulfate on interactions with positively charged growth factors and upregulation of cartilaginous markers in encapsulated MSCs
    • Lim, J. J., and Temenoff, J. S. (2013) The effect of desulfation of chondroitin sulfate on interactions with positively charged growth factors and upregulation of cartilaginous markers in encapsulated MSCs. Biomaterials 34, 5007-5018
    • (2013) Biomaterials , vol.34 , pp. 5007-5018
    • Lim, J.J.1    Temenoff, J.S.2
  • 60
    • 0029584361 scopus 로고
    • Binding of mouse and human fibulin-2 to extracellular matrix ligands
    • Sasaki, T., Göhring, W., Pan, T. C., Chu, M. L., and Timpl, R. (1995) Binding of mouse and human fibulin-2 to extracellular matrix ligands. J. Mol. Biol. 254, 892-899
    • (1995) J. Mol. Biol. , vol.254 , pp. 892-899
    • Sasaki, T.1    Göhring, W.2    Pan, T.C.3    Chu, M.L.4    Timpl, R.5
  • 61
    • 0033082328 scopus 로고    scopus 로고
    • Recombinant domain IV of perlecan binds to nidogens, laminin-nidogen complex, fibronectin, fibulin-2 and heparin
    • Hopf, M., Göhring, W., Kohfeldt, E., Yamada, Y., and Timpl, R. (1999) Recombinant domain IV of perlecan binds to nidogens, laminin-nidogen complex, fibronectin, fibulin-2 and heparin. Eur. J. Biochem. 259, 917-925
    • (1999) Eur. J. Biochem. , vol.259 , pp. 917-925
    • Hopf, M.1    Göhring, W.2    Kohfeldt, E.3    Yamada, Y.4    Timpl, R.5
  • 62
    • 0031020164 scopus 로고    scopus 로고
    • Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences
    • Utani, A., Nomizu, M., and Yamada, Y. (1997) Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences. J. Biol. Chem. 272, 2814-2820
    • (1997) J. Biol. Chem. , vol.272 , pp. 2814-2820
    • Utani, A.1    Nomizu, M.2    Yamada, Y.3
  • 63
    • 0036405396 scopus 로고    scopus 로고
    • Binding of mouse nidogen-2 to basement membrane components and cells and its expression in embryonic and adult tissues suggest complementary functions of the two nidogens
    • Salmivirta, K., Talts, J. F., Olsson, M., Sasaki, T., Timpl, R., and Ekblom, P. (2002) Binding of mouse nidogen-2 to basement membrane components and cells and its expression in embryonic and adult tissues suggest complementary functions of the two nidogens. Exp. Cell Res. 279, 188-201
    • (2002) Exp. Cell Res. , vol.279 , pp. 188-201
    • Salmivirta, K.1    Talts, J.F.2    Olsson, M.3    Sasaki, T.4    Timpl, R.5    Ekblom, P.6
  • 64
    • 0035847046 scopus 로고    scopus 로고
    • The proteoglycans aggrecan and Versican form networks with fibulin-2 through their lectin domain binding
    • Olin, A. I., Mörgelin, M., Sasaki, T., Timpl, R., Heinegård, D., and Aspberg, A. (2001) The proteoglycans aggrecan and Versican form networks with fibulin-2 through their lectin domain binding. J. Biol. Chem. 276, 1253-1261
    • (2001) J. Biol. Chem. , vol.276 , pp. 1253-1261
    • Olin, A.I.1    Mörgelin, M.2    Sasaki, T.3    Timpl, R.4    Heinegård, D.5    Aspberg, A.6
  • 65
    • 0034816999 scopus 로고    scopus 로고
    • Tyrosine sulfation enhances but is not required for PSGL-1 rolling adhesion on P-selectin
    • Rodgers, S. D., Camphausen, R. T., and Hammer, D. A. (2001) Tyrosine sulfation enhances but is not required for PSGL-1 rolling adhesion on P-selectin. Biophys. J. 81, 2001-2009
    • (2001) Biophys. J. , vol.81 , pp. 2001-2009
    • Rodgers, S.D.1    Camphausen, R.T.2    Hammer, D.A.3
  • 66
    • 0033598750 scopus 로고    scopus 로고
    • Tyrosine replacement in P-selectin glycoprotein ligand-1 affects distinct kinetic and mechanical properties of bonds with P- and L-selectin
    • Ramachandran, V., Nollert, M. U., Qiu, H., Liu, W. J., Cummings, R. D., Zhu, C., and McEver, R. P. (1999) Tyrosine replacement in P-selectin glycoprotein ligand-1 affects distinct kinetic and mechanical properties of bonds with P- and L-selectin. Proc. Natl. Acad. Sci. U. S. A. 96, 13771-13776
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13771-13776
    • Ramachandran, V.1    Nollert, M.U.2    Qiu, H.3    Liu, W.J.4    Cummings, R.D.5    Zhu, C.6    McEver, R.P.7
  • 67
    • 0025924755 scopus 로고
    • Sulfation of Tyr1680 of human blood coagulation factor VIII is essential for the interaction of factor VIII with von Willebrand factor
    • Leyte, A., Van Schijndel, H. B., Niehrs, C., Huttner, W. B., Verbeet, M. P., Mertens, K., and Van Mourik, J. A. (1991) Sulfation of Tyr1680 of human blood coagulation factor VIII is essential for the interaction of factor VIII with von Willebrand factor. J. Biol. Chem. 266, 740-746
    • (1991) J. Biol. Chem. , vol.266 , pp. 740-746
    • Leyte, A.1    Van Schijndel, H.B.2    Niehrs, C.3    Huttner, W.B.4    Verbeet, M.P.5    Mertens, K.6    Van Mourik, J.A.7
  • 68
  • 69
    • 44849094851 scopus 로고    scopus 로고
    • Management of retinal detachment: A guide for non-ophthalmologists
    • Kang, H. K., and Luff, A. J. (2008) Management of retinal detachment: a guide for non-ophthalmologists. BMJ 336, 1235-1240
    • (2008) BMJ , vol.336 , pp. 1235-1240
    • Kang, H.K.1    Luff, A.J.2
  • 70
    • 2442457890 scopus 로고    scopus 로고
    • Northern New Zealand Rhegmatogenous Retinal Detachment Study: Epidemiology and risk factors
    • Polkinghorne, P. J., and Craig, J. P. (2004) Northern New Zealand Rhegmatogenous Retinal Detachment Study: epidemiology and risk factors. Clin. Experiment. Ophthalmol. 32, 159-163
    • (2004) Clin. Experiment. Ophthalmol. , vol.32 , pp. 159-163
    • Polkinghorne, P.J.1    Craig, J.P.2
  • 71
    • 24944453158 scopus 로고    scopus 로고
    • Genetic risk of rhegmatogenous retinal detachment: A familial aggregation study
    • Go, S. L., Hoyng, C. B., and Klaver, C. C. (2005) Genetic risk of rhegmatogenous retinal detachment: a familial aggregation study. Arch. Ophthalmol. 123, 1237-1241
    • (2005) Arch. Ophthalmol. , vol.123 , pp. 1237-1241
    • Go, S.L.1    Hoyng, C.B.2    Klaver, C.C.3
  • 72
    • 43449135315 scopus 로고    scopus 로고
    • Glutamate accelerates RPE cell proliferation through ERK1/2 activation via distinct receptorspecific mechanisms
    • García, S., López, E., and López-Colomé, A. M. (2008) Glutamate accelerates RPE cell proliferation through ERK1/2 activation via distinct receptorspecific mechanisms. J. Cell Biochem. 104, 377-390
    • (2008) J. Cell Biochem. , vol.104 , pp. 377-390
    • García, S.1    López, E.2    López-Colomé, A.M.3
  • 74
    • 0023029370 scopus 로고
    • Acute changes in RPE apical morphology after retinal detachment in rabbit. A SEM study
    • Immel, J., Negi, A., and Marmor, M. F. (1986) Acute changes in RPE apical morphology after retinal detachment in rabbit. A SEM study. Invest. Ophthalmol. Vis. Sci. 27, 1770-1776
    • (1986) Invest. Ophthalmol. Vis. Sci. , vol.27 , pp. 1770-1776
    • Immel, J.1    Negi, A.2    Marmor, M.F.3
  • 75
    • 84860658474 scopus 로고    scopus 로고
    • A novel experimental mouse model of retinal detachment: Complete functional and histologic recovery of the retina
    • Zeng, R., Zhang, Y., Shi, F., and Kong, F. (2012) A novel experimental mouse model of retinal detachment: complete functional and histologic recovery of the retina. Invest. Ophthalmol. Vis. Sci. 53, 1685-1695
    • (2012) Invest. Ophthalmol. Vis. Sci. , vol.53 , pp. 1685-1695
    • Zeng, R.1    Zhang, Y.2    Shi, F.3    Kong, F.4
  • 77
    • 0025307563 scopus 로고
    • Retinotoxicity of 1, 4, -bis (4-Aminophenoxy) - 2-phenylbenzene (2-phenyl-APB-144) in albino and pigmented rats
    • Lee, K. P., and Valentine, R. (1990) Retinotoxicity of 1, 4, -bis (4-Aminophenoxy) - 2-phenylbenzene (2-phenyl-APB-144) in albino and pigmented rats. Arch. Toxicol. 64, 135-142
    • (1990) Arch. Toxicol. , vol.64 , pp. 135-142
    • Lee, K.P.1    Valentine, R.2
  • 79
    • 0032841562 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transition in proliferative vitreoretinopathy: Intermediate filament protein expression in retinal pigment epithelial cells
    • Casaroli-Marano, R. P., Pagan, R., and Vilaró, S. (1999) Epithelial-mesenchymal transition in proliferative vitreoretinopathy: intermediate filament protein expression in retinal pigment epithelial cells. Invest. Ophthalmol. Vis. Sci. 40, 2062-2072
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40 , pp. 2062-2072
    • Casaroli-Marano, R.P.1    Pagan, R.2    Vilaró, S.3


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